EC number:1.2.3.3
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.2 Acting on the aldehyde or oxo group of donors |
| 1.2.3 With oxygen as acceptor |
3D structure
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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.| PDB |
2WVH;
2WVA;
4ZP1;
2WVG;
1ZPD;
5TMA;
2W93;
2VK8;
2VK1;
1QPB;
1PYD;
1PVD;
6BD9;
6BD3;
5IMS;
1JSC;
5WKC;
1T9D;
5FEM;
1T9B;
1T9A;
1N0H;
1MCZ;
5DEI;
4K9P;
4K9O;
4K9N;
4JUF;
4JUC;
4JUB;
3FZN;
2V3W;
5DGT;
5DGD;
4QEL;
4MZX;
4MQ5;
4MPR;
4MPP;
4MPJ;
4K9M;
4K9L;
4K9K;
4JUD;
4JUA;
4JU9;
4JU8;
4JD5;
4GPE;
4GP9;
4GM4;
4GM1;
4GM0;
4GG1;
3FSJ;
3F6E;
3F6B;
2FWN;
2FN3;
1YNO;
1Q6Z;
1PO7;
1PI3;
1BFD;
1Y9D;
2EZU;
2EZT;
2EZ9;
2EZ8;
2EZ4;
1POX;
1POW;
1OZH;
5WDG;
5DX6;
5D6R;
1OZG;
1OZF;
1UPC;
2IHV;
2IHT;
1UPB;
1UPA;
1OVM;
5WJ1;
5K6T;
5K6R;
5K6Q;
5K3S;
5K2O;
3EA4;
3E9Y;
1Z8N;
1YI1;
1YI0;
1YHZ;
1YHY;
1YBH;
6EFH;
6EFG;
3OE1;
3EYA;
3EY9;
2VK4;
2VJY;
2IHU;
1T9C;
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References
External Links
| UniProtKB Enzyme Link: | UniProtKB 1.2.3.3 |
| BRENDA Enzyme Link: | BRENDA 1.2.3.3 |
| KEGG Enzyme Link: | KEGG1.2.3.3 |
| BioCyc Enzyme Link: | BioCyc 1.2.3.3 |
| ExPASy Enzyme Link: | ExPASy1.2.3.3 |
| EC2PDB Enzyme Link: | EC2PDB 1.2.3.3 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.2.3.3 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.2.3.3 |
| IntEnz Enzyme Link: | IntEnz 1.2.3.3 |
| MEDLINE Enzyme Link: | MEDLINE 1.2.3.3 |
| RHEA:20848 | H(+) + O2 + phosphate + pyruvate = acetyl phosphate + CO2 + H2O2 |
| RULE(radius=1) | [*:1]-[OH;+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])-[O;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
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Structure of the thiamine- and flavin-dependent enzyme pyruvate oxidase. | Muller YA, Schulz GE | 1993 Feb 12 | 8438155 |
| Radical phosphate transfer mechanism for the thiamin diphosphate- and FAD-dependent pyruvate oxidase from Lactobacillus plantarum. Kinetic coupling of intercofactor electron transfer with phosphate transfer to acetyl-thiamin diphosphate via a transient FAD semiquinone/hydroxyethyl-ThDP radical pair. | Tittmann K, Wille G, Golbik R, Weidner A, Ghisla S, Hübner G | 2005 Oct 11 | 16201755 |