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Enzyme Nomenclature
Information on EC 1.17.1.9 - formate dehydrogenase
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1.17.1.9 formate dehydrogenaseIUBMB Comments
The enzyme from most aerobic organisms is devoid of redox-active centres but that from the proteobacterium Methylosinus trichosporium contains iron-sulfur centres, flavin and a molybdenum centre . Together with EC 1.12.1.2 hydrogen dehydrogenase, forms a system previously known as formate hydrogenlyase.
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Word Map
- 1.17.1.9
- co2
- candida
- boidinii
- methanol
- nitrate
- dioxide
- selenocysteine
- formaldehyde
- selenium
-
methylotrophic
-
methanogen
- hydrogenlyase
- hydrogenases
-
selenoproteins
-
syntrophic
- molybdate
- desulfovibrio
- methanobacterium
-
acetogenic
- pterin
-
molybdoenzyme
- molybdopterin
- succinogenes
- vaccae
- tungstate
-
methanogenesis
-
selenocysteine-containing
- fhl
-
methanol-utilizing
-
wood-ljungdahl
-
mo-containing
- thermoaceticum
-
wolinella
- methanospirillum
-
selenium-dependent
- desulfuricans
-
selenium-containing
-
hydrogenotrophic
-
methanol-grown
- maripaludis
- medicine
- biotechnology
- drug development
- biofuel production
- analysis
- synthesis
The enzyme appears in viruses and cellular organisms
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydrogenase, formate
-
-
-
-
FDB2
FDH
FDH I
FDH II
-
-
-
-
Fdh-H
FDH1
Fdh2
Fdh3
FDHH
FdsABG
FoDH1
formate benzyl-viologen oxidoreductase
-
-
-
-
formate dehydrogenase (NAD)
-
-
-
-
formate dehydrogenase H
formate-NAD oxidoreductase
-
-
-
-
formate:NAD oxidoreductase
-
-
-
-
formic acid dehydrogenase
-
-
-
-
MycFDH
N-FDH
-
-
-
-
NAD+-dependent formate dehydrogenase
NAD-dependent FDH
NAD-dependent formate dehydrogenase
NAD-FDH
NAD-formate dehydrogenase
-
-
-
-
NAD-linked formate dehydrogenase
-
-
-
-
tungsten-containing formate dehydrogenase
FDH
-
-
-
-
FDH
-
-
FDH
-
FDH I
-
-
-
-
NAD+-dependent formate dehydrogenase
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
NAD+-dependent formate dehydrogenase
-
NAD-dependent formate dehydrogenase
-
-
-
-
tungsten-containing formate dehydrogenase
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
formate + NAD+ = CO2 + NADH
ordered kinetic mechanism with NAD+ adding before formate
-
formate + NAD+ = CO2 + NADH
ordered bi-bi mechanism, NAD+ is the first substrate and NADH is the last product
-
formate + NAD+ = CO2 + NADH
ordered BiBi mechanism with NAD+ and NADH being the first substrate and the second product, resp.
-
formate + NAD+ = CO2 + NADH
reaction mechanism: step I, formate binds directly to Mo, displacing Se-Cys140. Step II, the alpha-proton from formate may be transferred to the nearby His141 that acts as general base. Alternatively, step II may involve a selenium-carboxylated intermediate. Step III, electrons from MoIV are transferred via the 4Fe-4S center to an external electron acceptor and the catalytic cycle is completed
formate + NAD+ = CO2 + NADH
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
formate:NAD+ oxidoreductase
The enzyme from most aerobic organisms is devoid of redox-active centres but that from the proteobacterium Methylosinus trichosporium contains iron-sulfur centres, flavin and a molybdenum centre [3]. Together with EC 1.12.1.2 hydrogen dehydrogenase, forms a system previously known as formate hydrogenlyase.
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CAS REGISTRY NUMBER
COMMENTARY
9028-85-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CO2 + reduced 1,1'-diaminoethyl-4,4'-bipyridinium salt
formate + 1,1'-diaminoethyl-4,4'-bipyridinium salt
-
-
-
?
