EC number:1.2.7.12
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.2 Acting on the aldehyde or oxo group of donors |
| 1.2.7 With an iron-sulfur protein as acceptor |
| ID: | 1.2.7.12 |
|---|---|
| Description: | Formylmethanofuran dehydrogenase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.2.7.12 |
| BRENDA Enzyme Link: | BRENDA 1.2.7.12 |
| KEGG Enzyme Link: | KEGG1.2.7.12 |
| BioCyc Enzyme Link: | BioCyc 1.2.7.12 |
| ExPASy Enzyme Link: | ExPASy1.2.7.12 |
| EC2PDB Enzyme Link: | EC2PDB 1.2.7.12 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.2.7.12 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.2.7.12 |
| IntEnz Enzyme Link: | IntEnz 1.2.7.12 |
| MEDLINE Enzyme Link: | MEDLINE 1.2.7.12 |
| RHEA:19841 | H2O + N-formylmethanofuran + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + H(+) + methanofuran + 2 reduced [2Fe-2S]-[ferredoxin] |
| RULE(radius=1) | [*:1]-[Fe+;H0:2]-[*:3].[*:4]-[Fe+;H0:5]-[*:6].[*:7]=[CH;+0:8]-[NH;+0:9]-[*:10].[OH2;+0:11]>>[*:1]-[Fe;H0;+0:2]-[*:3].[*:4]-[Fe;H0;+0:5]-[*:6].[*:10]-[NH2;+0:9].[*:7]=[C;H0;+0:8]=[O;H0;+0:11] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The active species of 'CO2' utilized by formylmethanofuran dehydrogenase from methanogenic Archaea. | Vorholt JA, Thauer RK | 1997 Sep 15 | 9342247 |
| Tungstate can substitute for molybdate in sustaining growth of Methanobacterium thermoautotrophicum. Identification and characterization of a tungsten isoenzyme of formylmethanofuran dehydrogenase. | Bertram PA, Schmitz RA, Linder D, Thauer RK | 1994 | 8161283 |
| Formylmethanofuran dehydrogenases from methanogenic Archaea. Substrate specificity, EPR properties and reversible inactivation by cyanide of the molybdenum or tungsten iron-sulfur proteins. | Bertram PA, Karrasch M, Schmitz RA, Böcher R, Albracht SP, Thauer RK | 1994 Mar 1 | 8125106 |
| The molybdoenzyme formylmethanofuran dehydrogenase from Methanosarcina barkeri contains a pterin cofactor. | Karrasch M, Börner G, Enssle M, Thauer RK | 1990 Dec 12 | 2125267 |