Information on EC 1.2.99.9 - formate dehydrogenase (coenzyme F420)

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The expected taxonomic range for this enzyme is: Euryarchaeota

EC NUMBER
COMMENTARY hide
1.2.99.9
-
RECOMMENDED NAME
GeneOntology No.
formate dehydrogenase (coenzyme F420)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
formate + oxidized coenzyme F420 = CO2 + reduced coenzyme F420
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
methanogenesis from CO2
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SYSTEMATIC NAME
IUBMB Comments
formate:coenzyme-F420 oxidoreductase
The enzyme from methanogenic archaea is a involved in formate-dependent H2 production. It contains noncovalently bound FAD [1].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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H2 production and growth are severely reduced in a mutant containing a deletion of the gene encoding the Fdh1 isozyme, indicating that it was the primary Fdh. In contrast, a mutant containing a deletion of the gene encoding the Fdh2 isozyme possesses near-wild-type activities, indicating that this isozyme does not play a major role
physiological function
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a key enzyme for formate-dependent H2 production
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
formate + 2,3,5-triphenyltetrazoIium chloride
CO2 + ?
show the reaction diagram
formate + FAD
CO2 + FADH2
show the reaction diagram
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specific activity 5.4fold lower than for the reaction with coenzyme F420. Vmax /Km is 11fold as compared to reaction with coenzyme F420
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-
?
formate + FMN
CO2 + FMNH2
show the reaction diagram
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specific activity 9.1fold lower than for the reaction with coenzyme F420. Vmax /Km is 6.4fold as compared to reaction with coenzyme F420
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-
?
formate + oxidized benzyl viologen
CO2 + reduced benzyl viologen
show the reaction diagram
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-
-
-
?
formate + oxidized coenzyme F420
CO2 + reduced coenzyme F420
show the reaction diagram
formate + oxidized methyl viologen
CO2 + reduced methyl viologen
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
formate + oxidized coenzyme F420
CO2 + reduced coenzyme F420
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
molybdopterin
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denaturation of the enzyme releases a molybdopterin cofactor, the enzyme contains 1 mol of molybdenum
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
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nonheme iron-sulfur flavoprotein, contains 20.24 iron
Molybdenum
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the purified enzyme contains 0.0074 mM of molybdenum per g of protein
Zn2+
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contains 2 Zn2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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5 mM, 33% inhibition
2,2'-dipyridyl
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5 mM, 87% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.025
FAD
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pH 7.5, temperature not specified in the publication
0.013
FMN
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pH 7.5, temperature not specified in the publication
0.009 - 0.83
formate
0.006
oxidized coenzyme F420
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pH 7.5, temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.039
azide
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pH 7.5, temperature not specified in the publication
0.006
cyanide
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pH 7.5, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0009
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substrate: FMN, pH 7.5, temperature not specified in the publication
0.0016
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substrate: FAD, pH 7.5, temperature not specified in the publication
0.0082
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substrate: oxidized coenzyme F420, pH 7.5, temperature not specified in the publication
0.059
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substrate: oxidized methyl viologen, pH 7.5, temperature not specified in the publication
0.1 - 1
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substrate: coenzyme F420, pH 8.0, temperature not specified in the publication
36.2
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substrate: coenzyme F420, pH and temperature not specified in the publication
447
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substrate: methyl viologen, pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.9
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assayed with coenzyme F420
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3 - 8.3
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pH 7.3: about 40% of maximal activity, pH 8.3: about 70% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
176000
-
gel filtration
288000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
azide, FAD, glycerol, and 2-mercaptoethanol stabilize during purification
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is extremely sensitive to oxygen. The exposure of crude cell-free extract to 101.3 kPa (1 atm) of air results in rapid loss of activity. The removal of air by vacuum degassing with O2-free N2 and the addition of 1 mM sodium dithionite does not restore activity.Sodium azide (10 mM) partially protected the against inactivation by air
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727711
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE