The scientific suffix -ase indicates the presence of what type of protein?
"accession codes , , and . Glutamin-(asparagin-)ase In enzymology, a glutamin-(asparagin-)ase () is an enzyme that catalyzes the chemical reaction Thus, the two substrates of this enzyme are L-glutamine and HO, whereas its two products are L-glutamate and NH. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is L-glutamine(L-asparagine) amidohydrolase. This enzyme participates in 4 metabolic pathways: glutamate metabolism, alanine and aspartate metabolism, d-glutamine and d-glutamate metabolism, and nitrogen metabolism. As of late 2007, 3 structures have been solved for"
"-ose The suffix -ose ( or ) is used in biochemistry to form the names of sugars. This Latin suffix means ""full of"", ""abounding in"", ""given to"", or ""like"". Numerous systems exist to name specific sugars more descriptively. Monosaccharides, the simplest sugars, may be named according to the number of carbon atoms in each molecule of the sugar: pentose is a five-carbon monosaccharide, and hexose is a six-carbon monosaccharide. Aldehyde monosaccharides may be called aldoses; ketone monosaccharides may be called ketoses. Larger sugars such as disaccharides and polysaccharides can be named to reflect their qualities. Lactose, a disaccharide found in"
"structure and protein function. According to a 2018 article in ""The Guardian"", a study found that decreasing levels of asparagine ""dramatically"" reduced the spread of breast cancer in laboratory mice. The article noted that similar studies had not been conducted in humans. Asparagine Asparagine (symbol Asn or N), is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated −NH form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO form under biological conditions), and a side chain carboxamide, classifying it as a polar (at"
"Protease A protease (also called a peptidase or proteinase) is an enzyme that helps proteolysis: protein catabolism by hydrolysis of peptide bonds. Proteases have evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms. Proteases can be found in Animalia, Plantae, Fungi, Bacteria, Archaea and viruses. Proteases can be classified into seven broad groups: Proteases were first grouped into 84 families according to their evolutionary relationship in 1993, and classified under four catalytic types: serine, cysteine, aspartic, and metallo proteases. The threonine and glutamic-acid proteases were not described until 1995 and 2004"
"it appears in and the accent of the speaker. In a few words (for example, ""quinine"" and ""strychnine""), the sound is normal in some accents. ""Gasoline"" ends with ; ""glycerine"" more often with than with . The suffix ""-in"" () is etymologically related and overlaps in usage with ""-ine"". Many proteins and lipids have names ending with ""-in"": for example, the enzymes pepsin and trypsin, the hormones insulin and gastrin, and the lipids stearin (stearine) and olein. -ine -ine is a suffix used in chemistry to denote two kinds of substance. The first is a chemically basic and alkaloidal substance."
"milk, gets its name from the Latin word for milk combined with the sugar suffix; its name means ""milk sugar"". The polysaccharide that makes up plant starch is named amylose, or ""starch sugar""; see amyl. There are these theories about the origin of the ""-ose"" suffix:- -ose The suffix -ose ( or ) is used in biochemistry to form the names of sugars. This Latin suffix means ""full of"", ""abounding in"", ""given to"", or ""like"". Numerous systems exist to name specific sugars more descriptively. Monosaccharides, the simplest sugars, may be named according to the number of carbon atoms in each"
"(short form ""ase"") found 45 kb 3′ of ""l(1)sc"". It is a 2.8 kb gene encoding a 486 aa protein of 53.2 kDa. Achaete-scute complex The ""achaete-scute"" complex (""AS-C"") is a group of four genes (""achaete"", ""scute"", ""lethal of scute"", and ""asense"") in the fruit fly ""Drosophila melanogaster"". These genes encode basic helix-loop-helix transcription factors that have been best studied in their regulation of nervous system development. Because of their role in specifying neuroblast fate, the genes of the ""AS-C"" are called proneural genes. However, the ""AS-C"" has non-proneural functions, such as specifying muscle and gut progenitors. Homologues of ""AS-C"""
"essential proteins. The CAS/CSE family of proteins consist of two domains. An N-terminal Cse1 domain, which contains HEAT repeats, and a C-terminal domain. CAS/CSE protein family In molecular biology, the CAS/CSE protein family is a family of proteins which includes mammalian cellular apoptosis susceptibility (CAS) proteins and yeast chromosome-segregation protein, CSE1. CAS is involved in both cellular apoptosis and proliferation. Apoptosis is inhibited in CAS-depleted cells, while the expression of CAS correlates to the degree of cellular proliferation. Like CSE1, it is essential for the mitotic checkpoint in the cell cycle (CAS depletion blocks the cell in the G2 phase),"
"Alanine Alanine (symbol Ala or A) is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated form, −NH, under biological conditions), an α-carboxylic acid group (which is in the deprotonated form, −COO, under biological conditions), and a side chain methyl group, making it a nonpolar, aliphatic amino acid. It is non-essential in humans: because the body can synthesize it, it does not need to be present in the diet. It is encoded by all codons starting with GC (GCU, GCC, GCA, and GCG). The -isomer of alanine (left-handed)"
