EC 2.4.2

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.

enzyme that converts hypoxanthine to inosine monophosphate

Amidophosphoribosyltransferase (ATase), also known as glutamine phosphoribosylpyrophosphate amidotransferase (GPAT), is an enzyme responsible for catalyzing the conversion of 5-phosphoribosyl-1-pyrophosphate (PRPP) into 5-phosphoribosyl-1-amine (PRA), using the amine group from a glutamine side-chain. This is the committing step in de novo purine synthesis. In humans it is encoded by the PPAT (phosphoribosyl pyrophosphate amidotransferase) gene. ATase is a member of the purine/pyrimidine phosphoribosyltransferase family.

mammalian protein found in Homo sapiens

protein-coding gene in the species Homo sapiens

InterPro Family

InterPro Family

protein-coding gene in the species Homo sapiens

'''S-methyl-5'-thioadenosine phosphorylase (MTAP)''' is an enzyme responsible for polyamine metabolism. In humans, it is encoded by the methylthioadenosine phosphorylase (MTAP) gene on chromosome 9. Multiple alternatively spliced transcript variants have been described for this gene, but their full-length natures remain unknown.

class of enzymes

class of enzymes

class of enzymes

class of enzymes