EC number:2.7.1.187

Enzyme

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     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.1 Phosphotransferases with an alcohol group as acceptor
ID:2.7.1.187
Description:Acarbose 7(IV)-phosphotransferase.
Alternative Name: Acarbose 7-kinase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.1.187
BRENDA Enzyme Link: BRENDA 2.7.1.187
KEGG Enzyme Link: KEGG2.7.1.187
BioCyc Enzyme Link: BioCyc 2.7.1.187
ExPASy Enzyme Link: ExPASy2.7.1.187
EC2PDB Enzyme Link: EC2PDB 2.7.1.187
ExplorEnz Enzyme Link: ExplorEnz 2.7.1.187
PRIAM enzyme-specific profiles Link: PRIAM 2.7.1.187
IntEnz Enzyme Link: IntEnz 2.7.1.187
MEDLINE Enzyme Link: MEDLINE 2.7.1.187

EC number:2.7.1.187

MSA:

2.7.1.187;
Phylogenetic Tree:

2.7.1.187;
Uniprot:
M-CSA:
RHEA:45124 acarbose + ATP = acarbose 7(IV)-phosphate + ADP + H(+)
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8]>>[*:1]-[O;H0;+0:2]-[P;H0;+0:4](=[*:3])(-[*:5])-[*:6].[*:8]-[OH;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Acarbose 7-phosphotransferase from Actinoplanes sp.: purification, properties, and possible physiological function.Drepper A, Pape H1996 Jul8784428
Formation of acarbose phosphate by a cell-free extract from the acarbose producer Actinoplanes sp.Goeke K, Drepper A, Pape H1996 Jul8784426
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