"Casein Casein ( ""KAY-see-in"", from Latin ""caseus"" ""cheese"") is a family of related phosphoproteins (αS1, αS2, β, κ). These proteins are commonly found in mammalian milk, comprising c. 80% of the proteins in cow's milk and between 20% and 45% of the proteins in human milk.The j Casein has a wide variety of uses, from being a major component of cheese, to use as a food additive. The most common form of casein is sodium caseinate. As a food source, casein supplies amino acids, carbohydrates, and two essential elements, calcium and phosphorus. Casein contains a high number of proline residues,"
"Amino acid kinase In molecular biology, the amino acid kinase domain is a protein domain. It is found in protein kinases with various specificities, including the aspartate, glutamate and uridylate kinase families. In prokaryotes and plants the synthesis of the essential amino acids lysine and threonine is predominantly regulated by feed-back inhibition of aspartate kinase (AK) and dihydrodipicolinate synthase (DHPS). In ""Escherichia coli"", thrA, metLM, and lysC encode aspartokinase isozymes that show feedback inhibition by threonine, methionine, and lysine, respectively. The lysine-sensitive isoenzyme of aspartate kinase from spinach leaves has a subunit composition of 4 large and 4 small subunits."
"acids whose names end to the suffix ""-ous"". On the other hand, the suffix ""-ate"" occurs in names of anions and salts derived from acids whose names end to the suffix ""-ic"". Prefixes ""hypo-"" and ""per-"" occur in the name of anions and salts; for example the ion is called ""perchlorate"". In a few cases, the prefixes ""ortho-"" and ""para-"" occur in names of some oxyacids and their derivative anions. In such cases, the ""para-"" acid is what can be thought as remaining of the ""ortho-"" acid if a water molecule is separated from the ""ortho-"" acid molecule. For example,"
"Acetolactate synthase The acetolactate synthase (ALS) enzyme (also known as acetohydroxy acid synthase, or AHAS) is a protein found in plants and micro-organisms. ALS catalyzes the first step in the synthesis of the branched-chain amino acids (valine, leucine, and isoleucine). It is a human protein of yet unknown function, sharing some sequence similarity with bacterial ALS, and is encoded by the ILVBL gene. Human ILVBL gene has 17 exons resides on chromosome 19 at q13.1. Acetolactase is a protein consisting of 590 residues. These residues are classified into three separate subunits. The units are d1yhya1, d1yhya2, and d1yhya3. This is"
"the protease inhibitors they contain have been denatured. Protease A protease (also called a peptidase or proteinase) is an enzyme that helps proteolysis: protein catabolism by hydrolysis of peptide bonds. Proteases have evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms. Proteases can be found in Animalia, Plantae, Fungi, Bacteria, Archaea and viruses. Proteases can be classified into seven broad groups: Proteases were first grouped into 84 families according to their evolutionary relationship in 1993, and classified under four catalytic types: serine, cysteine, aspartic, and metallo proteases. The threonine and glutamic-acid"
"occasions. The ""β"" (beta) refers to the nitrogen's position on the second carbon in the ring. ""Lactam"" is a portmanteau of ""lactone"" (from the Latin ""lactis"", ""milk"", since lactic acid was isolated from soured milk) and ""amide"". The suffix ""-ase"", indicating an enzyme, is derived from ""diastase"" (from the Greek ""diastasis"", ""separation""), the first enzyme discovered in 1833 by Payen and Persoz. Beta-lactamase Beta-lactamases are enzymes () produced by bacteria that provide multi-resistance to β-lactam antibiotics such as penicillins, cephalosporins, cephamycins, and carbapenems (ertapenem), although carbapenems are relatively resistant to beta-lactamase. Beta-lactamase provides antibiotic resistance by breaking the antibiotics' structure."
"enzyme, where catalysis occurs, and is preserved in all superfamilies of serine protease enzymes. The triad is a coordinated structure consisting of three amino acids: His 57, Ser 195 (hence the name ""serine protease"") and Asp 102. These three key amino acids each play an essential role in the cleaving ability of the proteases. While the amino acid members of the triad are located far from one another on the sequence of the protein, due to folding, they will be very close to one another in the heart of the enzyme. The particular geometry of the triad members are highly"
"Aspartate—tRNA(Asn) ligase Aspartate---tRNAAsn ligase (, ""nondiscriminating aspartyl-tRNA synthetase"") is an enzyme with systematic name ""L-aspartate:tRNAAsx ligase (AMP-forming)"". This enzyme catalyses the following chemical reaction The 3 substrates of this enzyme are ATP, L-asparagine, and tRNAAsx, whereas its 3 products are AMP, diphosphate, and asparaginyl-tRNAAsx. When this enzyme acts on tRNAAsp, it catalyses the same reaction as EC 6.1.1.12, aspartate---tRNA ligase. It has, however, diminished discrimination, so that it can also form aspartyl-tRNAAsn. This relaxation of specificity has been found to result from the absence of a loop in the tRNA that specifically recognizes the third position of the anticodon [1]."
