ENZYME entry: EC 2.4.1.260

Accepted Name
Dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichol alpha-1,6-mannosyltransferase.
Alternative Name(s)
Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase.
Dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichyl alpha-6-mannosyltransferase.
Reaction catalysed
Dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(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 <=> D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate
Comment(s)
  • The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc(3)Man(9)GlcNAc(2) core- oligosaccharide on the lipid carrier dolichyl diphosphate.
  • Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man(5)GlcNAc(2)-PP-dolichol to Man(9)Glc-NAc(2)-PP-dolichol on the lumenal side use dolichyl beta-D-mannosyl phosphate.
  • Formerly EC 2.4.1.130.
Cross-references
BRENDA2.4.1.260
EC2PDB2.4.1.260
ExplorEnz2.4.1.260
PRIAM enzyme-specific profiles2.4.1.260
KEGG Ligand Database for Enzyme Nomenclature2.4.1.260
IUBMB Enzyme Nomenclature2.4.1.260
IntEnz2.4.1.260
MEDLINEFind literature relating to 2.4.1.260
MetaCyc2.4.1.260
UniProtKB/Swiss-Prot
A8MR93, ALG12_ARATH;  Q23361, ALG12_CAEEL;  Q9VH78, ALG12_DROME;  
Q9BV10, ALG12_HUMAN;  Q8VDB2, ALG12_MOUSE;  Q9USD4, ALG12_SCHPO;  
P53730, ALG12_YEAST;  

View entry in original ENZYME format
View entry in raw text format (no links)

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.-.-.-