CO2 + reduced 1,1'-dicarboxyl-4,4'-bipyridinium salt
formate + 1,1'-dicarboxyl-4,4'-bipyridinium salt
-
-
-
?
CO2 + reduced 1,1'-diphenyl-4,4'-bipyridinium salt
formate + 1,1'-diphenyl-4,4'-bipyridinium salt
-
-
-
?
CO2 + reduced 1-methyl-1'-aminoethyl-4,4'-bipyridinium salt
formate + 1-methyl-1'-aminoethyl-4,4'-bipyridinium salt
-
-
-
?
CO2 + reduced 1-methyl-1'-carboxymethyl-4,4'-bipyridinium salt
formate + 1-methyl-1'-carboxymethyl-4,4'-bipyridinium salt
-
-
-
?
formate + 3-acetylpyridine-NAD+
CO2 + 3-acetylpyridine-NADH
-
-
-
-
r
formate + 3-pyridinecarboxaldehyde-NAD+
CO2 + 3-pyridinecarboxaldehyde-NADH
-
-
-
-
?
formate + benzyl viologen
CO2 + reduced benzyl viologen + H+
-
-
-
-
?
formate + dextran-NAD+
CO2 + dextran-NADH
-
enzyme immobilized on glyoxyl agarose, 60% of the activity with NAD+
-
-
?
formate + NADP+
CO2 + NAPDH
-
NADP+ is a substrate for mutant enzymes only
-
-
?
CO2 + NADH
formate + NAD+
-
the enzyme exhibits a dramatic preference for the CO2 reduction reaction over the oxidation reaction of formate
-
-
r
CO2 + NADH
formate + NAD+
-
the enzyme exhibits a dramatic preference for the CO2 reduction reaction over the oxidation reaction of formate
-
-
r
formate + 2,6-dichloroindophenol
CO2 + reduced 2,6-dichlorophenolindophenol
-
54% of the activity with NAD+
-
-
?
formate + 2,6-dichloroindophenol
CO2 + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
formate + 2,6-dichloroindophenol
CO2 + reduced 2,6-dichlorophenolindophenol
-
33% of the activity with NAD+
-
-
?
formate + 2,6-dichloroindophenol
CO2 + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
formate + 2,6-dichlorophenolindophenol
CO2 + reduced 2,6-dichlorophenolindophenol
-
-
-
-
r
formate + 2,6-dichlorophenolindophenol
CO2 + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
formate + 2,6-dichlorophenolindophenol
CO2 + reduced 2,6-dichlorophenolindophenol
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
-
-
-
?
formate + 2,6-dichlorophenolindophenol
CO2 + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
formate + benzyl viologen
CO2 + reduced benzyl viologen
-
113% of the activity with NAD+
-
-
?
formate + benzyl viologen
CO2 + reduced benzyl viologen
-
-
-
-
r
formate + benzyl viologen
CO2 + reduced benzyl viologen
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
-
-
-
?
formate + ferricyanide
CO2 + ferrocyanide
-
10% of the activity with NAD+
-
-
?
formate + methyl viologen
CO2 + reduced methyl viologen
-
74% of the activity with NAD+
-
-
?
formate + methyl viologen
CO2 + reduced methyl viologen
-
-
-
-
?
formate + methylene blue
CO2 + reduced methylene blue
-
119% of the activity with NAD+
-
-
?
formate + methylene blue
CO2 + reduced methylene blue
-
-
-
-
?
formate + NAD+
CO2 + NADH
the enzyme shows strict substrate specificity for formate
-
-
?
formate + NAD+
CO2 + NADH
the enzyme shows strict substrate specificity for formate
-
-
?
formate + NAD+
CO2 + NADH
Candida methanolica
-
one of the key enzymes in the assimilation of C1 compounds, such as methanol
-
-
?
