text:
Elizabeth Banks
From Wikipedia, the free encyclopedia
Jump to navigation Jump to search
For the journalist, see Elizabeth Banks (journalist).
Elizabeth Banks
Banks at the 2018 San Diego Comic-Con
Born
Elizabeth Irene Mitchell
(1974-02-10) February 10, 1974 (age 44)
Pittsfield, Massachusetts, U.S.
Alma mater
University of Pennsylvania
American Conservatory Theater
Occupation
Actress
director
model
producer
Years active
1998–present
Spouse(s)
Max Handelman (m. 2003)
Children
2
Website
www.elizabethbanks.com
Elizabeth Irene Banks (née Mitchell;[1][2] born February 10, 1974)[3] is an American actress, director, model and producer. She is known for her starring role as Effie Trinket in The Hunger Games film series (2012–15) and as Gail Abernathy-McKadden in the Pitch Perfect film series (2012–17). She made her directorial debut with Pitch Perfect 2 (2014), whose $69 million opening-weekend gross set a record for a first-time director.[4][5]
Banks made her film debut in the low-budget independent film Surrender Dorothy (1998). She starred in the films Wet Hot American Summer (2001), Sam Raimi's Spider-Man trilogy (2002–2007), Seabiscuit (2003), The 40-Year-Old Virgin (2005), Slither (2006), Zack and Miri Make a Porno (2008), Role Models (2008), The Next Three Days (2010), Man on a Ledge (2012), What to Expect When You're Expecting (2012), The Lego Movie (2014), Love & Mercy (2014), Magic Mike XXL (2015), and Power Rangers (2017).
On television, Banks had a recurring role as Avery Jessup on the NBC sitcom 30 Rock, which garnered her two Primetime Emmy Award nominations. She also had recurring roles on the comedy series Scrubs and Modern Family, the latter of which earned her a Primetime Emmy Award nomination. Banks starred in the Netflix miniseries Wet Hot American Summer: First Day of Camp (2015) and Wet Hot American Summer: Ten Years Later (2017).
As of July 2018[update], Box Office Mojo ranked Banks as the 48th-highest-grossing actor of all time, and the ninth-highest-grossing actress.[6]
Contents
1 Early life
2 Career
3 Personal life
4 Filmography
4.1 Film
4.2 Television
4.3 Music videos
4.4 Video games
5 Awards and nominations
6 References
7 External links
Early life[edit]
Banks was born in Pittsfield, Massachusetts, and grew up on Brown Street, the eldest of four children of Ann (née Wallace) and Mark P. Mitchell.[7] Her father, a Vietnam veteran, was a factory worker for General Electric and her mother worked in a bank.[8] She has said that she grew up "Irish + WASP + Catholic."[9]
Growing up, Banks played baseball and rode horses. She was in Little League when she broke her leg sliding into third base. She then tried out for the school play, which was her start in acting.[10] She graduated from Pittsfield High School in 1992, and is a member of the Massachusetts Junior Classical League.[11] She attended the University of Pennsylvania, where she was a member of the Delta Delta Delta Sorority. She graduated magna cum laude in 1996 with a major in communications and a minor in theater arts.[12] In 1998, she completed schooling at the American Conservatory Theater in San Francisco, California, where she earned an MFA degree.[13][14]
Career[edit]
Banks at the Spider-Man 3 premiere in 2007
Banks changed her name to avoid confusion with actress Elizabeth Mitchell.[15] After auditioning in New York, she was offered a role on the soap opera Santa Barbara. Taking the role would have required her to quit her education at the American Conservatory Theatre, and Banks ultimately decided to forgo the offer due to having taken out student loans to complete her degree.[16] She made her acting debut in the 1998 independent film Surrender Dorothy, as Elizabeth Casey, and appeared in various films over the next seven years including Guy Ritchie's Swept Away[17] before gaining more prominent widespread exposure through the 2005 comedy film The 40-Year-Old Virgin.[18]
In August 2005, at the Williamstown Theatre Festival, Banks starred in William Inge's Bus Stop as Cherie, the sexy blonde aspiring nightclub singer.[19] Jeffrey Borak wrote that Banks' portrayal was acted "with poise, clarity and a shrewd feel for Cherie's complexities. Her performance is all of a piece and in harmony, stylistically, with the performances around her ..."[20] In 2005, she appeared on the series Stella, and in May 2006, she had a role in the season five finale of the NBC sitcom Scrubs as Dr. Kim Briggs, the love interest of J.D. (Zach Braff). The character appeared throughout seasons six, seven, and eight as a recurring guest star.[21]
In 2006, Banks appeared in the American football drama film Invincible, in which she played Mark Wahlberg's love interest. Later, she and co-star Wahlberg were nominated for the "Best Kiss" award at the MTV Movie Awards.[22] That same year, she landed the starring role in the comedy-horror film Slither.[23]
In 2007, Banks played the female lead in the comedy film Meet Bill, alongside Aaron Eckhart and Jessica Alba.[21] That same year, she had a small role in the Christmas comedy film Fred Claus, co-starring Vince Vaughn and Paul Giamatti as Santa's little helper, Charlyne. In 2008, she played the ex-wife and mother of the daughter of Ryan Reynolds lead in the comedy film Definitely, Maybe, alongside Isla Fisher and Ryan Reynolds,[24] starred with Seth Rogen as the eponymous female lead in the Kevin Smith comedy Zack and Miri Make a Porno,[21] and played United States First Lady Laura Bush in W., Oliver Stone's biopic of George W. Bush.[25]
In 2009, Banks appeared in the horror film The Uninvited, a remake of the South Korean film A Tale of Two Sisters.[26] The film was about an intrusive stepmother who makes life miserable for the teen daughters of her new husband. Banks based her character, Rachel, on Rebecca De Mornay's character in The Hand That Rocks the Cradle.[27] "It was very important to me that every line reading I gave could be interpreted two ways," says Banks of her role, "So that when you go back through the movie you can see that".[27]
Banks is a frequent co-star of actor Paul Rudd, the two having appeared in five films together to date (Wet Hot American Summer, The Baxter, The 40-Year-Old Virgin, Role Models, and Our Idiot Brother).[28] She is also a frequent co-star of actor Tobey Maguire, the two having also appeared in five films together (Spider-Man, Seabiscuit, Spider-Man 2, Spider-Man 3, and The Details).[29]
Banks was cast as a love interest for Jack Donaghy (Alec Baldwin) in the fourth season of the Emmy Award-winning sitcom 30 Rock.[30] Intended to appear in four episodes in 2010, Banks went on to become a recurring character with 13 appearances by the end of the fifth season, including her marriage in the episode Mrs. Donaghy. Her performance in season five earned her a nomination for Primetime Emmy Award for Outstanding Guest Actress in a Comedy Series for the 63rd Primetime Emmy Awards.[31]
Banks at the What to Expect When You're Expecting premiere in 2012
In 2012, Banks also starred in the film What to Expect When You're Expecting alongside Jennifer Lopez. She starred in the film The Hunger Games (2012), playing Effie Trinket, a woman from "The Capitol" who escorts the District 12 tributes to the annual Hunger Games. She reprised the role in the sequel films The Hunger Games: Catching Fire (2013), The Hunger Games: Mockingjay – Part 1 (2014), and The Hunger Games: Mockingjay – Part 2 (2015).[21] Banks co-starred in the 2014 movie Every Secret Thing, playing Detective Nancy Porter investigating the disappearance of a young child with similarities to a case she had previously been involved with.[32]
In 2014, Banks was recognized by Elle Magazine during The Women in Hollywood Awards, honoring women for their outstanding achievements in film, spanning all aspects of the motion picture industry, including acting, directing, and producing.[33]
Banks portrayed Melinda Ledbetter Wilson, the wife of Brian Wilson, in the 2015 biopic Love & Mercy, which is based on the life of the legendary musician and founding member of The Beach Boys, as portrayed by John Cusack.[34] After producing and appearing, as Gail, in the first Pitch Perfect film, Banks directed its sequel, Pitch Perfect 2 (2015), making her feature directorial debut. She also co-produced, and again played Gail in, both Pitch Perfect 2 and the next sequel Pitch Perfect 3 (2017).[35]
In 2015, she was named as a member of the Jury for the Main Competition at the 2015 Venice Film Festival. The festival is chaired by Alfonso Cuarón.[36] Also in 2015, Banks became a spokeswoman for Realtor.com in their series of television commercials.[37] As of mid-February 2016, Banks became the commercial face of Old Navy.[38] She also played space alien Rita Repulsa in the 2017 Power Rangers reboot film.[39]
In 2018, Banks co-starred as Jenny in the comedy film The Happytime Murders, alongside Melissa McCarthy and Maya Rudolph.[40] In 2019, she will reprise her starring role as Lucy "Wyldstyle" in the comedy film The Lego Movie 2: The Second Part. Banks will also direct, produce, and star as Bosley in the reboot film Charlie's Angels.
Personal life[edit]
Banks during a USO visit at Bagram Air Base, Afghanistan in 2015
Banks met her husband, Max Handelman, a sportswriter and producer from Portland, Oregon,[41] on her first day of college on September 6, 1992. They were married in 2003. The couple have two sons.[42] She and her husband had their first child, Felix, who was born through a surrogate in March 2011.[43] In November 2012, Banks announced the birth of another son, Magnus Mitchell, also by a surrogate.[44]
Banks went through parts of conversion to Judaism, her husband's faith, and studied with rabbis. In 2013, speaking of her religion, she stated that she practices Judaism, though "I did not have my mikveh, so technically I'm not converted," but that she has "been essentially a Jew for like 15 years," adding "Frankly, because I'm already doing everything [practicing religious rituals], I feel like I'm as Jewish as I'm ever going to be."[45][46]
Banks was a vocal supporter of Hillary Clinton's 2016 presidential campaign[47] and was involved in a rendition of Rachel Platten's single "Fight Song" with other celebrities at the 2016 Democratic National Convention.[48]
Filmography[edit]
Film[edit]
Year
Title
Role
Notes
1998 Surrender Dorothy Vicki Credited as Elizabeth Casey
2000 Shaft Trey's friend Credited as Elizabeth Maresal Mitchell
2001 Wet Hot American Summer Lindsay
Ordinary Sinner Rachel
2002 Spider-Man Betty Brant
Swept Away Debi
Catch Me If You Can Lucy Forrest
2003 The Trade Sioux Sever
Seabiscuit Marcela Howard
2004 Spider-Man 2 Betty Brant
2005 Heights Isabel Lee
Sexual Life Sarah
The Sisters Nancy Pecket
The Baxter Caroline Swann
The 40-Year-Old Virgin Beth
Daltry Calhoun May
2006 Slither Starla Grant
Invincible Janet Cantrell
2007 Spider-Man 3 Betty Brant
Meet Bill Jess
Fred Claus Charlene
2008 Definitely, Maybe Emily Jones
Meet Dave Gina Morrison
Lovely, Still Alex
W. Laura Bush
Zack and Miri Make a Porno Miriam "Miri" Linky
Role Models Beth Jones
2009 Big Breaks Starlet Short film
The Uninvited Rachel Summers
Surrogates N/A Executive producer
2010 The Next Three Days Lara Brennan
2011 The Details Nealy Lang
Just a Little Heart Attack Woman Short film
Also director
Our Idiot Brother Miranda Rochlin
2012 Man on a Ledge Lydia Mercer
The Hunger Games Effie Trinket
What to Expect When You're Expecting Wendy Cooper
People Like Us Frankie Davis
Pitch Perfect Gail Abernathy-McKadden Also producer
2013 Movie 43 Amy Segment: "Beezel"
Directed segment: "Middleschool Date"
The Hunger Games: Catching Fire Effie Trinket
2014 Little Accidents Diane Doyle
The Lego Movie Lucy "Wyldstyle" Voice role
Walk of Shame Meghan Miles
Every Secret Thing Detective Nancy Porter
Love & Mercy Melinda Ledbetter
The Hunger Games: Mockingjay – Part 1 Effie Trinket
2015 Pitch Perfect 2 Gail Abernathy-McKadden-Feinberger Also director and producer
Magic Mike XXL Paris
The Hunger Games: Mockingjay – Part 2 Effie Trinket
2017 The Most Hated Woman in America N/A Producer
Power Rangers Rita Repulsa
Pitch Perfect 3 Gail Abernathy-McKadden-Feinberger Also producer
2018 The Happytime Murders Jenny
2019 The Lego Movie 2: The Second Part Lucy "Wyldstyle" Post-production; voice role
Charlie's Angels Bosley Pre-production; also director and producer
TBA Queen for a Day Pre-production; also producer
Television[edit]
Year
Title
Role
Notes
1998 Keep Going Safety Ben's Mom Voice role
1999 All My Children Rosalie 1 episode
Third Watch Elaine Elchisak Episode: "Patterns"
Credited as Elizabeth Maresal Mitchell
2000 Sex and the City Catherine Episode: "Politically Erect"
2001 Law & Order: Special Victims Unit Jaina Tobias Jansen Episode: "Sacrifice"
2002 Without a Trace Clarissa Episode: "Snatch Back"
2005 Stella Tamara Episode: "Meeting Girls"
2006–09 Scrubs Dr. Kim Briggs 17 episodes
2007–08 Wainy Days Shelly 3 episodes
American Dad! Becky Arangino / Lisa Silver (voices) 3 episodes
2008 Comanche Moon Maggie Tilton 3 episodes
2009, 2013–15, 2017 Modern Family Sal 6 episodes
2010–12 30 Rock Avery Jessup 15 episodes
2012 Family Guy Pam Fishman (voice) Episode: "Into Fat Air"
Robot Chicken Mrs. Claus / Shana "Scarlett" O'Hara (voices) Episode: "Robot Chicken's ATM Christmas Special"
Comedy Bang! Bang! Herself Episode: "Elizabeth Banks Wears A Red Dress"
2013 Timms Valley Beth Billings-Timms (voice) Pilot
2014 Phineas and Ferb Grulinda (voice) Episode: "Imperfect Storm"
2015 Resident Advisors Doctor Episode: "Motivational Speaker "; also producer
Wet Hot American Summer: First Day of Camp Lindsay 6 episodes
Moonbeam City Chief Pizzaz Miller (voice) 10 episodes
The Muppets Herself Episode: "Pig Girls Don't Cry"
Saturday Night Live Herself (host) Episode: "Elizabeth Banks/Disclosure"
2017 Wet Hot American Summer: Ten Years Later Lindsay 5 episodes
Curb Your Enthusiasm Herself Episode: "A Disturbance in the Kitchen"
Music videos[edit]
Year
Title
Artist
2018 "Girls Like You" (featuring Cardi B) Maroon 5
"Girls Like You" (Vertical Video)
Video games[edit]
Year
Title
Role
2015 Lego Dimensions Lucy "Wyldstyle"
Awards and nominations[edit]
Year
Work
Association
Category
Result
Ref.
2003 Seabiscuit Screen Actors Guild Awards Outstanding Performance by a Cast in a Motion Picture Nominated [49]
2006 Invincible MTV Movie Awards Best Kiss Nominated [22]
Slither Fangoria Chainsaw Awards Relationship from Hell Nominated
2008 W. Detroit Film Critics Society Best Supporting Actress Nominated [50]
2009 N/A Women in Film Crystal + Lucy Awards Face of the Future Award Won [51]
