D00459
type: Enzyme
cath: Rossmann fold
ec: https://purl.uniprot.org/enzyme/1.2.1.2
csa: 2nac
uniprot: P33160
kegg enzyme: formate dehydrogenase
kegg enzyme: formate-NAD+ oxidoreductase
kegg enzyme: FDH I
kegg enzyme: FDH II
kegg enzyme: N-FDH
kegg enzyme: formic hydrogen-lyase
kegg enzyme: formate hydrogenlyase
kegg enzyme: hydrogenlyase
kegg enzyme: NAD+-linked formate dehydrogenase
kegg enzyme: NAD+-dependent formate dehydrogenase
kegg enzyme: formate dehydrogenase (NAD+)
kegg enzyme: NAD+-formate dehydrogenase
kegg enzyme: formate benzyl-viologen oxidoreductase
kegg enzyme: formic acid dehydrogenase
kegg pathway: Glyoxylate and dicarboxylate metabolism
kegg pathway: Methane metabolism
kegg substrate: Formate
kegg substrate: NAD+
kegg product: CO2
kegg product: NADH
kegg product: H+
pdb: 2nacA01
pdb: 2nacB01
pdb: 2nadA01
pdb: 2nadB01
pdb: 2nacA02
pdb: 2nacB02
pdb: 2nadA02
pdb: 2nadB02
pdb bound state: Unbound
  compound: Formate
  pdb: 2nacA01
pdb bound state: Unbound
  compound: Formate
  pdb: 2nacB01
pdb bound state: Unbound
  compound: Formate
  pdb: 2nadA01
pdb bound state: Unbound
  compound: Formate
  pdb: 2nadB01
pdb bound state: Unbound
  compound: Formate
  pdb: 2nacA02
pdb bound state: Unbound
  compound: Formate
  pdb: 2nacB02
pdb bound state: Unbound
  compound: Formate
  pdb: 2nadA02
pdb bound state: Unbound
  compound: Formate
  pdb: 2nadB02
pdb bound state: Unbound
  compound: NAD+
  pdb: 2nacA01
pdb bound state: Unbound
  compound: NAD+
  pdb: 2nacB01
pdb bound state: Unbound
  compound: NAD+
  pdb: 2nadA01
pdb bound state: Unbound
  compound: NAD+
  pdb: 2nadB01
pdb bound state: Unbound
  compound: NAD+
  pdb: 2nacA02
pdb bound state: Unbound
  compound: NAD+
  pdb: 2nacB02
pdb bound state: Unbound
  compound: CO2
  pdb: 2nacA01
pdb bound state: Unbound
  compound: CO2
  pdb: 2nacB01
pdb bound state: Unbound
  compound: CO2
  pdb: 2nadA01
pdb bound state: Unbound
  compound: CO2
  pdb: 2nadB01
pdb bound state: Unbound
  compound: CO2
  pdb: 2nacA02
pdb bound state: Unbound
  compound: CO2
  pdb: 2nacB02
active site residues resources: Site-directed mutagenesis of the formate dehydrogenase active centre: role of the His332-Gln313 pair in enzyme catalysis.
active site residues resources: The formate dehydrogenase isolated from the aerobe Methylobacterium sp. RXM is a molybdenum-containing protein.
active site residues resources: Formate dehydrogenase in a reversed micelle system: regulation of catalytic activity and oligomeric composition of the enzyme.
active site residues resources: http://ezcatdb.cbrc.jp/EzCatDB/reference/D00459#22
active site residues resources: P33160
references: Formate dehydrogenase from Pseudomonas oxalaticus.
references: Characterization and spectroscopic properties of reduced Mo and W formate dehydrogenase from C. thermoaceticum.
references: Formate dehydrogenase from Methanobacterium formicicum. Electron paramagnetic resonance spectroscopy of the molybdenum and iron-sulfur centers.
references: Purification and properties of formate dehydrogenase from Pseudomonas aeruginosa. Electron-paramagnetic-resonance studies on the molybdenum centre.
references: http://ezcatdb.cbrc.jp/EzCatDB/reference/D00459#5
references: Electron-paramagnetic-resonance and magnetic-circular-dichroism studies on the formate dehydrogenase-nitrate reductase particle from Pseudomonas aeruginosa.
references: Formate dehydrogenase from Methylosinus trichosporium OB3b. Purification and spectroscopic characterization of the cofactors.
references: Crystal structure of NAD-dependent formate dehydrogenase.
references: Catalytic properties and stability of a Pseudomonas sp.101 formate dehydrogenase mutants containing Cys-255-Ser and Cys-255-Met replacements.
references: Developmental regulation of the gene for formate dehydrogenase in Neurospora crassa.
references: High resolution structures of holo and apo formate dehydrogenase.
references: Site-directed mutagenesis of the formate dehydrogenase active centre: role of the His332-Gln313 pair in enzyme catalysis.
references: The formate dehydrogenase isolated from the aerobe Methylobacterium sp. RXM is a molybdenum-containing protein.
references: Effect of pH on kinetic parameters of NAD+-dependent formate dehydrogenase.
references: Formate dehydrogenase in a reversed micelle system: regulation of catalytic activity and oligomeric composition of the enzyme.
references: Bacterial formate dehydrogenase. Increasing the enzyme thermal stability by hydrophobization of alpha-helices.
references: Stabilization of NAD-dependent formate dehydrogenase from Candida boidinii by site-directed mutagenesis of cysteine residues.
references: Active-site characterization of Candida boidinii formate dehydrogenase.
references: Engineering of coenzyme specificity of formate dehydrogenase from Saccharomyces cerevisiae.
references: Effect of interactions between amino acid residues 43 and 61 on thermal stability of bacterial formate dehydrogenases.
references: Site-directed mutagenesis of the essential arginine of the formate dehydrogenase active centre.

