GDP-Man:Man2GlcNAc2-PP-dolichol alpha-1,6-mannosyltransferase
GDP-Man:Man2GlcNAc2-PP-dolichol alpha-1,6-mannosyltransferase (EC 2.4.1.257, GDP-Man:Man2GlcNAc2-PP-Dol alpha-1,6-mannosyltransferase, Alg2 mannosyltransferase, ALG2 (gene), GDP-Man:Man1GlcNAc2-PP-dolichol mannosyltransferase) is an enzyme with systematic name GDP-D-mannose:D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol alpha-6-mannosyltransferase.[1][2] This enzyme catalyses the following chemical reaction
- GDP-D-mannose + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol GDP + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
GDP-Man:Man2GlcNAc2-PP-dolichol alpha-1,6-mannosyltransferase | |||||||||
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Identifiers | |||||||||
EC number | 2.4.1.257 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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The biosynthesis of asparagine-linked glycoproteins utilizes a dolichyl diphosphate-linked glycosyl donor.
Human proteins containing this domain
References
- Kämpf M, Absmanner B, Schwarz M, Lehle L (May 2009). "Biochemical characterization and membrane topology of Alg2 from Saccharomyces cerevisiae as a bifunctional alpha1,3- and 1,6-mannosyltransferase involved in lipid-linked oligosaccharide biosynthesis". The Journal of Biological Chemistry. 284 (18): 11900–12. doi:10.1074/jbc.m806416200. PMC 2673259. PMID 19282279.
- O'Reilly MK, Zhang G, Imperiali B (August 2006). "In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis". Biochemistry. 45 (31): 9593–603. doi:10.1021/bi060878o. PMID 16878994.
External links
- GDP-Man:Man2GlcNAc2-PP-dolichol+alpha-1,6-mannosyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)
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