The Uninvited Fright Meter Awards Best Supporting Actress Nominated
2011 30 Rock Primetime Emmy Awards Outstanding Guest Actress in a Comedy Series Nominated [31]
Gold Derby Awards Best Comedy Guest actress Nominated
2012 The Hunger Games MTV Movie Awards Best On-Screen Transformation Won [52]
Teen Choice Awards Choice Movie: Female Scene Stealer Nominated [53]
30 Rock Primetime Emmy Awards Outstanding Guest Actress in a Comedy Series Nominated [31]
2013 Movie 43 Golden Raspberry Awards Worst Director Won [54]
N/A CinemaCon Excellence in Acting Won [55]
The Hunger Games: Catching Fire MTV Movie Awards Best On-Screen Transformation Nominated [56]
San Diego Film Critics Society Awards Best Supporting Actress Nominated [57]
Modern Family Online Film & Television Association Awards Best Guest Actress in a Comedy Series Nominated [58]
Gold Derby Awards Best Comedy Guest Actress Nominated
2014 The Lego Movie BTVA Awards Best Female Lead Vocal Performance Nominated [59]
Best Vocal Ensemble Nominated
BTVA People's Choice Awards Best Female Lead Vocal Performance Won
Best Vocal Ensemble Won
Love & Mercy Florida Film Critics Circle Awards Best Supporting Actress Nominated [60]
Austin Film Critics Association Best Supporting Actress Nominated [61]
Indiana Film Journalists Association Best Supporting Actress Nominated [62]
Denver Film Critics Society Best Supporting Actress Nominated [63]
Las Vegas Film Critics Society Best Supporting Actress Won [64]
San Francisco Film Critics Circle Best Supporting Actress Nominated [65]
Georgia Film Critics Association Best Supporting Actress Nominated
Santa Barbara International Film Festival Virtuoso Award Won [66]
Satellite Awards Best Supporting Actress – Motion Picture Nominated [67]
2015 N/A CinemaCon Breakthrough Filmmaker of the Year Won [68]
The Hunger Games: Mockingjay – Part 1 MTV Movie Awards Best On-Screen Transformation Won [69]
Modern Family Online Film & Television Association Awards Best Guest Actress in a Comedy Series Nominated [70]
Gold Derby Awards Best Comedy Guest Actress Nominated
Primetime Emmy Awards Outstanding Guest Actress in a Comedy Series Nominated [31]
Pitch Perfect 2 Golden Raspberry Awards The Razzie Redeemer Award Nominated [71]
2016 Lego Dimensions BTVA Awards Best Vocal Ensemble in a Video Game Won
BTVA People's Choice Awards Best Vocal Ensemble in a Video Game Won
2017 Power Rangers Teen Choice Awards Choice Movie Villain Nominated
References[edit]
Jump up ^ Vary, Adam B. (2008-10-20). "Elizabeth Banks Fall's First Lady Elizabeth Banks Movie Spotlight Movies Entertainment Weekly 2". Entertainment Weekly. Retrieved 2008-11-01.
Jump up ^ "Elizabeth Irene Mitchell". familytreemaker.genealogy.com. Retrieved July 26, 2012.
Jump up ^ "Monitor". Entertainment Weekly. Feb 15, 2013.
Jump up ^ "Box office: 'Pitch Perfect 2' crescendos past 'Mad Max: Fury Road' to $70.3 million". LATimes.com. 2015-05-17. Retrieved 2015-05-18.
Jump up ^ "Box Office Top 20: 'Pitch Perfect 2' lands at $69.2 million". yahoo.com. 2015-05-18. Archived from the original on 2015-05-21. Retrieved 2015-05-22.
Jump up ^ "Box Office Mojo - People Index". Box Office Mojo. Retrieved 2 November 2016.
Jump up ^ Jessica Willis (October 21, 2008). "From Pittsfield to the big screen". The Berkshire Eagle.
Jump up ^ James Mottram (2008-11-08). "Elizabeth Banks: from the top-shelf to First Lady in W". The Times. London. Retrieved 2008-11-07.
Jump up ^ "Elizabeth Banks". Twitter. Retrieved July 26, 2012.
Jump up ^ "About Elizabeth Banks". yahoo movies. Archived from the original on March 28, 2012. Retrieved July 26, 2012.
Jump up ^ "Elizabeth Banks Was A Sexy-Flirty Latin Clubber". TeamCoco. September 24, 2012. Retrieved March 16, 2013.
Jump up ^ "How to Succeed in Business by Really, Really Trying". Penn Gazette. December 22, 2009. Retrieved September 11, 2013.
Jump up ^ "Master of Fine Arts Program in Acting". www.act-sf.org. Retrieved 7 August 2015.
Jump up ^ "Elizabeth Banks And Annette Bening Honored At American Conservatory Theater Awards". Huffington post. Retrieved 7 August 2015.
Jump up ^ Strauss, Bob (2008-10-27). "From first lady to Porno star actress: Elizabeth Banks dishes the dirt". The Seattle Times. Archived from the original on 2008-10-30. Retrieved 2008-11-01.
Jump up ^ Banks, Elizabeth (November 4, 2015). "Love & Mercy, Elizabeth Banks". DP/30: The Oral History of Hollywood (Interview). Retrieved April 6, 2016.
Jump up ^ "Swept Away". New York Times. Retrieved 7 August 2015.
Jump up ^ "The 40-Year Old Virgin Is Ten Years Old". movie pilot.com. Retrieved 7 August 2015.
Jump up ^ Sommer, Elyse. 2005, Curtain Up.
Jump up ^ Borak, Jeffrey 2005. "Love blooms in a Kansas diner", Berkshire Eagle August 20, Art section.
^ Jump up to: a b c d "Elizabeth Banks Biography". biography.com. Retrieved 7 August 2015.
^ Jump up to: a b Jones, Alan. "Invincible". radiotimes.com. Retrieved 7 August 2015.
Jump up ^ "Slither movie review". Retrieved 7 August 2015.
Jump up ^ "Definitely, Maybe (2008)". New York Times. Retrieved 7 August 2015.
Jump up ^ "Elizabeth Banks is Oliver Stone's Laura Bush". ComingSoon.net. 2008-03-26. Retrieved 2008-11-01.
Jump up ^ Barton, Steve (2010-03-01). "Elizabeth Banks to Head Out into the Dark Fields?". Dreadcentral.com. Retrieved 2015-03-11.
^ Jump up to: a b "Elizabeth Banks: The Uninvited". SuicideGirls.com. 30 January 2009. Retrieved 2009-01-30.
Jump up ^ On, Cs (2010-02-27). "Elizabeth Banks Entering Dark Fields?". Comingsoon.net. Retrieved 2015-03-11.
Jump up ^ "Tobey Maguire on New Spider-Man Film". YouTube.com. 2012-05-08. Retrieved 2015-03-11.
Jump up ^ Joyce Eng. "Elizabeth Banks to Guest-Star on 30 Rock". TVGuide.com.
^ Jump up to: a b c d "Elizabeth Banks". Emmys.com. Retrieved 7 August 2015.
Jump up ^ "'Every Secret Thing' review: Diane Lane, Elizabeth Banks and Dakota Fanning grapple with underwhelming drama". ny daily news. Retrieved 7 August 2015.
Jump up ^ ELLE (15 October 2014). "Women in Hollywood 2014 - ELLE November 2014 Cover Story". ELLE.
Jump up ^ "Watch John Cusack and Elizabeth Banks's Awkward First Date in an Exclusive Clip from Love & Mercy". Vanity fair. Retrieved 7 August 2015.
Jump up ^ "Elizabeth Banks: 'I Had More to Offer an Industry That Clearly Didn't Expect Too Much'". variety.com. Retrieved 7 August 2015.
Jump up ^ "Elizabeth Banks, Diane Kruger join Alfonso Cuarón on Venice Film Festival jury". Entertainment weekly. Retrieved 7 August 2015.
Jump up ^ "Elizabeth Banks Is in Our New TV Ads, and That's Pretty Cool". Real Estate News and Advice - realtor.com.
Jump up ^ "WORK STUFF".
Jump up ^ "Elizabeth Banks Cast as Rita Repulsa in Power Rangers Movie". Entertainment Weekly. Retrieved February 3, 2016.
Jump up ^ Hipes, Patrick (September 13, 2017). "Elizabeth Banks Joins Gang For 'The Happytime Murders'". Deadline. Retrieved September 14, 2017.
Jump up ^ "Celebrity Wedding: Elizabeth Banks & Max Handelman". In Style. Retrieved 2009-01-06.
Jump up ^ Tiger, Caroline 2010. "How to Succeed in Show Business by Really Really Trying". The Pennsylvania Gazette Jan.-Feb., Vol. 108, No. 3, pp. 46–50.
Jump up ^ Michaud, Sarah (March 31, 2011). "Elizabeth Banks Names 'Miracle' Baby Felix". people.com. Retrieved July 26, 2012.
Jump up ^ Banks, Elizabeth (November 14, 2012). "IT'S A BOY!". elizabethbanks.com. Retrieved March 16, 2013.
Jump up ^ Butnick, Stephanie (January 17, 2013). "Jewish Actress Elizabeth Banks Discusses Her Conversion With Marc Maron". Jewcy. Retrieved March 16, 2013.
Jump up ^ "Episode 352 – Elizabeth Banks". WTF with Marc Maron. January 14, 2013. Retrieved March 16, 2013.
Jump up ^ Wilstein, Matt (June 27, 2016). "Elizabeth Banks Trolls Trump at DNC: 'A Cruel, Out-of-Touch Reality TV Star Who Wears Insane Wigs'". The Daily Beast. Retrieved October 21, 2016.
Jump up ^ "See Elizabeth Banks, Celebrities' 'Our Fight Song' Video". Retrieved 2016-08-13.
Jump up ^ "The 10th Annual Screen Actors Guild Awards - Screen Actors Guild Awards".
Jump up ^ "The 2008 Detroit Film Critics Society Awards". Detroit Film Critics Society. Retrieved April 17, 2014.
Jump up ^ "Women in Film to Honor Holly Hunter and Jennifer Aniston". womenandhollywood.com. Retrieved 7 August 2015.
Jump up ^ "2012 MTV Movie Awards". MTV. Retrieved November 5, 2015.
Jump up ^ "Teen Choice Awards 2012: 'Hunger Games,' 'Twilight' and Justin Bieber Win Big". ABC News. July 23, 2012. Retrieved November 5, 2015.
Jump up ^ "The 34th Annual RAZZIE® Award Nominees for 2013 Worst Director". The Golden Raspberry Award Foundation and John Wilson. Retrieved January 15, 2014.
Jump up ^ "CinemaCon: Elizabeth Banks to Receive Excellence in Acting Award". Hollywood Reporter.
Jump up ^ "Best on-screen transformation". mtv.com. Retrieved 7 August 2015.
Jump up ^ "San Diego Film Critics Select Top Films for 2013". San Diego Film Critics Society. December 11, 2013. Retrieved November 5, 2015.
Jump up ^ "Online Film & Television Association".
Jump up ^ "Behind The Voice Actors - BTVA Voice Acting Awards". Behind The Voice Actors.
Jump up ^ "'Carol' Leads 2015 Florida Film Critics Awards Nominations". FloridaFilmCritics.com.
Jump up ^ "The AFCA 2015 Awards Nominees". Archived from the original on 2015-12-19.
Jump up ^ "'Spotlight' named Best Picture by Indiana Film Journalists Association".
Jump up ^ "'Spotlight' named Best Picture by Indiana Film Journalists Association".
Jump up ^ "Las Vegas Film Critics SocietyAwards".
Jump up ^ "The San Francisco Film Critics Circle". Retrieved December 13, 2015.
Jump up ^ Scott Feinberg (17 November 2015). "Santa Barbara Film Fest: Elizabeth Banks, Paul Dano, Joel Edgerton and Jacob Tremblay Named Virtuosos". The Hollywood Reporter.
Jump up ^ "Satellite Awards Nominees Unveiled". hollywoodreporter. Retrieved 15 December 2015.
Jump up ^ "Elizabeth Banks Named CinemaCon's Breakthrough Filmmaker of the Year". Variety. Retrieved March 24, 2015.
Jump up ^ "YANGAROO and MTV Extend Deal for 2015 and 2016 MTV Movie Awards and MTV Video Music Awards", Naijadudes. Retrieved on 11 January 2015.
Jump up ^ "Online Film & Television Association".
Jump up ^ "Razzie Awards 2016 Winners Announced". ComingSoon.net. 27 February 2016. Retrieved 28 February 2016.
External links[edit]
Wikimedia Commons has media related to Elizabeth Banks.
Official website
Elizabeth Banks on IMDb
Elizabeth Banks at Box Office Mojo
Elizabeth Banks at the TCM Movie Database
Elizabeth Banks at AllMovie
Elizabeth Banks appearances on C-SPAN
show
Awards for Elizabeth Banks
show
v
t
e
Golden Raspberry Awards for Worst Director
1980–2000
Robert Greenwald (1980)
Michael Cimino (1981)
Ken Annakin / Terence Young (1982)
Peter Sasdy (1983)
John Derek (1984)
Sylvester Stallone (1985)
Prince (1986)
Norman Mailer / Elaine May (1987)
Blake Edwards / Stewart Raffill (1988)
William Shatner (1989)
John Derek (1990)
Michael Lehmann (1991)
David Seltzer (1992)
Jennifer Lynch (1993)
Steven Seagal (1994)
Paul Verhoeven (1995)
Andrew Bergman (1996)
Kevin Costner (1997)
Gus Van Sant (1998)
Barry Sonnenfeld (1999)
Roger Christian (2000)
2001–present
Tom Green (2001)
Guy Ritchie (2002)
Martin Brest (2003)
Pitof (2004)
John Asher (2005)
M. Night Shyamalan (2006)
Chris Sivertson (2007)
Uwe Boll (2008)
Michael Bay (2009)
M. Night Shyamalan (2010)
Dennis Dugan (2011)
Bill Condon (2012)
Elizabeth Banks, Steven Brill, Steve Carr, Rusty Cundieff, James Duffy, Griffin Dunne, Peter Farrelly, Patrik Forsberg, Will Graham, James Gunn, Bob Odenkirk, Brett Ratner, and Jonathan van Tulleken (2013)
Michael Bay (2014)
Josh Trank (2015)
Dinesh D'Souza and Bruce Schooley (2016)
Tony Leondis (2017)
show
v
t
e
MTV Movie Award for Best On-Screen Transformation
Elizabeth Banks (2012)
Jared Leto (2014)
Elizabeth Banks (2015)
Authority control
WorldCat Identities
BNE: XX4765546
BNF: cb15717822g (data)
GND: 142544787
ISNI: 0000 0001 1604 628X
LCCN: no2004004174
MusicBrainz: 9109a906-01a5-48e8-8f63-b915f2e83ada
SUDOC: 14442732X
VIAF: 229406474
Retrieved from "https://en.wikipedia.org/w/index.php?title=Elizabeth_Banks&oldid=857016994"
Categories:
1974 births
Living people
20th-century American actresses
21st-century American actresses
Actresses from Massachusetts
American film actresses
American people of Irish descent
American television actresses
American video game actresses
American voice actresses
American women film directors
American women film producers
American film producers
Converts to Judaism
Jewish American actresses
Massachusetts Democrats
People from Pittsfield, Massachusetts
Annenberg School for Communication at the University of Pennsylvania alumni
Hidden categories:
Infobox person using alma mater
Articles with hCards
Articles containing potentially dated statements from July 2018
All articles containing potentially dated statements
Wikipedia articles with BNE identifiers
Wikipedia articles with BNF identifiers
Wikipedia articles with GND identifiers
Wikipedia articles with ISNI identifiers
Wikipedia articles with LCCN identifiers
Wikipedia articles with MusicBrainz identifiers
Wikipedia articles with SUDOC identifiers
Wikipedia articles with VIAF identifiers
Navigation menu
Personal tools
Not logged in
Talk
Contributions
Create account
Log in
Namespaces
Article
Talk
Variants
Views
Read
Edit
View history
More
Search
Navigation
Main page
Contents
Featured content
Current events
Random article
Donate to Wikipedia
Wikipedia store
Interaction
Help
About Wikipedia
Community portal
Recent changes
Contact page
Tools
What links here
Related changes
Upload file
Special pages
Permanent link
Page information
Wikidata item
Cite this page
Print/export
Create a book
Download as PDF
Printable version
In other projects
Wikimedia Commons
Languages
Afrikaans
العربية
Asturianu
تۆرکجه
Bân-lâm-gú
Български
Català
Čeština
Dansk
Deutsch
Ελληνικά
Español
Euskara
فارسی
Français
Frysk
Galego
한국어
Ido
Bahasa Indonesia
Italiano
עברית
Қазақша
Latviešu
Lietuvių
Magyar
मैथिली
Malagasy
مصرى
Bahasa Melayu
Монгол
Nederlands
नेपाली
日本語
Norsk
Norsk nynorsk
Polski
Português
Română
Русский
Scots
Shqip
Simple English
Српски / srpski
Srpskohrvatski / српскохрватски
Suomi
Svenska
ไทย
Türkçe
Українська
اردو
Tiếng Việt
中文
डोटेली
45 more
Edit links
This page was last edited on 29 August 2018, at 00:55 (UTC).
Text is available under the Creative Commons Attribution-ShareAlike License; additional terms may apply. By using this site, you agree to the Terms of Use and Privacy Policy. Wikipedia® is a registered trademark of the Wikimedia Foundation, Inc., a non-profit organization.
Privacy policy
About Wikipedia
Disclaimers
Contact Wikipedia
Developers
Cookie statement
Mobile view
Enable previews