Rossmann fold
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.720
catalytic domain: index.html

Glyoxylate and dicarboxylate metabolism
type: KeggPathway
references: KEGG:MAP00630

Methane metabolism
type: KeggPathway
references: KEGG:MAP00680

Formate
type: KeggSubstrate
references: KEGG:C00058
compound type: carboxyl group
references: CHEBI:30751
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NAD+
type: KeggSubstrate
references: KEGG:C00003
compound type: amide group
compound type: amine group
compound type: nucleotide
references: CHEBI:15846
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

CO2
type: KeggProduct
references: KEGG:C00011
compound type: others
references: CHEBI:16526
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NADH
type: KeggProduct
references: KEGG:C00004
compound type: amide group
compound type: amine group
compound type: nucleotide
references: CHEBI:16908
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

H+
type: KeggProduct
references: KEGG:C00080
compound type: others
references: CHEBI:15378
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

2nacA02
type: Pdb
references: 2nac
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2nac
catalytic residue: ASN 146;ARG 284;GLN 313;HIS 332

2nacB02
type: Pdb
references: 2nac
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2nac
catalytic residue: ASN 146;ARG 284;GLN 313;HIS 332

2nadA02
type: Pdb
references: 2nad
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2nad
catalytic residue: ASN 146;ARG 284;GLN 313;HIS 332

2nadB02
type: Pdb
references: 2nad
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2nad
catalytic residue: ASN 146;ARG 284;GLN 313;HIS 332

Formate dehydrogenase from Pseudomonas oxalaticus.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7144587
journal: Methods Enzymol
volume: 89 Pt D
pages: 531-7
published year: 1982
authors:
  item: Hopner T
  item: Ruschig U
  item: Muller U
  item: Willnow P

Characterization and spectroscopic properties of reduced Mo and W formate dehydrogenase from C. thermoaceticum.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6311213
journal: Biochem Biophys Res Commun
volume: 115
pages: 61-7
published year: 1983
authors:
  item: Durfor CN
  item: Wetherbee PJ
  item: Deaton JC
  item: Solomon EI

