Enzyme

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     2. Transferases
        2.4 Glycosyltransferases
            2.4.1 Hexosyltransferases
ID:2.4.1.261
Description:Dolichyl-P-Man:Man(8)GlcNAc(2)-PP-dolichol alpha-1,2-mannosyltransferase.
Alternative Name: Dol-P-Man:Man(8)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.4.1.261
BRENDA Enzyme Link: BRENDA 2.4.1.261
KEGG Enzyme Link: KEGG2.4.1.261
BioCyc Enzyme Link: BioCyc 2.4.1.261
ExPASy Enzyme Link: ExPASy2.4.1.261
EC2PDB Enzyme Link: EC2PDB 2.4.1.261
ExplorEnz Enzyme Link: ExplorEnz 2.4.1.261
PRIAM enzyme-specific profiles Link: PRIAM 2.4.1.261
IntEnz Enzyme Link: IntEnz 2.4.1.261
MEDLINE Enzyme Link: MEDLINE 2.4.1.261
MSA:

2.4.1.261;

Phylogenetic Tree:

2.4.1.261;

Uniprot:
M-CSA:
RHEA:29539 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->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + dolichyl beta-D-mannosyl phosphate = 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]>>[*:4]-[CH;+0:3](-[*:5])-[O;H0;+0:7]-[*:6].[*:1]-[OH;+0:2]
Reaction
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References

TitleAuthorsDatePubMed ID
Mutations of an alpha1,6 mannosyltransferase inhibit endoplasmic reticulum-associated degradation of defective brassinosteroid receptors in Arabidopsis.Hong Z, Jin H, Fitchette AC, Xia Y, Monk AM, Faye L, Li J2009 Dec20023196
Quality control of glycoproteins bearing truncated glycans in an ALG9-defective (CDG-IL) patient.Vleugels W, Keldermans L, Jaeken J, Butters TD, Michalski JC, Matthijs G, Foulquier F2009 Aug19451548
ALG9 mannosyltransferase is involved in two different steps of lipid-linked oligosaccharide biosynthesis.Frank CG, Aebi M2005 Nov15987956
CDG-IL: an infant with a novel mutation in the ALG9 gene and additional phenotypic features.Weinstein M, Schollen E, Matthijs G, Neupert C, Hennet T, Grubenmann CE, Frank CG, Aebi M, Clarke JT, Griffiths A, Seargeant L, Poplawski N2005 Jul 1515945070
Identification and functional analysis of a defect in the human ALG9 gene: definition of congenital disorder of glycosylation type IL.Frank CG, Grubenmann CE, Eyaid W, Berger EG, Aebi M, Hennet T2004 Jul15148656