values: mw-page-base noprint

values: mw-head-base noprint

values: firstHeading firstHeading en

values: siteSub noprint

values: mw-jump-link #mw-head

values: mw-jump-link #p-search

values:
note
hatnote navigation-not-searchable

attrs: href class

values:
nofollow
external text
http://www.elizabethbanks.com

values:
/wiki/Effie_Trinket
mw-redirect
Effie Trinket

values: What to Expect When You're Expecting (film)

values:
/wiki/Avery_Jessup
mw-redirect
Avery Jessup

values: Wet Hot American Summer: First Day of Camp

values: Wet Hot American Summer: Ten Years Later

values: plainlinks noexcerpt noprint asof-tag update

values: checkbox button toctogglecheckbox toctogglecheckbox display:none

values:
/wiki/Surrender_Dorothy_(1998_film)
mw-redirect
Surrender Dorothy (1998 film)

values:
/wiki/Bus_Stop_(play)
mw-redirect
Bus Stop (play)

values:
/wiki/MTV_Movie_Awards
mw-redirect
MTV Movie Awards

values: List of Characters in the Hunger Games trilogy

values:
/wiki/Charlie%27s_Angels_(2019_film)
mw-redirect
Charlie's Angels (2019 film)

values:
headerSort
0
columnheader button
Sort ascending

values:
/wiki/Surrogates_(film)
mw-redirect
Surrogates (film)

values: background: #ececec; color: #2C2C2C; vertical-align: middle; font-size: smaller; text-align: center;

values: background: #DDF; color: #2C2C2C; vertical-align: middle; text-align: center;

values:
/wiki/Girls_Like_You_(Maroon_5_song)
mw-redirect
Girls Like You (Maroon 5 song)

values: background: #FDD; color: black; vertical-align: middle; text-align: center;

