Biology:Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase
| glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.4.1.122 | ||||||||
| CAS number | 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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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 [math]\displaystyle{ \rightleftharpoons }[/math] 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
References
- "Identification of the product formed by human erythrocyte galactosyltransferase". Biochim. Biophys. Acta 659 (2): 302–11. 1981. doi:10.1016/0005-2744(81)90056-5. PMID 6789880.
- "Purification and properties of UDP-gal:N-acetylgalactosaminide mucin: beta 1,3-galactosyltransferase from swine trachea mucosa". J. Biol. Chem. 257 (7): 3987–94. 1982. PMID 6801057.
- "Glycosyltransferases involved in elongation of N-glycosidically linked oligosaccharides of the complex or N-acetyllactosamine type". Methods Enzymol. 98: 98–134. 1983. doi:10.1016/0076-6879(83)98143-0. PMID 6366476.
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