EC number:1.17.2.3
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.17 Acting on CH or CH2 groups |
| 1.17.2 With a cytochrome as acceptor |
| ID: | 1.17.2.3 |
|---|---|
| Description: | Formate dehydrogenase (cytochrome c-553). |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.17.2.3 |
| BRENDA Enzyme Link: | BRENDA 1.17.2.3 |
| KEGG Enzyme Link: | KEGG1.17.2.3 |
| BioCyc Enzyme Link: | BioCyc 1.17.2.3 |
| ExPASy Enzyme Link: | ExPASy1.17.2.3 |
| EC2PDB Enzyme Link: | EC2PDB 1.17.2.3 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.17.2.3 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.17.2.3 |
| IntEnz Enzyme Link: | IntEnz 1.17.2.3 |
| MEDLINE Enzyme Link: | MEDLINE 1.17.2.3 |
| RHEA:15189 | 2 [Fe(III)cytochrome c553] + formate = 2 [Fe(II)cytochrome c553] + CO2 + H(+) |
| RULE(radius=1) | [*:1]=[CH;+0:2]-[OH;+0:3].[Fe+3;H0:4].[Fe+3;H0:5]>>[*:1]=[C;H0;+0:2]=[O;H0;+0:3].[Fe+2;H0:4].[Fe+2;H0:5] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Purification and characterization of the formate dehydrogenase from Desulfovibrio vulgaris Hildenborough. | Sebban C, Blanchard L, Bruschi M, Guerlesquin F | 1995 Nov 1 | 8566699 |
| Formate: cytochrome oxidoreductase of Desulfovibrio vulgaris. | Yagi T | 1969 Oct | 4982127 |
| Purification and properties of cytochrome c-553, an electron acceptor for formate dehydrogenase of Desulfovibrio vulgaris, Miyazaki. | Yagi T | 1979 Oct 10 | 226135 |
| Tungsten and molybdenum regulation of formate dehydrogenase expression in Desulfovibrio vulgaris Hildenborough. | da Silva SM, Pimentel C, Valente FM, Rodrigues-Pousada C, Pereira IA | 2011 Jun | 21498650 |