values: background: #99FF99; color: black; vertical-align: middle; text-align: center;

values: 63rd Primetime Creative Arts Emmy Awards

values: Teen Choice Award for Choice Movie Scene Stealer

values: 64th Primetime Creative Arts Emmy Awards

values: Golden Raspberry Award for Worst Director

values: San Diego Film Critics Society Awards 2013

values: Santa Barbara International Film Festival

values: Satellite Award for Best Supporting Actress – Motion Picture

values: 67th Primetime Creative Arts Emmy Awards

values: Teen Choice Award for Choice Movie Villain

values:
nofollow
external text
http://www.lvfcs.org/awards.html

values:
nofollow
http://sffcc.org/
external text

values: -moz-column-width: 30em; -webkit-column-width: 30em; column-width: 30em; list-style-type: decimal;

values:
nofollow
https://www.imdb.com/name/nm0006969/
external text

attrs: alt src width height style srcset data-file-width data-file-height

values:
nofollow
external text
https://www.allmovie.com/artist/p292126

values: Template:Golden Raspberry Award for Worst Director

values: Template talk:Golden Raspberry Award for Worst Director

values:
row
navbox-group
background: #EEDD82;width:1%

values:
/wiki/Steven_Brill_(scriptwriter)
mw-redirect
Steven Brill (scriptwriter)

values: nowraplinks hlist collapsible autocollapse navbox-inner mw-collapsible mw-made-collapsible mw-collapsed

values: Template:MTV Movie Award for Best On-Screen Transformation

values: Template talk:MTV Movie Award for Best On-Screen Transformation

values: nowraplinks collapsible autocollapse navbox-inner mw-collapsible mw-made-collapsible mw-collapsed

values: nowraplinks collapsible collapsed navbox-inner mw-collapsible mw-collapsed mw-made-collapsible

values:
nofollow
external text
https://d-nb.info/gnd/142544787

values:
nofollow
external text
http://isni.org/isni/000000011604628X

values:
nofollow
external text
https://www.idref.fr/14442732X

values:
nofollow
external text
https://viaf.org/viaf/229406474

values: Category:American people of Irish descent

values: Category:People from Pittsfield, Massachusetts

values: Category:Annenberg School for Communication at the University of Pennsylvania alumni

values: Category:Infobox person using alma mater

values: Category:Articles containing potentially dated statements from July 2018

values: Category:All articles containing potentially dated statements

values: Category:Wikipedia articles with BNE identifiers

values: Category:Wikipedia articles with BNF identifiers

values: Category:Wikipedia articles with GND identifiers

values: Category:Wikipedia articles with ISNI identifiers

values: Category:Wikipedia articles with LCCN identifiers

values: Category:Wikipedia articles with MusicBrainz identifiers

values: Category:Wikipedia articles with SUDOC identifiers

values: Category:Wikipedia articles with VIAF identifiers

values: Discussion about edits from this IP address [ctrl-alt-n]

values: A list of edits made from this IP address [ctrl-alt-y]

values: You are encouraged to create an account and log in; however, it is not mandatory

values: You're encouraged to log in; however, it's not mandatory. [ctrl-alt-o]

values:
/wiki/Elizabeth_Banks
View the content page [ctrl-alt-c]
c

values: Discussion about the content page [ctrl-alt-t]

values: p-namespaces navigation vectorTabs p-namespaces-label

values:
p-variants
navigation
vectorMenu emptyPortlet
p-variants-label

values: A list of recent changes in the wiki [ctrl-alt-r]

values: portal navigation p-interaction p-interaction-label

values: List of all English Wikipedia pages containing links to this page [ctrl-alt-j]

values: Recent changes in pages linked from this page [ctrl-alt-k]

values:
/wiki/Wikipedia:File_Upload_Wizard
Upload files [ctrl-alt-u]
u

values: A list of all special pages [ctrl-alt-q]

values: Permanent link to this revision of the page

values: Link to connected data repository item [ctrl-alt-g]

values: Printable version of this page [ctrl-alt-p]

values: portal navigation p-wikibase-otherprojects p-wikibase-otherprojects-label

values:
interlanguage-link interwiki-af
display: none;

values: إليزابيث بانكس – Arabic

values:
interlanguage-link interwiki-ast
display: none;

values:
interlanguage-link interwiki-azb
display: none;

values:
interlanguage-link interwiki-zh-min-nan
display: none;

values: Елизабет Банкс – Bulgarian

values:
interlanguage-link interwiki-bg
display: none;

values:
interlanguage-link interwiki-ca
display: none;

values:
interlanguage-link interwiki-cs
display: none;

values:
interlanguage-link interwiki-da
display: none;

values:
interlanguage-link interwiki-de
display: none;

values: Ελίζαμπεθ Μπανκς – Greek

values:
interlanguage-link interwiki-el
display: none;

values:
interlanguage-link interwiki-eu
display: none;

values: الیزابت بنکس – Persian

values:
interlanguage-link interwiki-fa
display: none;

values:
interlanguage-link interwiki-fy
display: none;

values:
interlanguage-link interwiki-gl
display: none;

values: 엘리자베스 뱅크스 – Korean

values:
interlanguage-link interwiki-ko
display: none;

values:
interlanguage-link interwiki-io
display: none;

values:
interlanguage-link interwiki-it
display: none;

values: אליזבת' בנקס – Hebrew

values:
interlanguage-link interwiki-he
display: none;

values: Элизабет Бэнкс – Kazakh

values:
interlanguage-link interwiki-kk
display: none;

values:
interlanguage-link interwiki-lv
display: none;

values:
interlanguage-link interwiki-lt
display: none;

values:
interlanguage-link interwiki-hu
display: none;

values: एलिजाबेथ ब्याङ्क्स – Maithili

values:
interlanguage-link interwiki-mai
display: none;

values:
interlanguage-link interwiki-mg
display: none;

values: اليزابيث بانكس – Egyptian Arabic

values:
interlanguage-link interwiki-arz
display: none;

values: Элизабет Бэнкс – Mongolian

values:
interlanguage-link interwiki-mn
display: none;

values:
interlanguage-link interwiki-nl
display: none;

values: एलिजाबेथ ब्याङ्क्स – Nepali

values:
interlanguage-link interwiki-ne
display: none;

values: エリザベス・バンクス – Japanese

values:
interlanguage-link interwiki-ja
display: none;

values:
interlanguage-link interwiki-no
display: none;

values:
interlanguage-link interwiki-nn
display: none;

values:
interlanguage-link interwiki-pl
display: none;

values:
interlanguage-link interwiki-ro
display: none;

values: Бэнкс, Элизабет – Russian

values:
interlanguage-link interwiki-sco
display: none;

values:
interlanguage-link interwiki-sq
display: none;

values:
interlanguage-link interwiki-simple
display: none;

values: Елизабет Бенкс – Serbian

values:
interlanguage-link interwiki-sr
display: none;

values:
interlanguage-link interwiki-sh
display: none;

values:
interlanguage-link interwiki-fi
display: none;

values:
interlanguage-link interwiki-sv
display: none;

values: เอลิซาเบท แบงส์ – Thai

values:
interlanguage-link interwiki-th
display: none;

values:
interlanguage-link interwiki-tr
display: none;

values: Елізабет Бенкс – Ukrainian

values:
interlanguage-link interwiki-uk
display: none;

values: الزبتھ بینکس – Urdu

values:
interlanguage-link interwiki-vi
display: none;

values: 伊丽莎白·班克斯 – Chinese

values: एलिजाबेथ ब्याङ्क्स – Doteli

values:
interlanguage-link interwiki-dty
display: none;

values: All languages (initial selection from common choices by you and others)

values: mediawiki ltr sitedir-ltr mw-hide-empty-elt ns-0 ns-subject page-Elizabeth_Banks rootpage-Elizabeth_Banks skin-vector action-view


