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ENZYME entry: EC 2.4.1.131

Accepted Name
GDP-Man:Man(3)GlcNAc(2)-PP-dolichol alpha-1,2-mannosyltransferase.
Reaction catalysed
2 GDP-alpha-D-mannose + D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol <=> 2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
Comment(s)
  • The biosynthesis of asparagine-linked glycoproteins (N-linked protein glycosylation) utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway.
  • ALG11 mannosyltransferase from Saccharomyces cerevisiae carries out two sequential steps in the formation of the lipid-linked core oligosaccharide, adding two mannose residues in alpha(1->2) linkages to the nascent oligosaccharide.
  • Formerly EC 2.4.1.n4.
Cross-references
BRENDA2.4.1.131
EC2PDB2.4.1.131
ExplorEnz2.4.1.131
PRIAM enzyme-specific profiles2.4.1.131
KEGG Ligand Database for Enzyme Nomenclature2.4.1.131
IUBMB Enzyme Nomenclature2.4.1.131
IntEnz2.4.1.131
MEDLINEFind literature relating to 2.4.1.131
MetaCyc2.4.1.131
UniProtKB/Swiss-Prot
Q9XEE9, ALG11_ARATH;  Q75B12, ALG11_ASHGO;  P53993, ALG11_CAEEL;  
Q59S72, ALG11_CANAL;  Q6FWD1, ALG11_CANGA;  Q7ZW24, ALG11_DANRE;  
Q6BVB2, ALG11_DEBHA;  Q54DM9, ALG11_DICDI;  Q2TAA5, ALG11_HUMAN;  
Q6CLD6, ALG11_KLULA;  Q3TZM9, ALG11_MOUSE;  Q8X092, ALG11_NEUCR;  
Q5R7Z6, ALG11_PONAB;  O74878, ALG11_SCHPO;  Q08B22, ALG11_XENLA;  
Q6P312, ALG11_XENTR;  Q6C9T3, ALG11_YARLI;  P53954, ALG11_YEAST;  

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All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.4.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.4.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.-.-.-