Biology:GDP-Man:Man2GlcNAc2-PP-dolichol alpha-1,6-mannosyltransferase

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Short description: Class of enzymes
GDP-Man:Man2GlcNAc2-PP-dolichol alpha-1,6-mannosyltransferase
Identifiers
EC number2.4.1.257
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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 [math]\displaystyle{ \rightleftharpoons }[/math] GDP + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol

The biosynthesis of asparagine-linked glycoproteins utilizes a dolichyl diphosphate-linked glycosyl donor.

Human proteins containing this domain

  • ALG2

References

  1. "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. May 2009. doi:10.1074/jbc.m806416200. PMID 19282279. 
  2. "In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis". Biochemistry 45 (31): 9593–603. August 2006. doi:10.1021/bi060878o. PMID 16878994. 

External links