Information on EC 1.2.2.1 - formate dehydrogenase (cytochrome)

for references in articles please use BRENDA:EC1.2.2.1
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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
1.2.2.1
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RECOMMENDED NAME
GeneOntology No.
formate dehydrogenase (cytochrome)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
formate + 2 ferricytochrome b1 = CO2 + 2 ferrocytochrome b1 + 2 H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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-
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reduction
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-
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Glyoxylate and dicarboxylate metabolism
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SYSTEMATIC NAME
IUBMB Comments
formate:ferricytochrome-b1 oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
37251-01-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
N.C.T.C. 6750
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Manually annotated by BRENDA team
N.C.T.C. 6750
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-
Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
formate + ferricytochrome b
CO2 + ferrocytochrome b
show the reaction diagram
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?
additional information
?
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crude extract of Escherichia coli is investigated for formic dehydrogenase activity. The extract is very active with methylene blue in the presence of formate. Spectroscopic examination shows that the formic dehydrogenase of the extract reacts normally with O2 through cytochrome b
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome c
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in its purest state the enzyme contains one molecule of cytochrome co-ordinated by two histidine side chains in the oxidized state
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Molybdenum
Se
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enzyme from cells grown in selenite contains selenium, covalently bound to the largest subunit
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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FdhE binds to the molybdoprotein subunits (FdnG and FdoG) of the respiratory formate dehydrogenase
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
420
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preparation I, 30°C
752
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preparation II, 30°C
760
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preparation III, 30°C
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
330000
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gel filtration
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of sodium dithionite stabilizes the enzyme
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663912
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.2.2.1)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)