"Form 1 beginning at residue Ile 54 and Form 2 at Thr 57. Cathepsin E Cathepsin E is an enzyme () that in humans is encoded by the ""CTSE"" gene. The enzyme is also known as ""slow-moving proteinase"", ""erythrocyte membrane aspartic proteinase"", ""SMP"", ""EMAP"", ""non-pepsin proteinase"", ""cathepsin D-like acid proteinase"", ""cathepsin E-like acid proteinase"", ""cathepsin D-type proteinase"") is an enzyme. Cathepsin E is a protease found in animals, as well as various other organisms, that belongs to the aspartic protease group. In humans it is encoded by the CTSE gene located at 1q32 on chromosome 1. It is an intracellular"
"Asparagine Asparagine (symbol Asn or N), is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated −NH form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO form under biological conditions), and a side chain carboxamide, classifying it as a polar (at physiological pH), aliphatic amino acid. It is non-essential in humans, meaning the body can synthesize it. It is encoded by the codons AAU and AAC. A reaction between asparagine and reducing sugars or other source of carbonyls produces acrylamide in food when"
"the dangers of drawing conclusions from correlations identified in epidemiological studies and the dangers of not reviewing all the evidence at hand. A small fraction of the population is allergic to casein. Casein Casein ( ""KAY-see-in"", from Latin ""caseus"" ""cheese"") is a family of related phosphoproteins (αS1, αS2, β, κ). These proteins are commonly found in mammalian milk, comprising c. 80% of the proteins in cow's milk and between 20% and 45% of the proteins in human milk.The j Casein has a wide variety of uses, from being a major component of cheese, to use as a food additive. The"
"regulatory mechanism of nitrogen and carbon storage and utilization. Amino acid kinase In molecular biology, the amino acid kinase domain is a protein domain. It is found in protein kinases with various specificities, including the aspartate, glutamate and uridylate kinase families. In prokaryotes and plants the synthesis of the essential amino acids lysine and threonine is predominantly regulated by feed-back inhibition of aspartate kinase (AK) and dihydrodipicolinate synthase (DHPS). In ""Escherichia coli"", thrA, metLM, and lysC encode aspartokinase isozymes that show feedback inhibition by threonine, methionine, and lysine, respectively. The lysine-sensitive isoenzyme of aspartate kinase from spinach leaves has a"
"Serine Serine (symbol Ser or S) is an ɑ-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated − form under biological conditions), a carboxyl group (which is in the deprotonated – form in physiological conditions), and a side chain consisting of a hydroxymethyl group (see hydroxyl), classifying it as a polar amino acid. It can be synthesized in the human body under normal physiological circumstances, making it a nonessential amino acid. It is encoded by the codons UCU, UCC, UCA, UCG, AGU and AGC. This compound is one of"
"Tyrosine Tyrosine (symbol Tyr or Y) or 4-hydroxyphenylalanine is one of the 20 standard amino acids that are used by cells to synthesize proteins. It is a non-essential amino acid with a polar side group. The word ""tyrosine"" is from the Greek ""tyros"", meaning ""cheese"", as it was first discovered in 1846 by German chemist Justus von Liebig in the protein casein from cheese. It is called tyrosyl when referred to as a functional group or side chain. While tyrosine is generally classified as a hydrophobic amino acid, it is more hydrophilic than phenylalanine. It is encoded by the codons"
"Aspartic acid Aspartic acid (symbol Asp or D; the ionic form is known as aspartate), is an α-amino acid that is used in the biosynthesis of proteins. Similar to all other amino acids it contains an amino group and a carboxylic acid. Its α-amino group is in the protonated –NH form under physiological conditions, while its α-carboxylic acid group is deprotonated −COO under physiological conditions. Aspartic acid has an acidic side chain (CHCOOH) which reacts with other amino acids, enzymes and proteins in the body. Under physiological conditions (pH 7.4) in proteins the side chain usually occurs as the negatively"
"Aspein Aspein is an unusually acidic bivalve shell matrix protein, which may have important roles in calcium carbonate biomineralization. The Aspein gene (""aspein"", Uniprot: Q76K52) encodes a sequence of 413 amino acids, including a high proportion of Asp (60.4%), Gly (16.0%), and Ser (13.2%), and the predicted isoelectric point is 1.78. This is the most acidic of all the molluscan shell matrix proteins sequenced so far, or probably even of all known proteins on earth. The main body of aspein is occupied by (Asp)2–10 sequences punctuated with Ser–Gly dipeptides. RT-PCR demonstrated that the transcript of aspein is expressed at the"
