Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase

glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase
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
Search PMC articles PubMed articles NCBI proteins

In enzymology, a glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase (EC 2.4.1.122) is an enzyme that catalyzes the chemical reaction

UDP-galactose + glycoprotein N-acetyl-D-galactosamine ${\displaystyle \rightleftharpoons }$ 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

• C1GALT1

References

• 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.