From Wikipedia, the free encyclopedia
GDP-Man:Man2GlcNAc2-PP-dolichol alpha-1,6-mannosyltransferase
Identifiers
EC no. 2.4.1.257
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

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 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

References

  1. ^ Kämpf M, Absmanner B, Schwarz M, Lehle L (May 2009). "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. doi: 10.1074/jbc.m806416200. PMC  2673259. PMID  19282279.
  2. ^ O'Reilly MK, Zhang G, Imperiali B (August 2006). "In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis". Biochemistry. 45 (31): 9593–603. doi: 10.1021/bi060878o. PMID  16878994.

External links


From Wikipedia, the free encyclopedia
GDP-Man:Man2GlcNAc2-PP-dolichol alpha-1,6-mannosyltransferase
Identifiers
EC no. 2.4.1.257
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

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 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

References

  1. ^ Kämpf M, Absmanner B, Schwarz M, Lehle L (May 2009). "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. doi: 10.1074/jbc.m806416200. PMC  2673259. PMID  19282279.
  2. ^ O'Reilly MK, Zhang G, Imperiali B (August 2006). "In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis". Biochemistry. 45 (31): 9593–603. doi: 10.1021/bi060878o. PMID  16878994.

External links



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