B-1,4-mannosyl-glycoprotein 4-b-N-acetylglucosaminyltransferase
Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase (EC 2.4.1.144, N-acetylglucosaminyltransferase III, N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III, uridine diphosphoacetylglucosamine-glycopeptide beta4-acetylglucosaminyltransferase III, beta-1,4-mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferase, GnTIII) is an enzyme with systematic name UDP-N-acetyl-D-glucosamine:beta-D-mannosyl-glycoprotein 4-beta-N-acetyl-D-glucosaminyltransferase.[1][2] This enzyme catalyses the following chemical reaction
- UDP-N-acetyl-D-glucosamine + beta-D-mannosyl-R UDP + 4-(N-acetyl-beta-D-glucosaminyl)-beta-D-mannosyl-R
| Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.4.1.144 | ||||||||
| CAS number | 83744-93-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
R represents the remainder of the N-linked oligosaccharide in the glycoprotein acceptor.
References
- Narasimhan S (September 1982). "Control of glycoprotein synthesis. UDP-GlcNAc:glycopeptide beta 4-N-acetylglucosaminyltransferase III, an enzyme in hen oviduct which adds GlcNAc in beta 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-glycosyl oligosaccharides". The Journal of Biological Chemistry. 257 (17): 10235–42. PMID 6213618.
- 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 in Enzymology. 98: 98–134. doi:10.1016/0076-6879(83)98143-0. PMID 6366476.
External links
- Beta-1,4-mannosyl-glycoprotein+4-beta-N-acetylglucosaminyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)
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