EC number:2.7.1.188

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:2.7.1.188
Description:2-epi-5-epi-valiolone 7-kinase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.1.188
BRENDA Enzyme Link: BRENDA 2.7.1.188
KEGG Enzyme Link: KEGG2.7.1.188
BioCyc Enzyme Link: BioCyc 2.7.1.188
ExPASy Enzyme Link: ExPASy2.7.1.188
EC2PDB Enzyme Link: EC2PDB 2.7.1.188
ExplorEnz Enzyme Link: ExplorEnz 2.7.1.188
PRIAM enzyme-specific profiles Link: PRIAM 2.7.1.188
IntEnz Enzyme Link: IntEnz 2.7.1.188
MEDLINE Enzyme Link: MEDLINE 2.7.1.188

EC number:2.7.1.188

MSA:

2.7.1.188;
Phylogenetic Tree:

2.7.1.188;
Uniprot:
M-CSA:
RHEA:44364 2-epi-5-epi-valiolone + ATP = 2-epi-5-epi-valiolone 7-phosphate + ADP + H(+)
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8]>>[*:8]-[OH;+0:7].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Biosynthesis of the C(7)-cyclitol moiety of acarbose in Actinoplanes species SE50/110. 7-O-phosphorylation of the initial cyclitol precursor leads to proposal of a new biosynthetic pathway.Zhang CS, Stratmann A, Block O, Brückner R, Podeschwa M, Altenbach HJ, Wehmeier UF, Piepersberg W2002 Jun 2111937512