EC number:2.7.1.63

Enzyme

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EC Tree
     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.1 Phosphotransferases with an alcohol group as acceptor
ID:2.7.1.63
Description:Polyphosphate--glucose phosphotransferase.
Alternative Name: Polyphosphate glucokinase.
Cath: 3.30.420.40;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.1.63
BRENDA Enzyme Link: BRENDA 2.7.1.63
KEGG Enzyme Link: KEGG2.7.1.63
BioCyc Enzyme Link: BioCyc 2.7.1.63
ExPASy Enzyme Link: ExPASy2.7.1.63
EC2PDB Enzyme Link: EC2PDB 2.7.1.63
ExplorEnz Enzyme Link: ExplorEnz 2.7.1.63
PRIAM enzyme-specific profiles Link: PRIAM 2.7.1.63
IntEnz Enzyme Link: IntEnz 2.7.1.63
MEDLINE Enzyme Link: MEDLINE 2.7.1.63

EC number:2.7.1.63

MSA:

2.7.1.63;
Phylogenetic Tree:

2.7.1.63;
Uniprot:
M-CSA:
RHEA:22036 [phosphate](n) + D-glucose = [phosphate](n-1) + D-glucose 6-phosphate + H(+)
RULE(radius=1) [*:1]-[O;H0;+0:2]-[P;H0;+0:3](=[*:4])(-[*:5])-[*:6].[*:7]-[OH;+0:8]>>[*:1]-[OH;+0:2].[*:4]=[P;H0;+0:3](-[*:5])(-[*:6])-[O;H0;+0:8]-[*:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Kinetic mechanisms of polyphosphate glucokinase from Mycobacterium tuberculosis.Hsieh PC, Kowalczyk TH, Phillips NF1996 Jul 308703950
Polyphosphate glucokinase from Propionibacterium shermanii. Kinetics and demonstration that the mechanism involves both processive and nonprocessive type reactions.Pepin CA, Wood HG1986 Apr 53007458
Crystal structure of bacterial inorganic polyphosphate/ATP-glucomannokinase. Insights into kinase evolution.Mukai T, Kawai S, Mori S, Mikami B, Murata K2004 Nov 2615377666