text:
Alcohol dehydrogenase
From Wikipedia, the free encyclopedia
Jump to: navigation, search
alcohol dehydrogenase
Crystallographic structure of the
homodimer of human ADH5.[1]
Identifiers
EC number
1.1.1.1
CAS number
9031-72-5
Databases
IntEnz
IntEnz view
BRENDA
BRENDA entry
ExPASy
NiceZyme view
KEGG
KEGG entry
MetaCyc
metabolic pathway
PRIAM
profile
PDB structures
RCSB PDB PDBe PDBsum
Gene Ontology
AmiGO / QuickGO
[show]Search
PMC
articles
PubMed
articles
NCBI
proteins
Alcohol dehydrogenases (ADH) (EC 1.1.1.1) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in generation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+.
Contents
[hide]
1 Evolution
2 Discovery
3 Properties
4 Oxidation of alcohol
4.1 Mechanism of action in humans
4.1.1 Steps
4.1.2 Involved subunits
5 Active site
6 Structural zinc site
7 Types
7.1 Human
7.2 Yeast and bacteria
7.3 Plants
7.4 Iron-containing
7.5 Other types
8 Applications
9 Clinical significance
9.1 Alcoholism
9.2 Drug dependence
9.3 Poisoning
10 See also
11 References
12 External links
Evolution[edit]
Genetic evidence from comparisons of multiple organisms showed that a glutathione-dependent formaldehyde dehydrogenase, identical to a class III alcohol dehydrogenase (ADH-3/ADH5), is presumed to be the ancestral enzyme for the entire ADH family.[2][3][4] Early on in evolution, an effective method for eliminating both endogenous and exogenous formaldehyde was important and this capacity has conserved the ancestral ADH-3 through time. Gene duplication of ADH-3, followed by series of mutations, the other ADHs evolved.[3][4]
The ability to produce ethanol from sugar (which is the basis of how alcoholic beverages are made) is believed to have initially evolved in yeast. Though this feature is not adaptive from an energy point of view, by making alcohol in such high concentrations so that they would be toxic to other organisms, yeast cells could effectively eliminate their competition. Since rotting fruit can contain more than 4% of ethanol, animals eating the fruit needed a system to metabolize exogenous ethanol. This was thought to explain the conservation of ethanol active ADH in species other than yeast, though ADH-3 is now known to also have a major role in nitric oxide signaling.[5][6]
In humans, sequencing of the ADH1B gene (responsible for production of an alcohol dehydrogenase polypeptide) shows two variants, in which there is an SNP (single nucleotide polymorphism) that leads to either a Histidine or an Arginine residue in the enzyme catalyzing the conversion of ethanol into acetaldehyde. In the Histidine variant, the enzyme is much more effective at the aforementioned conversion.[7] The enzyme responsible for the conversion of acetaldehyde to acetate, however, remains unaffected, which leads to differential rates of substrate catalysis and causes a buildup of toxic acetaldehyde, causing cell damage.[7] In humans, various haplotypes arising from this mutation are more concentrated in regions near Eastern China, a region also known for its low alcohol tolerance and dependence.
A study was conducted in order to find a correlation between allelic distribution and alcoholism, and the results suggest that the allelic distribution arose along with rice cultivation in the region between 12,000 and 6,000 years ago.[8] In regions where rice was cultivated, rice was also fermented into ethanol.[8] The results of increased alcohol availability led to alcoholism and abuse by those able to acquire it, resulting in lower reproductive fitness.[8] Those with the variant allele have little tolerance for alcohol, thus lowering chance of dependence and abuse.[7][8] The hypothesis posits that those individuals with the Histidine variant enzyme were sensitive enough to the effects of alcohol that differential reproductive success arose and the corresponding alleles were passed through the generations.
Classical Darwinian evolution would act to select against the detrimental form of the enzyme (Arg variant) because of the lowered reproductive success of individuals carrying the allele. The result would be a higher frequency of the allele responsible for the His-variant enzyme in regions that had been under selective pressure the longest. The distribution and frequency of the His variant follows the spread of rice cultivation to inland regions of Asia, with higher frequencies of the His variant in regions that have cultivated rice the longest.[7] The geographic distribution of the alleles seems to therefore be a result of natural selection against individuals with lower reproductive success, namely, those who carried the Arg variant allele and were more susceptible to alcoholism.[9]
Discovery[edit]
Horse LADH (Liver Alcohol Dehydrogenase)
The first-ever isolated alcohol dehydrogenase (ADH) was purified in 1937 from Saccharomyces cerevisiae (brewer's yeast).[10] Many aspects of the catalytic mechanism for the horse liver ADH enzyme were investigated by Hugo Theorell and coworkers.[11] ADH was also one of the first oligomeric enzymes that had its amino acid sequence and three-dimensional structure determined.[12][13][14]
In early 1960, it was discovered in fruit flies of the genus Drosophila.[15]
Properties[edit]
The alcohol dehydrogenases comprise a group of several isozymes that catalyse the oxidation of primary and secondary alcohols to aldehydes and ketones, respectively, and also can catalyse the reverse reaction.[15] In mammals this is a redox (reduction/oxidation) reaction involving the coenzyme nicotinamide adenine dinucleotide (NAD+).
Oxidation of alcohol[edit]
Mechanism of action in humans[edit]
Steps[edit]
Binding of the coenzyme NAD+
Binding of the alcohol substrate by coordination to zinc
Deprotonation of His-51
Deprotonation of nicotinamide ribose
Deprotonation of Thr-48
Deprotonation of the alcohol
Hydride transfer from the alkoxide ion to NAD+, leading to NADH and a zinc bound aldehyde or ketone
Release of the product aldehyde.
The mechanism in yeast and bacteria is the reverse of this reaction. These steps are supported through kinetic studies.[16]
Involved subunits[edit]
The substrate is coordinated to the zinc and this enzyme has two zinc atoms per subunit. One is the active site, which is involved in catalysis. In the active site, the ligands are Cys-46, Cys-174, His-67, and one water molecule. The other subunit is involved with structure. In this mechanism, the hydride from the alcohol goes to NAD+. Crystal structures indicate that the His-51 deprotonates the nicotinamide ribose, which deprotonates Ser-48. Finally, Ser-48 deprotonates the alcohol, making it an aldehyde.[16] From a mechanistic perspective, if the enzyme adds hydride to the re face of NAD+, the resulting hydrogen is incorporated into the pro-R position. Enzymes that add hydride to the re face are deemed Class A dehydrogenases.
Active site[edit]
The active site of alcohol dehydrogenase
The active site of human ADH1 (PDB:1HSO) consists of a zinc atom, His-67, Cys-174, Cys-46, Thr-48, His-51, Ile-269, Val-292, Ala-317, and Phe-319. In the commonly studied horse liver isoform, Thr-48 is a Ser, and Leu-319 is a Phe. The zinc coordinates the substrate (alcohol). The zinc is coordinated by Cys-46, Cys-174, and His-67. Leu-319, Ala-317, His-51, Ile-269 and Val-292 stabilize NAD+ by forming hydrogen bonds. His-51 and Ile-269 form hydrogen bonds with the alcohols on nicotinamide ribose. Phe-319, Ala-317 and Val-292 form hydrogen bonds with the amide on NAD+.[16]
Structural zinc site[edit]
The structural zinc binding motif in alcohol dehydrogenase from a MD simulation
Mammalian alcohol dehydrogenases also have a structural zinc site. This Zn ion plays a structural role and is crucial for protein stability. The structures of the catalytic and structural zinc sites in horse liver alcohol dehydrogenase (HLADH) as revealed in crystallographic structures, which has been studied computationally with quantum chemical as well as with classical molecular dynamics methods. The structural zinc site is composed of four closely spaced cysteine ligands (Cys97, Cys100, Cys103, and Cys111 in the amino acid sequence) positioned in an almost symmetric tetrahedron around the Zn ion. A recent study showed that the interaction between zinc and cysteine is governed by primarily an electrostatic contribution with an additional covalent contribution to the binding.[17]
Types[edit]
Human[edit]
In humans, ADH exists in multiple forms as a dimer and is encoded by at least seven different genes. There are five classes (I-V) of alcohol dehydrogenase, but the hepatic form that is used primarily in humans is class 1. Class 1 consists of α, β, and γ subunits that are encoded by the genes ADH1A, ADH1B, and ADH1C.[18] The enzyme is present at high levels in the liver and the lining of the stomach.[19] It catalyzes the oxidation of ethanol to acetaldehyde (ethanal):
CH3CH2OH + NAD+ → CH3CHO + NADH + H+
This allows the consumption of alcoholic beverages, but its evolutionary purpose is probably the breakdown of alcohols naturally contained in foods or produced by bacteria in the digestive tract.[20]
Another evolutionary purpose may be metabolism of the endogenous alcohol vitamin A (retinol), which generates the hormone retinoic acid, although the function here may be primarily the elimination of toxic levels of retinol.[21][22]
alcohol dehydrogenase 1A,
α polypeptide
Identifiers
Symbol
ADH1A
Alt. symbols
ADH1
Entrez
124
HUGO
249
OMIM
103700
RefSeq
NM_000667
UniProt
P07327
Other data
EC number
1.1.1.1
Locus
Chr. 4 q23
alcohol dehydrogenase 1B,
β polypeptide
Identifiers
Symbol
ADH1B
Alt. symbols
ADH2
Entrez
125
HUGO
250
OMIM
103720
RefSeq
NM_000668
UniProt
P00325
Other data
EC number
1.1.1.1
Locus
Chr. 4 q23
alcohol dehydrogenase 1C,
γ polypeptide
Identifiers
Symbol
ADH1C
Alt. symbols
ADH3
Entrez
126
HUGO
251
OMIM
103730
RefSeq
NM_000669
UniProt
P00326
Other data
EC number
1.1.1.1
Locus
Chr. 4 q23
Alcohol dehydrogenase is also involved in the toxicity of other types of alcohol: For instance, it oxidizes methanol to produce formaldehyde and ethylene glycol to ultimately yield glycolic and oxalic acids. Humans have at least six slightly different alcohol dehydrogenases. Each is a dimer (i.e., consists of two polypeptides), with each dimer containing two zinc ions Zn2+. One of those ions is crucial for the operation of the enzyme: It is located at the catalytic site and holds the hydroxyl group of the alcohol in place.
Alcohol dehydrogenase activity varies between men and women, between young and old, and among populations from different areas of the world. For example, young women are unable to process alcohol at the same rate as young men because they do not express the alcohol dehydrogenase as highly, although the inverse is true among the middle-aged.[23] The level of activity may not be dependent only on level of expression but also on allelic diversity among the population.
The human genes that encode class II, III, IV, and V alcohol dehydrogenases are ADH4, ADH5, ADH7, and ADH6, respectively.
alcohol dehydrogenase 4
(class II), π polypeptide
Identifiers
Symbol
ADH4
Entrez
127
HUGO
252
OMIM
103740
RefSeq
NM_000670
UniProt
P08319
Other data
EC number
1.1.1.1
Locus
Chr. 4 q22
alcohol dehydrogenase 5
(class III), χ polypeptide
Identifiers
Symbol
ADH5
Entrez
128
HUGO
253
OMIM
103710
RefSeq
NM_000671
UniProt
P11766
Other data
EC number
1.1.1.1
Locus
Chr. 4 q23
alcohol dehydrogenase 6
(class V)
Identifiers
Symbol
ADH6
Entrez
130
HUGO
255
OMIM
103735
RefSeq
NM_000672
UniProt
P28332
Other data
EC number
1.1.1.1
Locus
Chr. 4 q23
alcohol dehydrogenase 7
(class IV), μ or σ polypeptide
Identifiers
Symbol
ADH7
Entrez
131
HUGO
256
OMIM
600086
RefSeq
NM_000673
UniProt
