EC number:2.4.1.257

Enzyme

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     2. Transferases
        2.4 Glycosyltransferases
            2.4.1 Hexosyltransferases
ID:2.4.1.257
Description:GDP-Man:Man(2)GlcNAc(2)-PP-dolichol alpha-1,6-mannosyltransferase.
Alternative Name: GDP-Man:Man(2)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.4.1.257
BRENDA Enzyme Link: BRENDA 2.4.1.257
KEGG Enzyme Link: KEGG2.4.1.257
BioCyc Enzyme Link: BioCyc 2.4.1.257
ExPASy Enzyme Link: ExPASy2.4.1.257
EC2PDB Enzyme Link: EC2PDB 2.4.1.257
ExplorEnz Enzyme Link: ExplorEnz 2.4.1.257
PRIAM enzyme-specific profiles Link: PRIAM 2.4.1.257
IntEnz Enzyme Link: IntEnz 2.4.1.257
MEDLINE Enzyme Link: MEDLINE 2.4.1.257

EC number:2.4.1.257

MSA:

2.4.1.257;
Phylogenetic Tree:

2.4.1.257;
Uniprot:
M-CSA:
RHEA:29519 alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP + H(+)
RULE(radius=1) [*:1]-[O;H0;+0:2]-[CH;+0:3](-[*:4])-[*:5].[*:6]-[OH;+0:7]>>[*:4]-[CH;+0:3](-[*:5])-[O;H0;+0:7]-[*:6].[*:1]-[OH;+0:2]
Reaction
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References

TitleAuthorsDatePubMed ID
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.Kämpf M, Absmanner B, Schwarz M, Lehle L2009 May 119282279
In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis.O'Reilly MK, Zhang G, Imperiali B2006 Aug 816878994