formate + NAD+
CO2 + NADH
-
equilibrium strongly favors dehydrogenation of formate
-
-
r
formate + NAD+
CO2 + NADH
-
enzyme catalyzes formate oxidation about 30times faster than the CO2 reduction
-
-
r
formate + NAD+
CO2 + NADH
-
when Pseudomonas oxalaticus is grown on formate as main carbon and energy source, formate dehydrogenase is the key enzyme that generates NADH and CO
-
-
?
formate + NAD+
CO2 + NADH
-
equilibrium strongly favors dehydrogenation of formate
-
-
r
formate + NAD+
CO2 + NADH
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
FDH1 exhibits absolute specificity for formate and NAD+
-
-
?
formate + NAD+
CO2 + NADH
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
?
formate + NAD+
CO2 + NADH
any one of the three formate dehydrogenases Fdh1, Fdh2 or Fdh3 is sufficient to sustain growth on formate. None is required for growth on methanol or methylamine
-
-
?
formate + NAD+
CO2 + NADH
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
-
-
-
?
formate + NAD+
CO2 + NADH
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
-
-
?
formate + NAD+
CO2 + NADH
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
any one of the three formate dehydrogenases Fdh1, Fdh2 or Fdh3 is sufficient to sustain growth on formate. None is required for growth on methanol or methylamine
-
-
?
formate + NAD+
CO2 + NADH
-
the level of formate dehydrogenase is considerably diminished without molybdenum, and in the presence of tungsten the activity was not detected in significant amounts
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
role of formate dehydrogenase in detoxification of exogenous formate
-
-
?
formate + NAD+
CO2 + NADH
wild-type enzyme shows no activity with NADP+, mutant enzyme D196A/Y197R shows higher activity with NADP+ than with NAD+
-
-
?
formate + NAD+
CO2 + NADH
-
the enzyme exhibits a dramatic preference for the CO2 reduction reaction over the oxidation reaction of formate
-
-
r
formate + NAD+
CO2 + NADH
-
the enzyme exhibits a dramatic preference for the CO2 reduction reaction over the oxidation reaction of formate
-
-
r
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
last enzyme of the dissimilatory pathway of the methanol metabolism
-
-
?
formate + NAD+
CO2 + NADH
FDH is highly specific to NAD+ and virtually fails to catalyze the reaction with NADP+
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
100% specificity
-
-
?
formate + NAD+
CO2 + NADH + H+
100% specificity
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NADP+
CO2 + NADPH
activity with NADP+ is 2.4% of the activity with NAD+
-
-
?
formate + NADP+
CO2 + NADPH
activity with NADP+ is 2.4% of the activity with NAD+
-
-
?
formate + NADP+
CO2 + NADPH
FDH1 uses NADP+ with low specificity compared to NAD+
-
-
?
formate + NADP+
CO2 + NADPH
-
NADP+ is substrate for several mutant enzymes
-
-
?
formate + NADP+
CO2 + NADPH
-
NADP+ is substrate for several mutant enzymes
-
-
?
formate + NADP+
CO2 + NADPH
NADP+ is a substrate for mutant enzyme D221S only
-
-
?
formate + NADP+
CO2 + NADPH
wild-type enzyme shows no activity, mutant enzyme D196A/Y197R shows higher activity with NADP+ than with NAD+
-
-
?
formate + NADP+
CO2 + NADPH
FDH is highly specific to NAD+ and virtually fails to catalyze the reaction with NADP+
-
-
?
formate + NADP+
CO2 + NADPH
-
no reaction is catalyzed with wild-type enzyme, activity is detected with mutant enzyme D195S. The ratio of the catalytic efficiencies for NAD+ versus NADP+ for the mutant protein is 40:1 in favor of NAD+
-
-
?
formate + NADP+
CO2 + NADPH + H+
the wild type enzyme virtually fails to catalyze the reaction with NADP+
-
-
?
formate + nitrobluetetrazolium
CO2 + reduced nitrobluetetrazolium
-
54% of the activity with NAD+
-
-
?
formate + nitrobluetetrazolium
CO2 + reduced nitrobluetetrazolium
-
-
-
-
?
formate + phenazine methosulfate
CO2 + reduced phenazine methosulfate
-
-
-
-
?
formate + phenazine methosulfate
CO2 + reduced phenazine methosulfate
-
no activity
-
-
?