P40394
Other data
EC number
1.1.1.1
Locus
Chr. 4 q23-q24
Yeast and bacteria[edit]
Unlike humans, yeast and bacteria (except lactic acid bacteria, and E. coli in certain conditions) do not ferment glucose to lactate. Instead, they ferment it to ethanol and CO2. The overall reaction can be seen below:
Glucose + 2 ADP + 2 Pi → 2 ethanol + 2 CO2 + 2 ATP + 2 H2O[24]
Alcohol Dehydrogenase
In yeast[25] and many bacteria, alcohol dehydrogenase plays an important part in fermentation: Pyruvate resulting from glycolysis is converted to acetaldehyde and carbon dioxide, and the acetaldehyde is then reduced to ethanol by an alcohol dehydrogenase called ADH1. The purpose of this latter step is the regeneration of NAD+, so that the energy-generating glycolysis can continue. Humans exploit this process to produce alcoholic beverages, by letting yeast ferment various fruits or grains. It is interesting to note that yeast can produce and consume their own alcohol.
The main alcohol dehydrogenase in yeast is larger than the human one, consisting of four rather than just two subunits. It also contains zinc at its catalytic site. Together with the zinc-containing alcohol dehydrogenases of animals and humans, these enzymes from yeasts and many bacteria form the family of "long-chain"-alcohol dehydrogenases.
Brewer's yeast also has another alcohol dehydrogenase, ADH2, which evolved out of a duplicate version of the chromosome containing the ADH1 gene. ADH2 is used by the yeast to convert ethanol back into acetaldehyde, and it is expressed only when sugar concentration is low. Having these two enzymes allows yeast to produce alcohol when sugar is plentiful (and this alcohol then kills off competing microbes), and then continue with the oxidation of the alcohol once the sugar, and competition, is gone.[26]
Plants[edit]
In plants, ADH catalyses the same reaction as in yeast and bacteria to ensure that there is a constant supply of NAD+. Maize has two versions of ADH - ADH1 and ADH2, Arabidopsis thaliana contains only one ADH gene. The structure of Arabidopsis ADH is 47%-conserved, relative to ADH from horse liver. Structurally and functionally important residues, such as the seven residues that provide ligands for the catalytic and noncatalytic zinc atoms, however, are conserved, suggesting that the enzymes have a similar structure.[27] ADH is constitutively expressed at low levels in the roots of young plants grown on agar. If the roots lack oxygen, the expression of ADH increases significantly.[28] Its expression is also increased in response to dehydration, to low temperatures, and to abscisic acid, and it plays an important role in fruit ripening, seedlings development, and pollen development.[29] Differences in the sequences of ADH in different species have been used to create phylogenies showing how closely related different species of plants are.[30] It is an ideal gene to use due to its convenient size (2–3 kb in length with a ~1000 nucleotide coding sequence) and low copy number.[29]
Iron-containing[edit]
Iron-containing alcohol dehydrogenase
bacillus stearothermophilus glycerol dehydrogenase complex with glycerol
Identifiers
Symbol
Fe-ADH
Pfam
PF00465
Pfam clan
CL0224
InterPro
IPR001670
PROSITE
PDOC00059
SCOP
1jqa
SUPERFAMILY
1jqa
[show]Available protein structures:
Pfam
structures
PDB
RCSB PDB; PDBe; PDBj
PDBsum
structure summary
A third family of alcohol dehydrogenases, unrelated to the above two, are iron-containing ones. They occur in bacteria and fungi. In comparison to enzymes the above families, these enzymes are oxygen-sensitive.[citation needed] Members of the iron-containing alcohol dehydrogenase family include:
Saccharomyces cerevisiae alcohol dehydrogenase 4 (gene ADH4)[31]
Zymomonas mobilis alcohol dehydrogenase 2 (gene adhB)[32]
Escherichia coli propanediol oxidoreductase EC 1.1.1.77 (gene fucO),[33] an enzyme involved in the metabolism of fucose and which also seems to contain ferrous ion(s).
Clostridium acetobutylicum NADPH- and NADH-dependent butanol dehydrogenases EC 1.1.1.- (genes adh1, bdhA and bdhB),[34] enzymes that have activity using butanol and ethanol as substrates.
E. coli adhE,[35] an iron-dependent enzyme that harbours three different activities: alcohol dehydrogenase, acetaldehyde dehydrogenase (acetylating) EC 1.2.1.10 and pyruvate-formate-lyase deactivase.
Bacterial glycerol dehydrogenase EC 1.1.1.6 (gene gldA or dhaD).[36]
Clostridium kluyveri NAD-dependent 4-hydroxybutyrate dehydrogenase (4hbd) EC 1.1.1.61
Citrobacter freundii and Klebsiella pneumoniae 1,3-propanediol dehydrogenase EC 1.1.1.202 (gene dhaT)
Bacillus methanolicus NAD-dependent methanol dehydrogenase EC 1.1.1.244[37]
E. coli and Salmonella typhimurium ethanolamine utilization protein eutG.
E. coli hypothetical protein yiaY.
Other types[edit]
A further class of alcohol dehydrogenases belongs to quinoenzymes and requires quinoid cofactors (e.g., pyrroloquinoline quinone, PQQ) as enzyme-bound electron acceptors. A typical example for this type of enzyme is methanol dehydrogenase of methylotrophic bacteria.
Applications[edit]
In biotransformation, alcohol dehydrogenases are often used for the synthesis of enantiomerically pure stereoisomers of chiral alcohols. Often, high chemo- and enantioselectivity can be achieved. One example is the alcohol dehydrogenase from Lactobacillus brevis (LbADH), which is described to be a versatile biocatalyst.[38] The high chemospecificity has been confirmed also in the case of substrates presenting two potential redox sites. For instance cinnamaldehyde presents both aliphatic double bond and aldehyde function. Unlike conventional catalysts, alcohol dehydrogenases are able to selectively act only on the latter, yielding exclusively cinnamyl alcohol.[39]
In fuel cells, alcohol dehydrogenases can be used to catalyze the breakdown of fuel for an ethanol fuel cell. Scientists at Saint Louis University have used carbon-supported alcohol dehydrogenase with poly(methylene green) as an anode, with a nafion membrane, to achieve about 50 μA/cm2.[40]
In 1949, E. Racker defined one unit of alcohol dehydrogenase activity as the amount that causes a change in optical density of 0.001 per minute under the standard conditions of assay.[41] Recently, the international definition of enzymatic unit (E.U.) has been more common: one unit of Alcohol Dehydrogenase will convert 1.0 µmole of ethanol to acetaldehyde per minute at pH 8.8 at 25 °C.[42]
Clinical significance[edit]
Alcoholism[edit]
There have been studies showing that ADH may have an influence on the dependence on ethanol metabolism in alcoholics. Researchers have tentatively detected a few genes to be associated with alcoholism. If the variants of these genes encode slower metabolizing forms of ADH2 and ADH3, there is increased risk of alcoholism. The studies have found that mutations of ADH2 and ADH3 are related to alcoholism in Northeast Asian populations. However, research continues in order to identify the genes and their influence on alcoholism.[43]
On the other hand, it seems that there have been mutations in ADH that have been naturally selected because they protect against alcoholism. It could be that they speed up the conversion of alcohol into acetaldehyde causing drinkers to feel unwell.[44][45]
Drug dependence[edit]
Drug dependence is another problem associated with ADH, which researchers think might be linked to alcoholism. One particular study suggests that drug dependence has seven ADH genes associated with it. These results may lead to treatments that target these specific genes. However, more research is necessary.[46]
Poisoning[edit]
Fomepizole, a drug that inhibits alcohol dehydrogenase, can be used in the setting of acute methanol[47] or ethylene glycol[48] toxicity. This prevents the conversion of methanol to its toxic metabolites, formic acid and formaldehyde.
See also[edit]
Alcohol dehydrogenase (NAD(P)+)
Aldehyde dehydrogenase
Oxidoreductase
Blood alcohol content for rates of metabolism
References[edit]
This article incorporates text from the public domain Pfam and InterPro IPR001670
Jump up ^ PDB: 1m6h; Sanghani PC, Robinson H, Bosron WF, Hurley TD (September 2002). "Human glutathione-dependent formaldehyde dehydrogenase. Structures of apo, binary, and inhibitory ternary complexes". Biochemistry. 41 (35): 10778–86. doi:10.1021/bi0257639. PMID 12196016.
Jump up ^ Gutheil WG, Holmquist B, Vallee BL (Jan 1992). "Purification, characterization, and partial sequence of the glutathione-dependent formaldehyde dehydrogenase from Escherichia coli: a class III alcohol dehydrogenase". Biochemistry. 31 (2): 475–81. doi:10.1021/bi00117a025. PMID 1731906.
^ Jump up to: a b Danielsson O, Jörnvall H (Oct 1992). ""Enzymogenesis": classical liver alcohol dehydrogenase origin from the glutathione-dependent formaldehyde dehydrogenase line". Proceedings of the National Academy of Sciences of the United States of America. 89 (19): 9247–51. doi:10.1073/pnas.89.19.9247. PMC 50103  . PMID 1409630.
^ Jump up to: a b Persson B, Hedlund J, Jörnvall H (Dec 2008). "Medium- and short-chain dehydrogenase/reductase gene and protein families : the MDR superfamily". Cellular and Molecular Life Sciences. 65 (24): 3879–94. doi:10.1007/s00018-008-8587-z. PMC 2792335  . PMID 19011751.
Jump up ^ Staab CA, Hellgren M, Höög JO (Dec 2008). "Medium- and short-chain dehydrogenase/reductase gene and protein families : Dual functions of alcohol dehydrogenase 3: implications with focus on formaldehyde dehydrogenase and S-nitrosoglutathione reductase activities". Cellular and Molecular Life Sciences. 65 (24): 3950–60. doi:10.1007/s00018-008-8592-2. PMID 19011746.
Jump up ^ Godoy L, Gonzàlez-Duarte R, Albalat R (2006). "S-Nitrosogluthathione reductase activity of amphioxus ADH3: insights into the nitric oxide metabolism". International Journal of Biological Sciences. 2 (3): 117–24. doi:10.7150/ijbs.2.117. PMC 1458435  . PMID 16763671.
^ Jump up to: a b c d Whitfield, John B. "ADH and ALDH genotypes in relation to alcohol metabolic rate and sensitivity" (PDF). Alcohol and Alcoholism. [permanent dead link]
^ Jump up to: a b c d Peng Y, Shi H, Qi XB, Xiao CJ, Zhong H, Ma RL, Su B (2010). "The ADH1B Arg47His polymorphism in east Asian populations and expansion of rice domestication in history". BMC Evolutionary Biology. 10: 15. doi:10.1186/1471-2148-10-15. PMC 2823730  . PMID 20089146.
Jump up ^ Eng, Mimi Y. (2007-01-01). Alcohol Research and Health. U.S. Government Printing Office. ISSN 1535-7414.
Jump up ^ Negelein E, Wulff HJ (1937). "Diphosphopyridinproteid ackohol, acetaldehyd". Biochem. Z. 293: 351.
Jump up ^ Theorell H, McKEE JS (Oct 1961). "Mechanism of action of liver alcohol dehydrogenase". Nature. 192 (4797): 47–50. doi:10.1038/192047a0. PMID 13920552.
Jump up ^ Jörnvall H, Harris JI (Apr 1970). "Horse liver alcohol dehydrogenase. On the primary structure of the ethanol-active isoenzyme". European Journal of Biochemistry / FEBS. 13 (3): 565–76. doi:10.1111/j.1432-1033.1970.tb00962.x. PMID 5462776.
Jump up ^ Brändén CI, Eklund H, Nordström B, Boiwe T, Söderlund G, Zeppezauer E, Ohlsson I, Akeson A (Aug 1973). "Structure of liver alcohol dehydrogenase at 2.9-angstrom resolution". Proceedings of the National Academy of Sciences of the United States of America. 70 (8): 2439–42. doi:10.1073/pnas.70.8.2439. PMC 433752  . PMID 4365379.
Jump up ^ Hellgren M (2009). Enzymatic studies of alcohol dehydrogenase by a combination of in vitro and in silico methods, Ph.D. thesis (PDF). Stockholm, Sweden: Karolinska Institutet. p. 70. ISBN 978-91-7409-567-8.
^ Jump up to: a b Sofer W, Martin PF (1987). "Analysis of alcohol dehydrogenase gene expression in Drosophila". Annual Review of Genetics. 21: 203–25. doi:10.1146/annurev.ge.21.120187.001223. PMID 3327463.
