EC number:2.4.1.332

Enzyme

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     2. Transferases
        2.4 Glycosyltransferases
            2.4.1 Hexosyltransferases
ID:2.4.1.332
Description:1,2-alpha-glucosylglycerol phosphorylase.
Alternative Name: 2-O-alpha-D-glucopyranosylglycerol phosphorylase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.4.1.332
BRENDA Enzyme Link: BRENDA 2.4.1.332
KEGG Enzyme Link: KEGG2.4.1.332
BioCyc Enzyme Link: BioCyc 2.4.1.332
ExPASy Enzyme Link: ExPASy2.4.1.332
EC2PDB Enzyme Link: EC2PDB 2.4.1.332
ExplorEnz Enzyme Link: ExplorEnz 2.4.1.332
PRIAM enzyme-specific profiles Link: PRIAM 2.4.1.332
IntEnz Enzyme Link: IntEnz 2.4.1.332
MEDLINE Enzyme Link: MEDLINE 2.4.1.332

EC number:2.4.1.332

MSA:

2.4.1.332;
Phylogenetic Tree:

2.4.1.332;
Uniprot:
M-CSA:
RHEA:43060 2-O-(alpha-D-glucopyranosyl)glycerol + phosphate = beta-D-glucose 1-phosphate + glycerol
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[O;H0;+0:4]-[*:5].[*:6]-[OH;+0:7]>>[*:1]-[CH;+0:2](-[*:3])-[O;H0;+0:7]-[*:6].[*:5]-[OH;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Structural basis for reversible phosphorolysis and hydrolysis reactions of 2-O-α-glucosylglycerol phosphorylase.Touhara KK, Nihira T, Kitaoka M, Nakai H, Fushinobu S2014 Jun 2724828502
2-O-α-D-glucosylglycerol phosphorylase from Bacillus selenitireducens MLS10 possessing hydrolytic activity on β-D-glucose 1-phosphate.Nihira T, Saito Y, Ohtsubo K, Nakai H, Kitaoka M201424466148