NADH + 2,6-dichloroindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
NADH + 2,6-dichloroindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
S-formylglutathione + NAD+
?
-
about 40fold lower Km-value than with formate
-
-
?
S-formylglutathione + NAD+
?
-
lower KM-value than for formate but maximal activity is only 5.5% of that of formate
-
-
?
additional information
?
-
the enzyme shows no activity when methanol, ethanol, formaldehyde, sodium acetate, sodium malate, sodium oxalate, sodium lactate, sodium succinate, sodium citrate and sodium nitrate are used as the sole substrate
-
-
?
additional information
?
-
-
the enzyme shows no activity when methanol, ethanol, formaldehyde, sodium acetate, sodium malate, sodium oxalate, sodium lactate, sodium succinate, sodium citrate and sodium nitrate are used as the sole substrate
-
-
?
additional information
?
-
the enzyme shows no activity when methanol, ethanol, formaldehyde, sodium acetate, sodium malate, sodium oxalate, sodium lactate, sodium succinate, sodium citrate and sodium nitrate are used as the sole substrate
-
-
?
additional information
?
-
no activity with NADP+
-
-
?
additional information
?
-
-
possible role of enzyme in oxalate metabolism
-
-
?
additional information
?
-
-
no substrate: acetate, pyruvate, malate, oxalate, succinate, methanol, isocitrate, fumarate
-
-
?
additional information
?
-
no activity with malate, lactate, glycolate, pyruvate, and glyoxylate
-
-
?
additional information
?
-
no activity with malate, lactate, glycolate, pyruvate, and glyoxylate
-
-
?
additional information
?
-
-
no activity with malate, lactate, glycolate, pyruvate, and glyoxylate
-
-
?
additional information
?
-
no activity with malate, lactate, glycolate, pyruvate, and glyoxylate
-
-
?
additional information
?
-
no activity with malate, lactate, glycolate, pyruvate, and glyoxylate
-
-
?
additional information
?
-
-
S-formylglutathione rather than free formate is an intermediate in oxidation of methanol by yeast
-
-
?
additional information
?
-
-
S-formylglutathione rather than free formate is an intermediate in oxidation of methanol by yeast
-
-
?
additional information
?
-
-
the enzyme also exhibits nitrate reductase activity with methyl viologen as cosubstrate
-
-
?
additional information
?
-
-
no activity with oxalate, malonate, succinate, malate, glycolate, acetate, lactate, maleate, citrate, and chloride
-
-
?
additional information
?
-
no activity with methanol, formaldehyde, ethanol, sodium acetate, sodium propionate, sodium oxalate, and sodium citrate
-
-
?
additional information
?
-
-
no activity with methanol, formaldehyde, ethanol, sodium acetate, sodium propionate, sodium oxalate, and sodium citrate
-
-
?
additional information
?
-
-
the enzyme also can act as a decarboxylase with mesoxalate
-
-
?
additional information
?
-
the enzyme also can act as a decarboxylase with mesoxalate
-
-
?
additional information
?
-
-
the wild type enzyme shows no activity with NADP+
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
formate + NADP+
CO2 + NAPDH
-
NADP+ is a substrate for mutant enzymes only
-
-
?