^ Jump up to: a b c Hammes-Schiffer S, Benkovic SJ (2006). "Relating protein motion to catalysis". Annual Review of Biochemistry. 75: 519–41. doi:10.1146/annurev.biochem.75.103004.142800. PMID 16756501.
Jump up ^ Brandt EG, Hellgren M, Brinck T, Bergman T, Edholm O (Feb 2009). "Molecular dynamics study of zinc binding to cysteines in a peptide mimic of the alcohol dehydrogenase structural zinc site" (PDF). Physical Chemistry Chemical Physics. 11 (6): 975–83. doi:10.1039/b815482a. PMID 19177216.
Jump up ^ Sultatos LG, Pastino GM, Rosenfeld CA, Flynn EJ (Mar 2004). "Incorporation of the genetic control of alcohol dehydrogenase into a physiologically based pharmacokinetic model for ethanol in humans". Toxicological Sciences. 78 (1): 20–31. doi:10.1093/toxsci/kfh057. PMID 14718645.
Jump up ^ Farrés J, Moreno A, Crosas B, Peralba JM, Allali-Hassani A, Hjelmqvist L, Jörnvall H, Parés X (Sep 1994). "Alcohol dehydrogenase of class IV (sigma sigma-ADH) from human stomach. cDNA sequence and structure/function relationships". European Journal of Biochemistry / FEBS. 224 (2): 549–57. doi:10.1111/j.1432-1033.1994.00549.x. PMID 7925371.
Jump up ^ Kovacs B, Stöppler MC. "Alcohol and Nutrition". MedicineNet, Inc. Archived from the original on 23 June 2011. Retrieved 2011-06-07.
Jump up ^ Duester G (Sep 2008). "Retinoic acid synthesis and signaling during early organogenesis". Cell. 134 (6): 921–31. doi:10.1016/j.cell.2008.09.002. PMC 2632951  . PMID 18805086.
Jump up ^ Hellgren M, Strömberg P, Gallego O, Martras S, Farrés J, Persson B, Parés X, Höög JO (Feb 2007). "Alcohol dehydrogenase 2 is a major hepatic enzyme for human retinol metabolism". Cellular and Molecular Life Sciences. 64 (4): 498–505. doi:10.1007/s00018-007-6449-8. PMID 17279314.
Jump up ^ Parlesak A, Billinger MH, Bode C, Bode JC (2002). "Gastric alcohol dehydrogenase activity in man: influence of gender, age, alcohol consumption and smoking in a caucasian population". Alcohol and Alcoholism. 37 (4): 388–93. doi:10.1093/alcalc/37.4.388. PMID 12107043.
Jump up ^ Cox, Michael; Nelson, David R.; Lehninger, Albert L (2005). Lehninger Principles of Biochemistry. San Francisco: W. H. Freeman. p. 180. ISBN 0-7167-4339-6.
Jump up ^ Leskovac V, Trivić S, Pericin D (Dec 2002). "The three zinc-containing alcohol dehydrogenases from baker's yeast, Saccharomyces cerevisiae". FEMS Yeast Research. 2 (4): 481–94. doi:10.1111/j.1567-1364.2002.tb00116.x. PMID 12702265.
Jump up ^ Coghlan A (23 December 2006). "Festive special: The brewer's tale - life". New Scientist. Archived from the original on 15 September 2008. Retrieved 2009-04-27.
Jump up ^ Chang C, Meyerowitz EM (Mar 1986). "Molecular cloning and DNA sequence of the Arabidopsis thaliana alcohol dehydrogenase gene". Proceedings of the National Academy of Sciences of the United States of America. 83 (5): 1408–12. doi:10.1073/pnas.83.5.1408. PMC 323085  . PMID 2937058.
Jump up ^ Chung HJ, Ferl RJ (Oct 1999). "Arabidopsis alcohol dehydrogenase expression in both shoots and roots is conditioned by root growth environment". Plant Physiology. 121 (2): 429–36. doi:10.1104/pp.121.2.429. PMC 59405  . PMID 10517834.
^ Jump up to: a b Thompson CE, Fernandes CL, de Souza ON, de Freitas LB, Salzano FM (May 2010). "Evaluation of the impact of functional diversification on Poaceae, Brassicaceae, Fabaceae, and Pinaceae alcohol dehydrogenase enzymes". Journal of Molecular Modeling. 16 (5): 919–28. doi:10.1007/s00894-009-0576-0. PMID 19834749.
Jump up ^ Järvinen P, Palmé A, Orlando Morales L, Lännenpää M, Keinänen M, Sopanen T, Lascoux M (Nov 2004). "Phylogenetic relationships of Betula species (Betulaceae) based on nuclear ADH and chloroplast matK sequences". American Journal of Botany. Amjbot.org. 91 (11): 1834–45. doi:10.3732/ajb.91.11.1834. PMID 21652331. Archived from the original on 26 May 2010.
Jump up ^ Williamson VM, Paquin CE (Sep 1987). "Homology of Saccharomyces cerevisiae ADH4 to an iron-activated alcohol dehydrogenase from Zymomonas mobilis". Molecular & General Genetics. 209 (2): 374–81. doi:10.1007/bf00329668. PMID 2823079.
Jump up ^ Conway T, Sewell GW, Osman YA, Ingram LO (Jun 1987). "Cloning and sequencing of the alcohol dehydrogenase II gene from Zymomonas mobilis". Journal of Bacteriology. 169 (6): 2591–7. PMC 212129  . PMID 3584063.
Jump up ^ Conway T, Ingram LO (Jul 1989). "Similarity of Escherichia coli propanediol oxidoreductase (fucO product) and an unusual alcohol dehydrogenase from Zymomonas mobilis and Saccharomyces cerevisiae". Journal of Bacteriology. 171 (7): 3754–9. PMC 210121  . PMID 2661535.
Jump up ^ Walter KA, Bennett GN, Papoutsakis ET (Nov 1992). "Molecular characterization of two Clostridium acetobutylicum ATCC 824 butanol dehydrogenase isozyme genes". Journal of Bacteriology. 174 (22): 7149–58. PMC 207405  . PMID 1385386.
Jump up ^ Kessler D, Leibrecht I, Knappe J (Apr 1991). "Pyruvate-formate-lyase-deactivase and acetyl-CoA reductase activities of Escherichia coli reside on a polymeric protein particle encoded by adhE". FEBS Letters. 281 (1-2): 59–63. doi:10.1016/0014-5793(91)80358-A. PMID 2015910.
Jump up ^ Truniger V, Boos W (Mar 1994). "Mapping and cloning of gldA, the structural gene of the Escherichia coli glycerol dehydrogenase". Journal of Bacteriology. 176 (6): 1796–800. PMC 205274  . PMID 8132480.
Jump up ^ de Vries GE, Arfman N, Terpstra P, Dijkhuizen L (Aug 1992). "Cloning, expression, and sequence analysis of the Bacillus methanolicus C1 methanol dehydrogenase gene". Journal of Bacteriology. 174 (16): 5346–53. PMC 206372  . PMID 1644761.
Jump up ^ Leuchs S, Greiner L (2011). "Alcohol dehydrogenase from Lactobacillus brevis: A versatile catalyst for enenatioselective reduction" (PDF). CABEQ: 267–281. [permanent dead link]
Jump up ^ Zucca P, Littarru M, Rescigno A, Sanjust E (May 2009). "Cofactor recycling for selective enzymatic biotransformation of cinnamaldehyde to cinnamyl alcohol". Bioscience, Biotechnology, and Biochemistry. 73 (5): 1224–6. doi:10.1271/bbb.90025. PMID 19420690.
Jump up ^ Moore CM, Minteer SD, Martin RS (Feb 2005). "Microchip-based ethanol/oxygen biofuel cell". Lab on a Chip. 5 (2): 218–25. doi:10.1039/b412719f. PMID 15672138.
Jump up ^ Racker E (1950). "Crystalline alcohol dehydrogenase from baker's yeast". J. Biol. Chem. 184 (1): 313–9. PMID 15443900.
Jump up ^ "Enzymatic Assay of Alcohol Dehydrogenase (EC 1.1.1.1)". Sigma Aldrich. Retrieved 13 July 2015.
Jump up ^ Sher KJ, Grekin ER, Williams NA (2005). "The development of alcohol use disorders". Annual Review of Clinical Psychology. 1: 493–523. doi:10.1146/annurev.clinpsy.1.102803.144107. PMID 17716097.
Jump up ^ Kelsey Elizabeth Johnson & Benjamin F. Voight (Feb 2018). "Patterns of shared signatures of recent positive selection across human populations". Nature Ecology & Evolution. doi:10.1038/s41559-018-0478-6.
Jump up ^ Andy Coghlan (Feb 24, 2018). "Evolution may stop us drinking alcohol". New Scientist.
Jump up ^ Luo X, Kranzler HR, Zuo L, Wang S, Schork NJ, Gelernter J (Feb 2007). "Multiple ADH genes modulate risk for drug dependence in both African- and European-Americans". Human Molecular Genetics. 16 (4): 380–90. doi:10.1093/hmg/ddl460. PMC 1853246  . PMID 17185388.
Jump up ^ International Programme on Chemical Safety (IPCS): Methanol (PIM 335), [1], retrieved on March 1, 2008
Jump up ^ Velez LI, Shepherd G, Lee YC, Keyes DC (2007). "Ethylene glycol ingestion treated only with fomepizole". J Med Toxicol. 3 (3): 125–8. doi:10.1007/BF03160922. PMC 3550067  . PMID 18072148.
External links[edit]
Wikimedia Commons has media related to Alcohol dehydrogenase.
PDBsum has links to three-dimensional structures of various alcohol dehydrogenases contained in the Protein Data Bank
ExPASy contains links to the alcohol dehydrogenase sequences in Swiss-Prot, to a Medline literature search about the enzyme, and to entries in other databases.
[show]
v
t
e
Oxidoreductases: alcohol oxidoreductases (EC 1.1)
1.1.1: NAD/NADP acceptor
3-hydroxyacyl-CoA dehydrogenase
3-hydroxybutyryl-CoA dehydrogenase
Alcohol dehydrogenase
Aldo-keto reductase
1A1
1B1
1B10
1C1
1C3
1C4
7A2
Aldose reductase
Beta-Ketoacyl ACP reductase
Carbohydrate dehydrogenases
Carnitine dehydrogenase
D-malate dehydrogenase (decarboxylating)
DXP reductoisomerase
Glucose-6-phosphate dehydrogenase
Glycerol-3-phosphate dehydrogenase
HMG-CoA reductase
IMP dehydrogenase
Isocitrate dehydrogenase
Lactate dehydrogenase
L-threonine dehydrogenase
L-xylulose reductase
Malate dehydrogenase
Malate dehydrogenase (decarboxylating)
Malate dehydrogenase (NADP+)
Malate dehydrogenase (oxaloacetate-decarboxylating)
Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)
Phosphogluconate dehydrogenase
Sorbitol dehydrogenase
Hydroxysteroid dehydrogenase: 3β
3β-HSD
NSDHL
11β
11β-HSD1
11β-HSD2
17β
1.1.2: cytochrome acceptor
D-lactate dehydrogenase (cytochrome)
D-lactate dehydrogenase (cytochrome c-553)
Mannitol dehydrogenase (cytochrome)
1.1.3: oxygen acceptor
Glucose oxidase
L-gulonolactone oxidase
Xanthine oxidase
1.1.4: disulfide as acceptor
Vitamin K epoxide reductase
Vitamin-K-epoxide reductase (warfarin-insensitive)
1.1.5: quinone/similar acceptor
Malate dehydrogenase (quinone)
Quinoprotein glucose dehydrogenase
1.1.99: other acceptors
Choline dehydrogenase
L2HGDH
[show]
v
t
e
Enzymes
Activity
Active site
Binding site
Catalytic triad
Oxyanion hole
Enzyme promiscuity
Catalytically perfect enzyme
Coenzyme
Cofactor
Enzyme catalysis
Regulation
Allosteric regulation
Cooperativity
Enzyme inhibitor
Classification
EC number
Enzyme superfamily
Enzyme family
List of enzymes
Kinetics
Enzyme kinetics
Eadie–Hofstee diagram
Hanes–Woolf plot
Lineweaver–Burk plot
Michaelis–Menten kinetics
Types
EC1 Oxidoreductases (list)
EC2 Transferases (list)
EC3 Hydrolases (list)
EC4 Lyases (list)
EC5 Isomerases (list)
EC6 Ligases (list)
Molecular and Cellular Biology portal
Retrieved from "https://en.wikipedia.org/w/index.php?title=Alcohol_dehydrogenase&oldid=837427019"
Categories:
Genes on human chromosome 4
Protein families
EC 1.1.1
NADH-dependent enzymes
Iron enzymes
Zinc enzymes
Alcohol and health
Hidden categories:
All articles with dead external links
Articles with dead external links from June 2017
Articles with permanently dead external links
Use dmy dates from July 2013
Protein pages needing a picture
All articles with unsourced statements
Articles with unsourced statements from August 2011
Navigation menu
Personal tools
Not logged in
Talk
Contributions
Create account
Log in
Namespaces
Article
Talk
Variants
Views
Read
Edit
View history
More
Search
Navigation
Main page
Contents
Featured content
Current events
Random article
Donate to Wikipedia
Wikipedia store
Interaction
Help
About Wikipedia
Community portal
Recent changes
Contact page
Tools
What links here
Related changes
Upload file
Special pages
Permanent link
Page information
Wikidata item
Cite this page
Print/export
Create a book
Download as PDF
Printable version
In other projects
Wikimedia Commons
Languages
العربية
Български
Bosanski
Català
Čeština
Dansk
Deutsch
Español
Français
한국어
Bahasa Indonesia
Italiano
Македонски
Nederlands
日本語
Polski
Português
Русский
Slovenčina
Slovenščina
Српски / srpski
Srpskohrvatski / српскохрватски
Suomi
Svenska
中文
16 more
Edit links
This page was last edited on 20 April 2018, at 19:14.
Text is available under the Creative Commons Attribution-ShareAlike License; additional terms may apply. By using this site, you agree to the Terms of Use and Privacy Policy. Wikipedia® is a registered trademark of the Wikimedia Foundation, Inc., a non-profit organization.
Privacy policy
About Wikipedia
Disclaimers
Contact Wikipedia
Developers
Cookie statement
Mobile view
Enable previews

