EC Tree |
1. Oxidoreductases |
1.2 Acting on the aldehyde or oxo group of donors |
1.2.5 With a quinone or similar compound as acceptor |
ID: | 1.2.5.1 |
---|---|
Description: | Pyruvate dehydrogenase (quinone). |
Alternative Name: |
Pyruvate oxidase. Pyruvate dehydrogenase (cytochrome). Pyruvate dehydrogenase. |
Cath: | 3.40.50.970; 3.40.50.1220; |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 1.2.5.1 |
BRENDA Enzyme Link: | BRENDA 1.2.5.1 |
KEGG Enzyme Link: | KEGG1.2.5.1 |
BioCyc Enzyme Link: | BioCyc 1.2.5.1 |
ExPASy Enzyme Link: | ExPASy1.2.5.1 |
EC2PDB Enzyme Link: | EC2PDB 1.2.5.1 |
ExplorEnz Enzyme Link: | ExplorEnz 1.2.5.1 |
PRIAM enzyme-specific profiles Link: | PRIAM 1.2.5.1 |
IntEnz Enzyme Link: | IntEnz 1.2.5.1 |
MEDLINE Enzyme Link: | MEDLINE 1.2.5.1 |
RHEA:27405 | a ubiquinone + H2O + pyruvate = a ubiquinol + acetate + CO2 |
RULE(radius=1) | [*:1]-[C;H0;+0:2](-[CH3;+0:3])=[O;H0;+0:4].[*:5]-[C;H0;+0:6]1=[C;H0;+0:7](-[*:8])-[C;H0;+0:9](=[O;H0;+0:10])-[C;H0;+0:11](-[*:12])=[C;H0;+0:13](-[*:14])-[C;H0;+0:15]-1=[O;H0;+0:16].[OH2;+0:17]>>[*:1]-[CH3;+0:2].[*:5]-[c;H0;+0:6]1:[c;H0;+0:7](-[*:8]):[c;H0;+0:9](-[OH;+0:10]):[c;H0;+0:11](-[*:12]):[c;H0;+0:13](-[*:14]):[c;H0;+0:15]:1-[OH;+0:16].[O;H0;+0:4]=[C;H0;+0:3]=[O;H0;+0:17] |
Reaction | ![]() |
Core-to-Core |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Role of flavin in acetoin production by two bacterial pyruvate oxidases. | Bertagnolli BL, Hager LP | 1993 Jan | 8424670 |
Reconstitution of native Escherichia coli pyruvate oxidase from apoenzyme monomers and FAD. | Recny MA, Hager LP | 1982 Nov 10 | 6752142 |
Role of the tetrameric structure of Escherichia coli pyruvate oxidase in enzyme activation and lipid binding. | Wang AY, Chang YY, Cronan JE Jr | 1991 Jun 15 | 2040613 |