|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 188.8.131.527
Enzymes and Genes:
(mannosyl)9-(N-acetylglucosaminyl)2-diphosphodolichol glucosyltransferase : ALG6 ( Saccharomyces cerevisiae )
In Pathway: dolichyl-diphosphooligosaccharide biosynthesis
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol α-1,3-glucosyltransferase
Enzyme Commission Synonyms: ALG6, Dol-P-Glc:Man9GlcNAc2-PP-Dol α-1,3-glucosyltransferase
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): 7.5214844 [Latendresse13]
Enzyme Commission Summary:
The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 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 a (mannosyl)5-(N-acetylglucosaminyl)2-diphosphodolichol to a (mannosyl)9-(N-acetylglucosaminyl)2-diphosphodolichol on the lumenal side use dolichyl β-D-mannosyl phosphate. Subsequent addition of the three glucose residues by EC 184.108.40.2067, EC 220.127.116.115 and EC 18.104.22.1686 represents the final stage of the lipid-linked oligosaccharide assembly.
Unification Links: Rhea:30638
Reiss96: Reiss G, te Heesen S, Zimmerman J, Robbins PW, Aebi M (1996). "Isolation of the ALG6 locus of Saccharomyces cerevisiae required for glucosylation in the N-linked glycosylation pathway." Glycobiology 6(5);493-8. PMID: 8877369
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493