CO2 + NADH
formate + NAD+
-
the enzyme exhibits a dramatic preference for the CO2 reduction reaction over the oxidation reaction of formate
-
-
r
CO2 + NADH
formate + NAD+
-
the enzyme exhibits a dramatic preference for the CO2 reduction reaction over the oxidation reaction of formate
-
-
r
formate + NAD+
CO2 + NADH
the enzyme shows strict substrate specificity for formate
-
-
?
formate + NAD+
CO2 + NADH
the enzyme shows strict substrate specificity for formate
-
-
?
formate + NAD+
CO2 + NADH
Candida methanolica
-
one of the key enzymes in the assimilation of C1 compounds, such as methanol
-
-
?
formate + NAD+
CO2 + NADH
-
when Pseudomonas oxalaticus is grown on formate as main carbon and energy source, formate dehydrogenase is the key enzyme that generates NADH and CO
-
-
?
formate + NAD+
CO2 + NADH
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
any one of the three formate dehydrogenases Fdh1, Fdh2 or Fdh3 is sufficient to sustain growth on formate. None is required for growth on methanol or methylamine
-
-
?
formate + NAD+
CO2 + NADH
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
-
-
-
?
formate + NAD+
CO2 + NADH
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
any one of the three formate dehydrogenases Fdh1, Fdh2 or Fdh3 is sufficient to sustain growth on formate. None is required for growth on methanol or methylamine
-
-
?
formate + NAD+
CO2 + NADH
-
the level of formate dehydrogenase is considerably diminished without molybdenum, and in the presence of tungsten the activity was not detected in significant amounts
-
-
?
formate + NAD+
CO2 + NADH
-
role of formate dehydrogenase in detoxification of exogenous formate
-
-
?
formate + NAD+
CO2 + NADH
-
the enzyme exhibits a dramatic preference for the CO2 reduction reaction over the oxidation reaction of formate
-
-
r
formate + NAD+
CO2 + NADH
-
the enzyme exhibits a dramatic preference for the CO2 reduction reaction over the oxidation reaction of formate
-
-
r
formate + NAD+
CO2 + NADH
-
last enzyme of the dissimilatory pathway of the methanol metabolism
-
-
?
formate + NADP+
CO2 + NADPH
-
NADP+ is substrate for several mutant enzymes
-
-
?
formate + NADP+
CO2 + NADPH
-
NADP+ is substrate for several mutant enzymes
-
-
?
additional information
?
-
the enzyme shows no activity when methanol, ethanol, formaldehyde, sodium acetate, sodium malate, sodium oxalate, sodium lactate, sodium succinate, sodium citrate and sodium nitrate are used as the sole substrate
-
-
?
additional information
?
-
-
the enzyme shows no activity when methanol, ethanol, formaldehyde, sodium acetate, sodium malate, sodium oxalate, sodium lactate, sodium succinate, sodium citrate and sodium nitrate are used as the sole substrate
-
-
?
additional information
?
-
the enzyme shows no activity when methanol, ethanol, formaldehyde, sodium acetate, sodium malate, sodium oxalate, sodium lactate, sodium succinate, sodium citrate and sodium nitrate are used as the sole substrate
-
-
?
additional information
?
-
-
possible role of enzyme in oxalate metabolism
-
-
?
additional information
?
-
-
S-formylglutathione rather than free formate is an intermediate in oxidation of methanol by yeast
-
-
?
additional information
?
-
-
S-formylglutathione rather than free formate is an intermediate in oxidation of methanol by yeast
-
-
?
additional information
?