Formate dehydrogenase from Methanobacterium formicicum. Electron paramagnetic resonance spectroscopy of the molybdenum and iron-sulfur centers.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6309816
journal: J Biol Chem
volume: 258
pages: 10839-45
published year: 1983
authors:
  item: Barber MJ
  item: Siegel LM
  item: Schauer NL
  item: May HD
  item: Ferry JG

Purification and properties of formate dehydrogenase from Pseudomonas aeruginosa. Electron-paramagnetic-resonance studies on the molybdenum centre.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3038082
journal: Biochem J
volume: 243
pages: 235-9
published year: 1987
authors:
  item: Gadsby PM
  item: Greenwood C
  item: Coddington A
  item: Thomson AJ
  item: Godfrey C

http://ezcatdb.cbrc.jp/EzCatDB/reference/D00459#5
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3038081
journal: Biochem J
volume: 243
pages: 225-33
published year: 1987
authors:
  item: Godfrey C
  item: Coddington A
  item: Greenwood C
  item: Thomson AJ
  item: Gadsby PM
title: Purification and properties of formate dehydrogenase from Pseudomonas aeruginosa. Characterization of haem and iron-sulphur centres by magnetic-circular-dichroism and electron-paramagnetic-resonance spectroscopy.

Electron-paramagnetic-resonance and magnetic-circular-dichroism studies on the formate dehydrogenase-nitrate reductase particle from Pseudomonas aeruginosa.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3038083
journal: Biochem J
volume: 243
pages: 241-8
published year: 1987
authors:
  item: Godfrey C
  item: Gadsby PM
  item: Thomson AJ
  item: Greenwood C
  item: Coddington A

Formate dehydrogenase from Methylosinus trichosporium OB3b. Purification and spectroscopic characterization of the cofactors.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1657982
journal: J Biol Chem
volume: 266
pages: 21853-63
published year: 1991
authors:
  item: Jollie DR
  item: Lipscomb JD

Crystal structure of NAD-dependent formate dehydrogenase.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS)
medline id: 92283270
references: http://www.ncbi.nlm.nih.gov/pubmed/1597184
journal: Eur J Biochem
volume: 206
pages: 441-52
published year: 1992
authors:
  item: Lamzin VS
  item: Aleshin AE
  item: Strokopytov BV
  item: Yukhnevich MG
  item: Popov VO
  item: Harutyunyan EH
  item: Wilson KS
references: P33160

Catalytic properties and stability of a Pseudomonas sp.101 formate dehydrogenase mutants containing Cys-255-Ser and Cys-255-Met replacements.
type: BibliographicResource
comment: MUTAGENESIS OF CYS-255
medline id: 93249485
references: http://www.ncbi.nlm.nih.gov/pubmed/8484798
journal: Biochem Biophys Res Commun
volume: 192
pages: 976-81
published year: 1993
authors:
  item: Tishkov VI
  item: Galkin AG
  item: Marchenko GN
  item: Egorova OA
  item: Sheluho DV
  item: Kulakova LB
  item: Dementieva LA
  item: Egorov AM
references: P33160

Developmental regulation of the gene for formate dehydrogenase in Neurospora crassa.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8509325
journal: J Bacteriol
volume: 175
pages: 3703-9
published year: 1993
authors:
  item: Chow CM
  item: RajBhandary UL

High resolution structures of holo and apo formate dehydrogenase.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/8114093
journal: J Mol Biol
volume: 236
pages: 759-85
published year: 1994
authors:
  item: Lamzin VS
  item: Dauter Z
  item: Popov VO
  item: Harutyunyan EH
  item: Wilson KS
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Site-directed mutagenesis of the formate dehydrogenase active centre: role of the His332-Gln313 pair in enzyme catalysis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8706817
journal: FEBS Lett
volume: 390
pages: 104-8
published year: 1996
authors:
  item: Tishkov VI
  item: Matorin AD
  item: Rojkova AM
  item: Fedorchuk VV
  item: Savitsky PA
  item: Dementieva LA
  item: Lamzin VS
  item: Mezentzev AV
  item: Popov VO

