EC number:2.4.1.265

Enzyme

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     2. Transferases
        2.4 Glycosyltransferases
            2.4.1 Hexosyltransferases
ID:2.4.1.265
Description:glucosyltransferase.
Alternative Name: Dol-P-Glc:Glc(1)Man(9)GlcNAc(2)-PP-Dol alpha-1->3-glucosyltransferase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.4.1.265
BRENDA Enzyme Link: BRENDA 2.4.1.265
KEGG Enzyme Link: KEGG2.4.1.265
BioCyc Enzyme Link: BioCyc 2.4.1.265
ExPASy Enzyme Link: ExPASy2.4.1.265
EC2PDB Enzyme Link: EC2PDB 2.4.1.265
ExplorEnz Enzyme Link: ExplorEnz 2.4.1.265
PRIAM enzyme-specific profiles Link: PRIAM 2.4.1.265
IntEnz Enzyme Link: IntEnz 2.4.1.265
MEDLINE Enzyme Link: MEDLINE 2.4.1.265

EC number:2.4.1.265

MSA:

2.4.1.265;
Phylogenetic Tree:

2.4.1.265;
Uniprot:
M-CSA:
RHEA:31307 alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + dolichyl beta-D-glucosyl phosphate = alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + dolichyl phosphate + H(+)
RULE(radius=1) [*:1]-[O;H0;+0:2]-[CH;+0:3](-[*:4])-[*:5].[*:6]-[OH;+0:7]>>[*:6]-[O;H0;+0:7]-[CH;+0:3](-[*:4])-[*:5].[*:1]-[OH;+0:2]
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References

TitleAuthorsDatePubMed ID
New phenotype of mutations deficient in glucosylation of the lipid-linked oligosaccharide: cloning of the ALG8 locus.Stagljar I, te Heesen S, Aebi M1994 Jun 218016100
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.Runge KW, Robbins PW1986 Nov 253536907
A deficiency in dolichyl-P-glucose:Glc1Man9GlcNAc2-PP-dolichyl alpha3-glucosyltransferase defines a new subtype of congenital disorders of glycosylation.Chantret I, Dancourt J, Dupré 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 SE2003 Mar 1412480927