"synthase), the NSAAs are generally larger than standard amino acids and most often have a phenylalanine core but with a large variety of different substituents. These allow a large repertoire of new functions, such as labelling (see figure), as a fluorescent reporter (""e.g."" dansylalanine) or to produce translationally protein in ""E. coli"" with Eukaryotic post-translational modifications (""e.g."" phosphoserine, phosphothreonine, and phosphotyrosine). Unnatural amino acids incorporated into proteins include heavy atom containing amino acids to facilitate certain x-ray crystallographic studies; amino acids with novel steric/packing and electronic properties; photocrosslinking amino acids which can be used to probe protein-protein interactions in vitro"
"Testin Testin also known as TESS is a protein that in humans is encoded by the ""TES"" gene located on chromosome 7. TES is a 47 kDa protein composed of 421 amino acids found at focal adhesions and is thought to have a role in regulation of cell motility. In addition to this, TES functions as a tumour suppressor. The ""TES"" gene is located within a fragile region of chromosome 7, and the promoter elements of the ""TES"" gene have been shown to be susceptible to methylation – this prevents the expression of the TES protein. TES came to greater"
"Lysine Lysine (symbol Lys or K) is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated −NH form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO form under biological conditions), and a side chain lysyl ((CH)NH), classifying it as a basic, charged (at physiological pH), aliphatic amino acid. It is encoded by the codons, AAA and AAG. Like almost all other amino acids, the α-carbon is chiral and lysine may refer to either enantiomer or a racemic mixture of both. For the purpose"
"the U.S. Department of Justice, Antitrust Division. This case served as the basis of the movie ""The Informant!"", and a book of the same title. Lysine Lysine (symbol Lys or K) is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated −NH form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO form under biological conditions), and a side chain lysyl ((CH)NH), classifying it as a basic, charged (at physiological pH), aliphatic amino acid. It is encoded by the codons, AAA and AAG. Like"
"CAS/CSE protein family In molecular biology, the CAS/CSE protein family is a family of proteins which includes mammalian cellular apoptosis susceptibility (CAS) proteins and yeast chromosome-segregation protein, CSE1. CAS is involved in both cellular apoptosis and proliferation. Apoptosis is inhibited in CAS-depleted cells, while the expression of CAS correlates to the degree of cellular proliferation. Like CSE1, it is essential for the mitotic checkpoint in the cell cycle (CAS depletion blocks the cell in the G2 phase), and has been shown to be associated with the microtubule network and the mitotic spindle, as is the protein MEK, which is thought"
"got disproved by the late 1950s. It is involved on mRNA processing and degradation in bacteria, plants, and in humans. In humans, the enzyme is encoded by the gene. In its active form, the protein forms a ring structure consisting of three PNPase molecules. Each PNPase molecule consists of two RNase PH domains, an S1 RNA binding domain and a K-homology domain. The protein is present in bacteria and in the chloroplasts and mitochondria of some eukaryotic cells. In eukaryotes and archaea, a structurally and evolutionary related complex exists, called the ""exosome complex"". The same abbreviation (""PNPase"") is also used"
"acid from protein hydrolysates using a chemical approach. The second utilizes enzymatic synthesis from phenolics, pyruvate, and ammonia through the use of tyrosine phenol-lyase. Advances in genetic engineering and the advent of industrial fermentation have shifted the synthesis of L-tyrosine to the use of engineered strains of ""E. coli"". Tyrosine Tyrosine (symbol Tyr or Y) or 4-hydroxyphenylalanine is one of the 20 standard amino acids that are used by cells to synthesize proteins. It is a non-essential amino acid with a polar side group. The word ""tyrosine"" is from the Greek ""tyros"", meaning ""cheese"", as it was first discovered in"
"Aladin (protein) Aladin, also known as adracalin, is a nuclear envelope protein that in humans is encoded by the ""AAAS"" gene. It is named after the achalasia-addisonianism-alacrima syndrome (triple A syndrome) which occurs when the gene is mutated. Aladin is a component of the nuclear pore complex, to which it is attached by nucleoporin NDC1. Mutant aladin causes selective failure of nuclear protein import and hypersensitivity to oxidative stress. Mutant aladin also causes decreased nuclear import of apraxin, a repair protein for single-strand breaks, and DNA ligase I, employed in DNA base excision repair. These decreases in DNA repair proteins"