-
-
the wild type enzyme shows no activity with NADP+
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
molybdopterin
-
the alpha-subunit contains a putative binding motif for the molybdopterin cofactor
FMN
-
formate dehydrogenase I contains 1 mol of FMN per mol of enzyme, formate dehydrogenase II contains 2 mol of FMN per mol of enzyme
FMN
-
contains 0.6 mol of noncovalently bound FMN per mol of enzyme. The beta-subunit contains a putative binding motif for NAD+
NAD+
-
-
NAD+
-
-
287875, 287889, 288099, 288108, 288110, 288119, 656695, 686449, 687304, 699307, 700012, 711548, 711549, 713421, 724766, 725739, 726088, 740947, 742266
NAD+
-
the beta-subunit contains a putative binding motif for NAD+. No activity with NADP+
NAD+
wild-type enzyme shows no activity with NADP+, mutant enzyme D196A/Y197R shows higher activity with NADP+ than with NAD+
NAD+
FDH1 shows activity using NAD+ or NADP+, FDH1 is highly specific to NAD+ compared to NADP+
NADP+
-
no reaction is catalyzed with wild-type enzyme, activity is detected with mutant enzyme D195S. The ratio of the catalytic efficiencies for NAD+ versus NADP+ for the mutant protein is 40:1 in favor of NAD+
NADP+
wild-type enzyme shows no activity with NADP+, mutant enzyme D196A/Y197R shows higher activity with NADP+ than with NAD+
NADP+
the wild type enzyme virtually fails to use NADP+ as a cofacor
NADP+
FDH1 shows activity using NAD+ or NADP+, FDH1 is highly specific to NAD+ compared to NADP+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Fe
Fe2+
the enzyme activity is increased 49.4% over the control by 1 mM Fe2+
Iron
-
contains 5 mol nonheme iron per mol of enzyme. The beta-subunit contains a putative binding motif for an iron-sulfur cluster. The alpha-subunit contains at least one iron-sulfur cluster
K+
the enzyme activity is increased 6.7% over the control by 1 mM K+
Li+
the enzyme activity is increased 13.8% over the control by 1 mM Li+
Mg2+
the enzyme activity is increased 7.6% over the control by 1 mM Mg2+
Mn2+
the enzyme activity is increased 29.8% over the control by 1 mM Mn2+
Molybdenum
additional information
Ca2+
the enzyme activity is increased 13.8% over the control by 1 mM Ca2+
Co2+
the enzyme activity is increased 9.8% over the control by 1 mM Co2+
Fe
-
formate dehydrogenase I contains 18-25 mol of iron per mol of enzyme. Formate dehydrogenase II contains 6-10 mol of iron per mol of enzyme
Molybdenum
-
0.64 gatom per mol of enzyme. The enzyme contains molybdopterin guanine dinucleotide
additional information
no divalent metal cation is needed as a cofactor for enzyme activity
additional information
no divalent metal cation is needed as a cofactor for enzyme activity
additional information
-
no divalent metal cation is needed as a cofactor for enzyme activity
additional information
Mn2+, Ba2+, and Mg2+ do not significantly change the enzyme activity
additional information
Li+, Na+, K+, NH4+, Cl?, HPO42-, HCO3-, and SO42- at 100 mM have scarcely effect on the enzymatic activity. The enzyme activity is very slightly increased in the presence of 1 mM Co2+, Ni2+, Cu2+, Zn2+, Fe3+, Mn2+, Mg2+, Ca2+, and NH4+
additional information
-
Li+, Na+, K+, NH4+, Cl?, HPO42-, HCO3-, and SO42- at 100 mM have scarcely effect on the enzymatic activity. The enzyme activity is very slightly increased in the presence of 1 mM Co2+, Ni2+, Cu2+, Zn2+, Fe3+, Mn2+, Mg2+, Ca2+, and NH4+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-methyl-3-methylimidazolium dimethylphosphate
-
adding more than 40% (v/v) of 1-methyl-3-methylimidazolium dimethylphosphate inactivates formate dehydrogenase. In the presence of 30% (v/v) 1-methyl-3-methylimidazolium dimethylphosphate, the catalytic efficiency of the wild type enzyme is reduced by 2.8fold
2,3-Butanedione
Achromobacter parvulus
-
modification of 12 Arg residues per molecule results in complete inactivation. NAD+ protects
2-chloro-1-(3-pyridyl)-ethanone
-
20 mM, pH 6.5, 30°C, 5 h, 10% loss of activity
dimethylimidazolium dimethyl phosphate
