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In biochemistry, a transferase is any one of a class of enzymes that catalyse the transfer of specific functional groups (e.g. a methyl or glycosyl group) from one molecule (called the donor) to another (called the acceptor). [2]
Most glycosyltransferase enzymes form one of two folds: GT-A or GT-B. Glycosyltransferases (GTFs, Gtfs) are enzymes that establish natural glycosidic linkages.They catalyze the transfer of saccharide moieties from an activated nucleotide sugar (also known as the "glycosyl donor") to a nucleophilic glycosyl acceptor molecule, the nucleophile of which can be oxygen- carbon-, nitrogen-, or sulfur ...
The MdcA family catalyzes reactions involving acetyl-CoA and malonate (EC 2.8.3.3), but it too is an acyl-ACP transferase (as part of malonate decarboxylase; EC 4.1.1.9). The Gct family has members that catalyze CoA-transferase reactions, but half of the members do not. They instead catalyze hydrolysis or other reactions involving acyl-CoA.
A deficiency in the bilirubin specific form of glucuronosyltransferase is thought to be the cause of Gilbert's syndrome, which is characterized by unconjugated hyperbilirubinemia.
N-acetyltransferase (NAT) is an enzyme that catalyzes the transfer of acetyl groups from acetyl-CoA to arylamines, arylhydroxylamines and arylhydrazines. [1] [2] [3] They have wide specificity for aromatic amines, particularly serotonin, and can also catalyze acetyl transfer between arylamines without CoA.
Transamination is mediated by several types of aminotransferase enzymes. An aminotransferase may be specific for an individual amino acid, or it may be able to process any member of a group of similar ones, for example the branched-chain amino acids, which comprises valine, isoleucine, and leucine.
Animals must metabolize proteins to amino acids, at the expense of muscle tissue, when blood sugar is low. The preference of liver transaminases for oxaloacetate or alpha-ketoglutarate plays a key role in funneling nitrogen from amino acid metabolism to aspartate and glutamate for conversion to urea for excretion of nitrogen.
Alanine transaminase (ALT), also known as alanine aminotransferase (ALT or ALAT), formerly serum glutamate-pyruvate transaminase (GPT) or serum glutamic-pyruvic transaminase (SGPT), is a transaminase enzyme (EC 2.6.1.2) that was first characterized in the mid-1950s by Arthur Karmen and colleagues. [1]