Enzyme

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EC Tree
     1. Oxidoreductases
        1.17 Acting on CH or CH2 groups
            1.17.99 With unknown physiological acceptors
ID:1.17.99.7
Description:Formate dehydrogenase (acceptor).
Alternative Name: Formate dehydrogenase O.
Formate dehydrogenase H.
Prosite: PDOC00392;
PDB:
PDBScop

3D structure

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References

External Links

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:

1.17.99.7;

Phylogenetic Tree:

1.17.99.7;

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

References

TitleAuthorsDatePubMed ID
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 TC1998 Mar 109521673
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 PD1996 Apr 58626495
Escherichia coli formate-hydrogen lyase. Purification and properties of the selenium-dependent formate dehydrogenase component.Axley MJ, Grahame DA, Stadtman TC1990 Oct 252211698