FDh is inactivated and unstable in the presence of high concentration (above 50%) of the water soluble dimethylimidazolium dimethyl phosphate ionic liquid
ethyl 4-chloroacetoacetate
-
the D221G mutant is extremely sensitive to ethyl 4-chloroacetoacetate with half-lives shorter than 6 min
ethyl-4-chloroacetoacetate
-
wild-type, 7.43% residual activity at 20 mM
oxidized ADP
-
inactivates by specific reaction at the nucleotide binding site, with negative cooperativity between subunits accounting for appearance of two phases of inactivation, protection by NAD+, NADH and ADP
Sodium azide
94% inhibition at 1 mM; 99% inhibition at 1 mM
Cu2+
82 inhibition at 1 mM; complete inhibition at 1 mM
N3-
-
0.25 mM. Inhibition is partly overcome by addition of formate or NAD+
N3-
-
0.25 mM. Inhibition is partly overcome by addition of formate or NAD+
NADH
-
inhibition is partly overcome by addition of formate or NAD+
NADH
66% inhibition at 0.12 mM; 73% inhibition at 0.12 mM
NADPH
26% inhibition at 0.24 mM; 58% inhibition at 0.24 mM
NO3-
-
0.25 mM. Inhibition is partly overcome by addition of formate or NAD+
additional information
no notable effect on the enzyme activity is observed when adding NH4+ or HPO2-
-
additional information
-
no notable effect on the enzyme activity is observed when adding NH4+ or HPO2-
-
additional information
-
not inhibitory: Mg2+, Mn2+, Co2+, Ni2+, Cd2+, Zn2+, Ca2+, Fe2+, Fe3+, Cu2+
-
additional information
-
no loss of activity after 5 h at pH 6.5, 30°C, after 5 h with 20 mM ethyl 4-chloro-3-oxobutanoate, 20 mM ethyl-4-bromo-3-oxobutanoate, 20 mM ethyl 2-chloro-3-oxobutanoate, or 20 mM 2,3'-dichloroacetophenone
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
the enzyme activity is increased 12% over the control by 1 mM EDTA
formate
-
activates in a slow reaction of which the velocity is dependent on the concentration of formate
KCl
-
adding 5 mM NAD+ in 0.2 M KCl improves the FDH elution and increases the specific FDH activity by 1.38fold as compared to elution with 1 M KCl
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.1
ethyl formate
-
in 100 mM potassium phosphate buffer at pH 7.5, at 30°C
2.9
methyl formate
-
in 100 mM potassium phosphate buffer at pH 7.5, at 30°C
1.7
phenyl formate
-
in 100 mM potassium phosphate buffer at pH 7.5, at 30°C
4.7
propyl formate
-
in 100 mM potassium phosphate buffer at pH 7.5, at 30°C
0.017
reduced 1,1'-diaminoethyl-4,4'-bipyridinium salt
at pH 7.4, temperature not specified in the publication
0.371
reduced 1,1'-dicarboxyl-4,4'-bipyridinium salt
at pH 7.4, temperature not specified in the publication
0.118
reduced 1-methyl-1'-aminoethyl-4,4'-bipyridinium salt
at pH 7.4, temperature not specified in the publication
0.292
reduced 1-methyl-1'-carboxymethyl-4,4'-bipyridinium salt
at pH 7.4, temperature not specified in the publication
0.212
reduced methyl viologen
at pH 7.4, temperature not specified in the publication
0.037
2,6-dichlorophenolindophenol
-
formate dehydrogenase I, reaction with formate
0.042
2,6-dichlorophenolindophenol
-
formate dehydrogenase II, reaction with formate
0.2
2,6-dichlorophenolindophenol
-
formate dehydrogenase I or formate dehydrogenase II, reaction with NADH
0.24
benzyl viologen
-
formate dehydrogenase II, reaction with formate
0.25
benzyl viologen
-
formate dehydrogenase I, reaction with formate
6.5
CO2
wild type enzyme, pH and temperature not specified in the publication
7.5
CO2
mutant enzyme A198G, pH and temperature not specified in the publication
32
CO2
mutant enzyme D221S, pH and temperature not specified in the publication
0.46
ferricyanide
-
formate dehydrogenase I, reaction with formate
0.5
ferricyanide
-
formate dehydrogenase II, reaction with formate
0.62
ferricyanide
-
formate dehydrogenase II, reaction with NADH
0.69
ferricyanide
-
formate dehydrogenase I, reaction with NADH
0.011
formate
-
pH 7.5, 30°C, enzyme from Sephadex G-15 desalted fraction
0.277
formate
-
with 2,6-dichlorophenolindophenol as cosubstrate, at pH 9.0 and 30°C
0.9
formate
-
mutant enzyme F290Y, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
1.1
formate
-