The formate dehydrogenase isolated from the aerobe Methylobacterium sp. RXM is a molybdenum-containing protein.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9020054
journal: Biochem Biophys Res Commun
volume: 230
pages: 30-4
published year: 1997
authors:
  item: Duarte RO
  item: Reis AR
  item: Girio F
  item: Moura I
  item: Moura JJ
  item: Collaco TA

Effect of pH on kinetic parameters of NAD+-dependent formate dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9020883
journal: Biochem J
volume: 321
pages: 475-80
published year: 1997
authors:
  item: Mesentsev AV
  item: Lamzin VS
  item: Tishkov VI
  item: Ustinnikova TB
  item: Popov VO

Formate dehydrogenase in a reversed micelle system: regulation of catalytic activity and oligomeric composition of the enzyme.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9481877
journal: Biochemistry (Mosc)
volume: 62
pages: 1439-43
published year: 1997
authors:
  item: Klyachko NL
  item: Vakula SV
  item: Gladyshev VN
  item: Tishkov VI
  item: Levashov AV

Bacterial formate dehydrogenase. Increasing the enzyme thermal stability by hydrophobization of alpha-helices.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10069397
journal: FEBS Lett
volume: 445
pages: 183-8
published year: 1999
authors:
  item: Rojkova AM
  item: Galkin AG
  item: Kulakova LB
  item: Serov AE
  item: Savitsky PA
  item: Fedorchuk VV
  item: Tishkov VI

Stabilization of NAD-dependent formate dehydrogenase from Candida boidinii by site-directed mutagenesis of cysteine residues.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10691964
journal: Eur J Biochem
volume: 267
pages: 1280-9
published year: 2000
authors:
  item: Slusarczyk H
  item: Felber S
  item: Kula MR
  item: Pohl M

Active-site characterization of Candida boidinii formate dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11171126
journal: Biochem J
volume: 354
pages: 455-63
published year: 2001
authors:
  item: Labrou NE
  item: Rigden DJ

Engineering of coenzyme specificity of formate dehydrogenase from Saccharomyces cerevisiae.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12144528
journal: Biochem J
volume: 367
pages: 841-7
published year: 2002
authors:
  item: Serov AE
  item: Popova AS
  item: Fedorchuk VV
  item: Tishkov VI

Effect of interactions between amino acid residues 43 and 61 on thermal stability of bacterial formate dehydrogenases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12460112
journal: Biochemistry (Mosc)
volume: 67
pages: 1145-51
published year: 2002
authors:
  item: Fedorchuk VV
  item: Galkin AG
  item: Yasny IE
  item: Kulakova LB
  item: Rojkova AM
  item: Filippova AA
  item: Tishkov VI

Site-directed mutagenesis of the essential arginine of the formate dehydrogenase active centre.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11825616
journal: Biochim Biophys Acta
volume: 1594
pages: 136-49
published year: 2002
authors:
  item: Galkin AG
  item: Kutsenko AS
  item: Bajulina NP
  item: Esipova NG
  item: Lamzin VS
  item: Mesentsev AV
  item: Shelukho DV
  item: Tikhonova TV
  item: Tishkov VI
  item: Ustinnikova TB
  item: Popov VO

TransitionStateAnalogue
pdb: 2nadA01
ligand het code: AZI

TransitionStateAnalogue
pdb: 2nadB01
ligand het code: AZI

ReferenceForCatalyticMechanism
reference index: 8
reference section: p.451

ReferenceForCatalyticMechanism
reference index: 11

ReferenceForCatalyticMechanism
reference index: 12
reference section: Fig. 2, p.106

ReferenceForCatalyticMechanism
reference index: 14
reference section: Scheme 1, p.475

ReferenceForCatalyticMechanism
reference index: 21
reference section: p.148