EC number:1.2.3.6

Enzyme

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     1. Oxidoreductases
        1.2 Acting on the aldehyde or oxo group of donors
            1.2.3 With oxygen as acceptor
ID:1.2.3.6
Description:Pyruvate oxidase (CoA-acetylating).

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.2.3.6
BRENDA Enzyme Link: BRENDA 1.2.3.6
KEGG Enzyme Link: KEGG1.2.3.6
BioCyc Enzyme Link: BioCyc 1.2.3.6
ExPASy Enzyme Link: ExPASy1.2.3.6
EC2PDB Enzyme Link: EC2PDB 1.2.3.6
ExplorEnz Enzyme Link: ExplorEnz 1.2.3.6
PRIAM enzyme-specific profiles Link: PRIAM 1.2.3.6
IntEnz Enzyme Link: IntEnz 1.2.3.6
MEDLINE Enzyme Link: MEDLINE 1.2.3.6

EC number:1.2.3.6

MSA:

1.2.3.6;
Phylogenetic Tree:

1.2.3.6;
Uniprot:
M-CSA:
RHEA:21912 CoA + H(+) + O2 + pyruvate = acetyl-CoA + CO2 + H2O2
RULE(radius=1) [*:1]-[SH;+0:2].[*:3]=[C;H0;+0:4](-[OH;+0:5])-[C;H0;+0:6](=[*:7])-[*:8].[H+;H0:9].[O;H0;+0:10]=[O;H0;+0:11]>>[*:7]=[C;H0;+0:6](-[*:8])-[S;H0;+0:2]-[*:1].[*:3]=[C;H0;+0:4]=[O;H0;+0:5].[OH;+0:10]-[OH;+0:11]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Pyruvate oxidase (CoA acetylating) in Entamoeba histolytica.Takeuchi T, Weinbach EC, Diamond LS1975 Jul 22167776
An energy-conserving pyruvate-to-acetate pathway in Entamoeba histolytica. Pyruvate synthase and a new acetate thiokinase.Reeves RE, Warren LG, Susskind B, Lo HS1977 Jan 2513076