EC Tree |
1. Oxidoreductases |
1.17 Acting on CH or CH2 groups |
1.17.99 With unknown physiological acceptors |
ID: | 1.17.99.7 | ||
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Description: | Formate dehydrogenase (acceptor). | ||
Alternative Name: |
Formate dehydrogenase O. Formate dehydrogenase H. | ||
Prosite: | PDOC00392; | ||
PDB: |
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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 1.17.99.7 |
BRENDA Enzyme Link: | BRENDA 1.17.99.7 |
KEGG Enzyme Link: | KEGG1.17.99.7 |
BioCyc Enzyme Link: | BioCyc 1.17.99.7 |
ExPASy Enzyme Link: | ExPASy1.17.99.7 |
EC2PDB Enzyme Link: | EC2PDB 1.17.99.7 |
ExplorEnz Enzyme Link: | ExplorEnz 1.17.99.7 |
PRIAM enzyme-specific profiles Link: | PRIAM 1.17.99.7 |
IntEnz Enzyme Link: | IntEnz 1.17.99.7 |
MEDLINE Enzyme Link: | MEDLINE 1.17.99.7 |
MSA: | |
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Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
RHEA:27290 | A + formate + H(+) = AH2 + CO2 |
RULE(radius=1) | [*:1]=[CH;+0:2]-[OH;+0:3].[H+;H0:4]>>[*:1]=[C;H0;+0:2]=[O;H0;+0:3] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
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Selenium-containing formate dehydrogenase H from Escherichia coli: a molybdopterin enzyme that catalyzes formate oxidation without oxygen transfer. | Khangulov SV, Gladyshev VN, Dismukes GC, Stadtman TC | 1998 Mar 10 | 9521673 |
Characterization of crystalline formate dehydrogenase H from Escherichia coli. Stabilization, EPR spectroscopy, and preliminary crystallographic analysis. | Gladyshev VN, Boyington JC, Khangulov SV, Grahame DA, Stadtman TC, Sun PD | 1996 Apr 5 | 8626495 |
Escherichia coli formate-hydrogen lyase. Purification and properties of the selenium-dependent formate dehydrogenase component. | Axley MJ, Grahame DA, Stadtman TC | 1990 Oct 25 | 2211698 |