EC number:3.7.1.7

Enzyme

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     3. Hydrolases
        3.7 Acting on carbon-carbon bonds
            3.7.1 In ketonic substances
ID:3.7.1.7
Description:Beta-diketone hydrolase.
Alternative Name: Oxidized PVA hydrolase.
Cath: 3.40.50.1820;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.7.1.7
BRENDA Enzyme Link: BRENDA 3.7.1.7
KEGG Enzyme Link: KEGG3.7.1.7
BioCyc Enzyme Link: BioCyc 3.7.1.7
ExPASy Enzyme Link: ExPASy3.7.1.7
EC2PDB Enzyme Link: EC2PDB 3.7.1.7
ExplorEnz Enzyme Link: ExplorEnz 3.7.1.7
PRIAM enzyme-specific profiles Link: PRIAM 3.7.1.7
IntEnz Enzyme Link: IntEnz 3.7.1.7
MEDLINE Enzyme Link: MEDLINE 3.7.1.7

EC number:3.7.1.7

MSA:

3.7.1.7;
Phylogenetic Tree:

3.7.1.7;
Uniprot:
M-CSA:
RHEA:11908 H2O + nonane-4,6-dione = butanoate + H(+) + pentan-2-one
RULE(radius=1) [*:1]=[C;H0;+0:2](-[*:3])-[CH2;+0:4]-[*:5].[OH2;+0:6]>>[*:5]-[CH3;+0:4].[*:1]=[C;H0;+0:2](-[*:3])-[OH;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Biochemical and molecular characterization of a periplasmic hydrolase for oxidized polyvinyl alcohol from Sphingomonas sp. strain 113P3.Klomklang W, Tani A, Kimbara K, Mamoto R, Ueda T, Shimao M, Kawai F2005 Apr15817792
The gene pvaB encodes oxidized polyvinyl alcohol hydrolase of Pseudomonas sp. strain VM15C and forms an operon with the polyvinyl alcohol dehydrogenase gene pvaA.Shimao M, Tamogami T, Kishida S, Harayama S2000 Mar10746768