Transferases

thumb|300px|right|RNA polymerase from [[Saccharomyces cerevisiae complexed with α-Amanitin (in red). Despite the use of the term "polymerase," RNA polymerases are classified as a form of nucleotidyl transferase.]]

Transaminases or aminotransferases are enzymes that catalyze a transamination reaction between an amino acid and an α-keto acid. They are important in the synthesis of amino acids, which form proteins.

class of enzymes

thumb|Most glycosyltransferase enzymes form one of two folds: GT-A or GT-B Glycosyltransferases (GTFs, Gtfs) are enzymes (EC 2.4) 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-based.

enzymes that catalyze acyl group transfer from acetyl-CoA to histones

In biochemistry, phosphorylases are enzymes that catalyze the addition of a phosphate group from an inorganic phosphate (phosphate+hydrogen) to an acceptor.

thumb|Acyl Acyltransferase is a type of transferase enzyme that acts upon acyl groups.

'''Uridine 5'-diphospho-glucuronosyltransferase (UDP-glucuronosyltransferase, UDPGT or UGT''') is a microsomal glycosyltransferase () that catalyzes the transfer of the glucuronic acid component of UDP-glucuronic acid to a small hydrophobic molecule. This is a glucuronidation reaction.

An acetyltransferase (also referred to as a transacetylase) is any of a class of transferase enzymes that transfers an acetyl group in a reaction called acetylation. In biological organisms, post-translational modification of a protein via acetylation can profoundly transform its functionality by altering various properties like hydrophobicity, solubility, and surface attributes. These alterations have the potential to influence the protein's conformation and its interactions with substrates, cofactors, and other macromolecules.

class of enzymes

class of enzymes

mammalian protein found in Homo sapiens

In biochemistry, phosphotransferases are enzymes that catalyze phosphorylations (addition of inorganic phosphate, abbreviated P, to some substrate).

enzyme class, includes alll types of glycogen/starch synthases

protein-coding gene in the species Homo sapiens

thumb|500x500px|Regulation of bacterial glutamine synthase (GlnA) by adenylylation and (indirectly) by uridylylation. Uridylyltransferase (GlnD) uridylylates the regulatory PII protein (GlnB) which determines whether adenylyltransferase (GlnE) adenylylates or de-adenylylates glutamine synthase. GlnD is a bifunctional enzyme that both attaches and removes UMP from GlnB. GlnD is activated by Alpha-Ketoglutaric acid|α-ketoglutarate and ATP (green) but inhibited by [[glutamine and inorganic phosphate (Pi, in red). The protein names are those in E. coli. Homologs in other bacteria may have differen

class of enzymes

class of enzymes

protein-coding gene in the species Homo sapiens

class of enzymes

A phosphoribosyltransferase is a type of transferase enzyme.

cytosolic DNA sensor

Wikimedia list article

class of enzymes

class of enzymes

class of enzymes