key: html

type: local

value: div

attrs: id class

values: mw-page-base noprint

values: mw-head-base noprint

value: a

attrs: id class lang

values: firstHeading firstHeading en

values: siteSub noprint

values: jump-to-nav mw-jump

value: th

attrs: colspan style

value: tr

value: img

attrs: alt src width height srcset data-file-width data-file-height

attrs: href class title

values:
/wiki/Protein_crystallography
mw-redirect
Protein crystallography

attrs: href title

value: sup

value: td

attrs: scope style

values:
row
background-color: #e7dcc3

values:
/wiki/CAS_registry_number
mw-redirect
CAS registry number

values:
nofollow
external text
http://www.expasy.org/enzyme/1.1.1.1

values:
/wiki/PRIAM_enzyme_specific_profiles
mw-redirect
PRIAM enzyme specific profiles

values:
/wiki/Gene_Ontology
mw-redirect
Gene Ontology

values:
nofollow
external text
//www.ebi.ac.uk/QuickGO/term/GO:0004022

values: background-color: #e7dcc3; border:#fafafa 2px solid; border-width:3px 2px 0 0;

values: background-color: #eee; border:#fafafa 2px solid; border-width:3px 0 0 2px;

values: National Center for Biotechnology Information

values: width:22em;float:none; clear:none; margin:0; border-width:0; border-collapse:collapse; text-align:left; width:100%

values:
nofollow
external text
https://enzyme.expasy.org/EC/1.1.1.1

values:
/wiki/Fermentation_(food)
mw-redirect
Fermentation (food)

values:
/wiki/Single_nucleotide_polymorphism
mw-redirect
Single nucleotide polymorphism

values:
/wiki/Darwinian_evolution
mw-redirect
Darwinian evolution

attrs: alt src width height class srcset data-file-width data-file-height

values: Edit section: Mechanism of action in humans

values:
/wiki/Hydrogen_bonds
mw-redirect
Hydrogen bonds

values:
/wiki/Alcoholic_beverage
mw-redirect
Alcoholic beverage

values:
/wiki/Digestive_tract
mw-redirect
Digestive tract

values:
nofollow
external text
https://www.omim.org/103700

values:
nofollow
external text
https://www.uniprot.org/uniprot/P07327

values:
/wiki/Chromosome_4_(human)
mw-redirect
Chromosome 4 (human)

values:
nofollow
external text
https://www.omim.org/103720

values:
nofollow
external text
https://www.uniprot.org/uniprot/P00325

values:
nofollow
external text
https://www.omim.org/103730

values:
nofollow
external text
https://www.uniprot.org/uniprot/P00326

values:
nofollow
external text
https://www.omim.org/103740

values:
nofollow
external text
https://www.uniprot.org/uniprot/P08319

values:
nofollow
external text
https://www.omim.org/103710

values:
nofollow
external text
https://www.uniprot.org/uniprot/P11766

values:
nofollow
external text
https://www.omim.org/103735

values:
nofollow
external text
https://www.uniprot.org/uniprot/P28332

values:
nofollow
external text
https://www.omim.org/600086

values:
nofollow
external text
https://www.uniprot.org/uniprot/P40394

values:
/wiki/Lactic_acid_bacteria
mw-redirect
Lactic acid bacteria

values:
/wiki/Brewer%27s_yeast
mw-redirect
Brewer's yeast

values:
nofollow
external text
https://www.yeastgenome.org/locus/adh1

values:
nofollow
external text
https://www.yeastgenome.org/locus/adh2

values:
nofollow
external text
http://pfam.xfam.org/family?acc=PF00465

values:
nofollow
external text
http://pfam.xfam.org/clan/CL0224

values: This claim needs references to reliable sources. (August 2011)

values:
noprint Inline-Template Template-Fact
white-space:nowrap;

values:
nofollow
external text
https://enzyme.expasy.org/EC/1.1.1.77

values:
nofollow
external text
https://enzyme.expasy.org/EC/1.1.1.-

values:
/wiki/Substrate_(biochemistry)
mw-redirect
Substrate (biochemistry)

values:
nofollow
external text
https://enzyme.expasy.org/EC/1.2.1.10

values:
nofollow
external text
https://enzyme.expasy.org/EC/1.1.1.6

values:
/wiki/4-hydroxybutyrate_dehydrogenase
mw-redirect
4-hydroxybutyrate dehydrogenase

values:
nofollow
external text
https://enzyme.expasy.org/EC/1.1.1.61

values:
nofollow
external text
https://enzyme.expasy.org/EC/1.1.1.202

values:
nofollow
external text
https://enzyme.expasy.org/EC/1.1.1.244

values:
/wiki/Salmonella_typhimurium
mw-redirect
Salmonella typhimurium

values:
/wiki/Optical_density
mw-redirect
Optical density

values:
nofollow
external text
//doi.org/10.1021%2Fbi0257639

values:
/wiki/PubMed_Identifier
mw-redirect
PubMed Identifier

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/12196016

values:
nofollow
external text
//doi.org/10.1021%2Fbi00117a025

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/1731906

values:
nofollow
external text
//doi.org/10.1073%2Fpnas.89.19.9247

attrs: alt src title width height srcset data-file-width data-file-height

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/1409630

values:
nofollow
external text
//doi.org/10.1007%2Fs00018-008-8587-z

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/19011751

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/19011746

values:
nofollow
external text
//doi.org/10.7150%2Fijbs.2.117

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/16763671

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/20089146

values:
nofollow
external text
//www.worldcat.org/issn/1535-7414

values:
nofollow
external text
//doi.org/10.1038%2F192047a0

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/13920552

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/5462776

values:
nofollow
external text
//doi.org/10.1073%2Fpnas.70.8.2439

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/4365379

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/3327463

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/16756501

values:
nofollow
external text
//doi.org/10.1039%2Fb815482a

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/19177216

values:
nofollow
external text
//doi.org/10.1093%2Ftoxsci%2Fkfh057

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/14718645

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/7925371

values:
nofollow
external text
//doi.org/10.1016%2Fj.cell.2008.09.002

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/18805086

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/17279314

values:
nofollow
external text
//doi.org/10.1093%2Falcalc%2F37.4.388

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/12107043

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/12702265

values:
nofollow
external text
//doi.org/10.1073%2Fpnas.83.5.1408

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/2937058

values:
nofollow
external text
//doi.org/10.1104%2Fpp.121.2.429

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/10517834

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/19834749

values:
nofollow
external text
//doi.org/10.3732%2Fajb.91.11.1834

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/21652331

values:
nofollow
external text
//doi.org/10.1007%2Fbf00329668

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/2823079

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/3584063

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/2661535

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/1385386

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/2015910

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/8132480

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/1644761

values:
nofollow
external text
//doi.org/10.1271%2Fbbb.90025

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/19420690

values:
nofollow
external text
//doi.org/10.1039%2Fb412719f

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/15672138

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/15443900

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/17716097

values:
nofollow
external text
//doi.org/10.1093%2Fhmg%2Fddl460

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/17185388

values:
nofollow
external text
//doi.org/10.1007%2FBF03160922

values:
nofollow
external text
//www.ncbi.nlm.nih.gov/pubmed/18072148

values: -moz-column-width: 33em; -webkit-column-width: 33em; column-width: 33em; list-style-type: decimal;

values: Nicotinamide adenine dinucleotide phosphate

values:
/wiki/Beta-Ketoacyl_ACP_reductase
mw-redirect
Beta-Ketoacyl ACP reductase

values:
/wiki/Carnitine_dehydrogenase
mw-redirect
Carnitine dehydrogenase

values: Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)

values: Corticosteroid 11-beta-dehydrogenase isozyme 2

values: D-lactate dehydrogenase (cytochrome c-553)

values: nowraplinks collapsible autocollapse navbox-inner

values:
/wiki/Catalytically_perfect_enzyme
mw-redirect
Catalytically perfect enzyme

values:
/wiki/Enzyme_superfamily
mw-redirect
Enzyme superfamily

values:
/wiki/Enzyme_family
mw-redirect
Enzyme family

values: Category:All articles with dead external links

values: Category:Articles with dead external links from June 2017

values: Category:Articles with permanently dead external links

values: Category:Protein pages needing a picture

values: Category:All articles with unsourced statements

values: Category:Articles with unsourced statements from August 2011

values: Discussion about edits from this IP address [ctrl-alt-n]

values: A list of edits made from this IP address [ctrl-alt-y]

values: You are encouraged to create an account and log in; however, it is not mandatory

values: You're encouraged to log in; however, it's not mandatory. [ctrl-alt-o]

values:
/wiki/Alcohol_dehydrogenase
View the content page [ctrl-alt-c]
c

values: Discussion about the content page [ctrl-alt-t]

values: p-namespaces navigation vectorTabs p-namespaces-label

values:
p-variants
navigation
vectorMenu emptyPortlet
p-variants-label

values: Past revisions of this page [ctrl-alt-h]

values: p-views navigation vectorTabs p-views-label

values:
p-cactions
navigation
vectorMenu emptyPortlet
p-cactions-label

values:
mw-wiki-logo
/wiki/Main_Page
Visit the main page

values:
/wiki/Main_Page
Visit the main page [ctrl-alt-z]
z

values: Featured content – the best of Wikipedia

values: Find background information on current events

values:
/wiki/Special:Random
Load a random article [ctrl-alt-x]
x

values: portal navigation p-navigation p-navigation-label

values: Guidance on how to use and edit Wikipedia

values: About the project, what you can do, where to find things

values: A list of recent changes in the wiki [ctrl-alt-r]

values: portal navigation p-interaction p-interaction-label

values: List of all English Wikipedia pages containing links to this page [ctrl-alt-j]

values: Recent changes in pages linked from this page [ctrl-alt-k]

values:
/wiki/Wikipedia:File_Upload_Wizard
Upload files [ctrl-alt-u]
u

values: A list of all special pages [ctrl-alt-q]

values: Permanent link to this revision of the page

values: Link to connected data repository item [ctrl-alt-g]

values: Printable version of this page [ctrl-alt-p]

values: portal navigation p-wikibase-otherprojects p-wikibase-otherprojects-label

values: نازعة هيدروجين الكحول – Arabic

values: Алкохолдехидрогеназа – Bulgarian

values:
interlanguage-link interwiki-bg
display: none;

values:
interlanguage-link interwiki-bs
display: none;

values:
interlanguage-link interwiki-ca
display: none;

values:
interlanguage-link interwiki-cs
display: none;

values:
interlanguage-link interwiki-da
display: none;

values: 알코올 탈수소효소 – Korean

values:
interlanguage-link interwiki-ko
display: none;

values:
interlanguage-link interwiki-it
display: none;

values: Алкохол дехидрогеназа – Macedonian

values:
interlanguage-link interwiki-mk
display: none;

values:
interlanguage-link interwiki-nl
display: none;

values: アルコールデヒドロゲナーゼ – Japanese

values: Алкогольдегидрогеназа – Russian

values:
interlanguage-link interwiki-sk
display: none;

values:
interlanguage-link interwiki-sl
display: none;

values: Alkohol dehidrogenaza (NADP+) – Serbo-Croatian

values: /static/images/wikimedia-button-1.5x.png 1.5x, /static/images/wikimedia-button-2x.png 2x

values: /static/images/poweredby_mediawiki_132x47.png 1.5x, /static/images/poweredby_mediawiki_176x62.png 2x

values:
suggestions
display: none; font-size: 13px;

values: mediawiki ltr sitedir-ltr mw-hide-empty-elt ns-0 ns-subject page-Alcohol_dehydrogenase rootpage-Alcohol_dehydrogenase skin-vector action-view