mutant enzyme F290A, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
1.2
formate
-
mutant enzyme F290Q, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
1.3
formate
-
mutant enzyme F290T, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
1.5
formate
-
wild type enzyme, in 0.1 M sodium phosphate buffer, pH 7.0, at 30°C
1.5
formate
-
wild type enzyme, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
2 - 3
formate
-
mutant enzyme D221A, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
2.9
formate
-
mutant enzyme F290E, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
3.2
formate
-
wild type enzyme, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
3.7
formate
-
mutant enzyme F311Y, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
4.1
formate
-
mutant enzyme F290S, in 0.1 M sodium phosphate buffer, pH 7.0, at 30°C
4.1
formate
-
mutant enzyme F290S, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
4.2
formate
-
wild type enzyme, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
4.5
formate
-
mutant enzyme F290N, in 0.1 M sodium phosphate buffer, pH 7.0, at 30°C
4.5
formate
-
mutant enzyme F290N, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
5
formate
mutant enzyme K328V, at 20°C, after 2 weeks or 4 months of enzyme storage
5
formate
-
mutant enzyme F290D, in 0.1 M sodium phosphate buffer, pH 7.0, at 30°C
5
formate
-
mutant enzyme F290D, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
5.63
formate
-
wild type enzyme, at 20°C, in 20 mM triethanolamine at pH 8
6
formate
-
oxidized mutant enzyme T169C/T226C, at 20°C, in 20 mM triethanolamine at pH 8
10.8
formate
-
reduced mutant enzyme T169C/T226C, at 20°C, in 20 mM triethanolamine at pH 8
16
formate
mutant enzyme K47E, at 20°C, after 2 weeks of enzyme storage
19.2
formate
-
mutant enzyme F311N, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
19.6
formate
with NAD+ as cosubstrate, in 100 mM Tris-HCl (pH 7.0), at 30°C
20
formate
mutant enzyme K47E, at 20°C, after 4 months of enzyme storage
20
formate
native wild type enzyme, at 20°C, after 2 weeks of enzyme storage
22.7
formate
-
mutant enzyme F311S, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
29.8
formate
-
mutant enzyme F311D, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
30
formate
-
with 3-pyridinecarboxaldehyde-NAD+ as electron acceptor
35
formate
native wild type enzyme, at 20°C, after 4 months of enzyme storage
39.1
formate
with NADP+ as cosubstrate, in 100 mM Tris-HCl (pH 7.0), at 30°C
40
formate
-
mutant enzyme D221G, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
41
formate
-
mutant enzyme D221S, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
46
formate
-
mutant enzyme D221Q, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
57
formate
-
mutant enzyme C145S/D221A/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
62
formate
-
mutant enzyme D221G/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
69
formate
-
mutant enzyme C145S/D221G/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
81
formate
-
mutant enzyme C145S/A198G/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
83
formate
-
mutant enzyme C145S/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
98
formate
-
mutant enzyme C145S/A198G/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 30°C
113
formate
-
mutant enzyme C145S/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 30°C
127
formate
-
mutant enzyme A198G/D221Q, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
1000
formate
pH 7.0, 30°C, mutant enzyme D196A/Y197R, reaction with NADP+
0.0086
NAD+
-
mutant enzyme F290A, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
0.0091
NAD+
-
mutant enzyme F290S, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
0.0109
NAD+
-
mutant enzyme F290Y, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
0.0117
NAD+
-
mutant enzyme F290Q, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
0.0128
NAD+
-
mutant enzyme F290D, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
0.0133
NAD+
-
wild type enzyme, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication