In enzymology, a glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase (EC 2.4.1.122) is an enzyme that catalyzes the chemical reaction
glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase | |||||||||
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Identifiers | |||||||||
EC no. | 2.4.1.122 | ||||||||
CAS no. | 97089-61-7 | ||||||||
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 | ||||||||
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- UDP-galactose + glycoprotein N-acetyl-D-galactosamine UDP + glycoprotein D-galactosyl-1,3-N-acetyl-D-galactosamine
Thus, the two substrates of this enzyme are UDP-galactose and glycoprotein N-acetyl-D-galactosamine, whereas its two products are UDP and glycoprotein D-galactosyl-1,3-N-acetyl-D-galactosamine.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-galactose:glycoprotein-N-acetyl-D-galactosamine 3-beta-D-galactosyltransferase. This enzyme is also called uridine diphosphogalactose-mucin beta-(1->3)-galactosyltransferase. This enzyme participates in O-glycan biosynthesis and glycan structures - biosynthesis 1.
See also
editReferences
edit- Hesford FJ, Berger EG, Van den Eijnden DH (1981). "Identification of the product formed by human erythrocyte galactosyltransferase". Biochim. Biophys. Acta. 659 (2): 302–11. doi:10.1016/0005-2744(81)90056-5. PMID 6789880.
- Mendicino J, Sivakami S, Davila M, Chandrasekaran EV (1982). "Purification and properties of UDP-gal:N-acetylgalactosaminide mucin: beta 1,3-galactosyltransferase from swine trachea mucosa". J. Biol. Chem. 257 (7): 3987–94. doi:10.1016/S0021-9258(18)34880-4. PMID 6801057.
- Schachter H, Narasimhan S, Gleeson P, Vella G (1983). Glycosyltransferases involved in elongation of N-glycosidically linked oligosaccharides of the complex or N-acetyllactosamine type. Methods Enzymol. Vol. 98. pp. 98–134. doi:10.1016/0076-6879(83)98143-0. ISBN 978-0-12-181998-9. PMID 6366476.