ALG8 (enzyme class)
| Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.4.1.265 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferase (EC 2.4.1.265, ALG8, Dol-P-Glc:Glc1Man9GlcNAc2-PP-Dol alpha-1,3-glucosyltransferase) is an enzyme with systematic name dolichyl beta-D-glucosyl phosphate:D-Glc-alpha-(1->3)-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->2)-D-Man-alpha-(1->6))-D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol alpha-1,3-glucosyltransferase.[1][2][3]
This enzyme catalyses the following chemical reaction
which is in words:
- dolichyl beta-D-glucosyl phosphate + D-Glc-alpha-(1->3)-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->2)-D-Man-alpha-(1->6)]-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol D-Glc-alpha-(1->3)-D-Glc-alpha-(1->3)-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->2)-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
See also
- EC 2.4.1.267 (dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferase)
- EC 2.4.1.256 (dolichyl-P-Glc:Glc2Man9GlcNAc2-PP-dolichol alpha-1,2-glucosyltransferase)
References
- ^ Stagljar, I.; te Heesen, S.; Aebi, M. (1994). "New phenotype of mutations deficient in glucosylation of the lipid-linked oligosaccharide: cloning of the ALG8 locus". Proc. Natl. Acad. Sci. USA. 91 (13): 5977–5981. doi:10.1073/pnas.91.13.5977. PMID 8016100.
- ^ Runge, K.W.; Robbins, P.W. (1986). "A new yeast mutation in the glucosylation steps of the asparagine-linked glycosylation pathway. Formation of a novel asparagine-linked oligosaccharide containing two glucose residues". J. Biol. Chem. 261 (33): 15582–15590. PMID 3536907.
- ^ Chantret, I.; Dancourt, J.; Dupre, T.; Delenda, C.; Bucher, S.; Vuillaumier-Barrot, S.; Ogier de Baulny, H.; Peletan, C.; Danos, O.; Seta, N.; Durand, G.; Oriol, R.; Codogno, P.; Moore, S.E. (2003). "A deficiency in dolichyl-P-glucose:Glc1Man9GlcNAc2-PP-dolichyl α3-glucosyltransferase defines a new subtype of congenital disorders of glycosylation". J. Biol. Chem. 278: 9962–9971. doi:10.1074/jbc.M211950200. PMID 12480927.
{{cite journal}}: CS1 maint: unflagged free DOI (link)
External links
- Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichol+alpha-1,3-glucosyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)