Enzyme

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     2. Transferases
        2.4 Glycosyltransferases
            2.4.1 Hexosyltransferases
ID:2.4.1.260
Description:Dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichol alpha-1,6-mannosyltransferase.
Alternative Name: Dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichyl alpha-6-mannosyltransferase.
Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.4.1.260
BRENDA Enzyme Link: BRENDA 2.4.1.260
KEGG Enzyme Link: KEGG2.4.1.260
BioCyc Enzyme Link: BioCyc 2.4.1.260
ExPASy Enzyme Link: ExPASy2.4.1.260
EC2PDB Enzyme Link: EC2PDB 2.4.1.260
ExplorEnz Enzyme Link: ExplorEnz 2.4.1.260
PRIAM enzyme-specific profiles Link: PRIAM 2.4.1.260
IntEnz Enzyme Link: IntEnz 2.4.1.260
MEDLINE Enzyme Link: MEDLINE 2.4.1.260
MSA:

2.4.1.260;

Phylogenetic Tree:

2.4.1.260;

Uniprot:
M-CSA:
RHEA:29535 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)]-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->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
ALG9 mannosyltransferase is involved in two different steps of lipid-linked oligosaccharide biosynthesis.Frank CG, Aebi M2005 Nov15987956
The Saccharomyces cerevisiae alg12delta mutant reveals a role for the middle-arm alpha1,2Man- and upper-arm alpha1,2Manalpha1,6Man- residues of Glc3Man9GlcNAc2-PP-Dol in regulating glycoprotein glycan processing in the endoplasmic reticulum and Golgi apparatus.Cipollo JF, Trimble RB2002 Nov12460943