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2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
4-(formyloxy)butyl acetate + NAD+
?
-
59% conversion
-
-
?
butyl formate + NAD+
?
-
41% conversion
-
-
?
CO2 + NADH
formate + NAD+
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
-
-
-
?
CO2 + reduced methyl viologen
formate + methyl viologen
-
-
-
?
formate + 2,6-dichloroindophenol
CO2 + reduced 2,6-dichlorophenolindophenol
formate + 2,6-dichlorophenolindophenol
CO2 + reduced 2,6-dichlorophenolindophenol
formate + 3-acetylpyridine-NAD+
CO2 + 3-acetylpyridine-NADH
-
-
-
-
r
formate + 3-pyridinecarboxaldehyde-NAD+
CO2 + 3-pyridinecarboxaldehyde-NADH
-
-
-
-
?
formate + benzyl viologen
CO2 + reduced benzyl viologen
formate + benzyl viologen
CO2 + reduced benzyl viologen + H+
-
-
-
-
?
formate + cytochrome c
CO2 + reduced cytochrome c
-
-
-
-
?
formate + deamino-NAD+
CO2 + deamino-NADH
-
-
-
-
r
formate + dextran-NAD+
CO2 + dextran-NADH
-
enzyme immobilized on glyoxyl agarose, 60% of the activity with NAD+
-
-
?
formate + FAD
CO2 + FADH2
-
-
-
-
?
formate + ferricyanide
CO2 + ferrocyanide
formate + FMN
CO2 + FMNH2
formate + methyl viologen
CO2 + reduced methyl viologen
formate + methylene blue
CO2 + reduced methylene blue
formate + NAD+
CO2 + NADH
formate + NAD+
CO2 + NADH + H+
formate + NAD+
HCO3- + NADH
formate + NADP+
CO2 + NADPH
formate + NADP+
CO2 + NADPH + H+
formate + NADP+
CO2 + NAPDH
-
NADP+ is a substrate for mutant enzymes only
-
-
?
formate + nitrobluetetrazolium
CO2 + reduced nitrobluetetrazolium
formate + O2
CO2 + H2O2
-
-
-
?
formate + phenazine methosulfate
CO2 + reduced phenazine methosulfate
formate + riboflavin
CO2 + reduced riboflavin
-
-
-
-
?
formate + thio-NAD+
CO2 + thio-NADH
-
-
-
-
r
glyoxylate + NAD+
? + NADH
-
wild-type, low activity towards glyoxylate
-
-
?
HCO3- + NADH
formate + NAD+
methyl formate + NAD+
?
-
23% conversion
-
-
?
NADH + 2,6-dichloroindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
NADH + benzyl viologen
NAD+ + reduced benzyl viologen
-
-
-
-
?
phenyl formate + NAD+
?
-
86% conversion
-
-
?
propyl formate + NAD+
?
-
39% conversion
-
-
?
S-formylglutathione + NAD+
?
S-formylthioglycolate + NAD+
?
-
-
-
-
?
additional information
?
-
2 ferricyanide + NADH

2 ferrocyanide + NAD+ + H+
-
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
-
?
CO2 + NADH

formate + NAD+
-
-
-
r
CO2 + NADH
formate + NAD+
-
-
-
r
CO2 + NADH
formate + NAD+
-
-
-
-
r
CO2 + NADH
formate + NAD+
-
-
-
-
r
CO2 + NADH
formate + NAD+
-
-
-
-
?
CO2 + NADH
formate + NAD+
-
-
-
-
?
CO2 + NADH
formate + NAD+
-
-
-
r
CO2 + NADH
formate + NAD+
-
-
-
r
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
CO2 + NADH
formate + NAD+
-
-
-
?
ethyl formate + NAD+

?
-
-
-
-
?
ethyl formate + NAD+
?
-
26% conversion
-
-
?
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
-
-
-
-
?
formate + 2,6-dichlorophenolindophenol
CO2 + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
formate + benzyl viologen

CO2 + reduced benzyl viologen
-
-
-
-
?
formate + benzyl viologen
CO2 + reduced benzyl viologen
-
113% of the activity with NAD+
-
-
?
formate + benzyl viologen
CO2 + reduced benzyl viologen
-
-
-
-
?
formate + benzyl viologen
CO2 + reduced benzyl viologen
-
-
-
-
r
formate + benzyl viologen
CO2 + reduced benzyl viologen
-
-
-
-
r
formate + benzyl viologen
CO2 + reduced benzyl viologen
-
-
-
-
?
formate + benzyl viologen
CO2 + reduced benzyl viologen
-
-
-
-
?
formate + benzyl viologen
CO2 + reduced benzyl viologen
-
-
-
-
?
formate + ferricyanide

CO2 + ferrocyanide
-
10% of the activity with NAD+
-
-
?
formate + ferricyanide
CO2 + ferrocyanide
-
-
-
-
?
formate + ferricyanide
CO2 + ferrocyanide
-
-
-
-
?
formate + ferricyanide
CO2 + ferrocyanide
-
-
-
-
?
formate + FMN

CO2 + FMNH2
-
-
-
-
?
formate + FMN
CO2 + FMNH2
-
-
-
-
?
formate + methyl viologen

CO2 + reduced methyl viologen
-
74% of the activity with NAD+
-
-
?
formate + methyl viologen
CO2 + reduced methyl viologen
-
-
-
-
?
formate + methyl viologen
CO2 + reduced methyl viologen
-
-
-
-
r
formate + methylene blue

CO2 + reduced methylene blue
-
119% of the activity with NAD+
-
-
?
formate + methylene blue
CO2 + reduced methylene blue
-
-
-
-
?
formate + NAD+

CO2 + NADH
Achromobacter parvulus
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
?
formate + NAD+
CO2 + NADH
Arabidopsis thaliana cv. Xanthi
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
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
-
-
-
-
?
formate + NAD+
CO2 + NADH
Candida methanolica
-
one of the key enzymes in the assimilation of C1 compounds, such as methanol
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
r
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
-
enzyme provides NADH for synthesis
-
-
?
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
-
-
-
-
r
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
r
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
ir
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
Kloeckera sp.
-
-
-
-
?
formate + NAD+
CO2 + NADH
Kloeckera sp.
-
last step of methanol oxidation system
-
-
?
formate + NAD+
CO2 + NADH
Kloeckera sp. 2201
-
-
-
-
?
formate + NAD+
CO2 + NADH
Kloeckera sp. 2201
-
last step of methanol oxidation system
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
FDH1 exhibits absolute specificity for formate and NAD+
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
formate + NAD+
CO2 + NADH
methylotrophic bacterium
-
-
-
-
?
formate + NAD+
CO2 + NADH
methylotrophic bacterium 1
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
ir
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
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
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
Pseudomonas methylica
-
-
-
-
?
formate + NAD+
CO2 + NADH
Pseudomonas methylica
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
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
-
-
-
r
formate + NAD+
CO2 + NADH
-
-
-
r
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
?
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
-
-
-
?
formate + NAD+
CO2 + NADH
Torulopsis candida
-
-
-
-
?
formate + NAD+
CO2 + NADH
Torulopsis candida NRRL Y-11419
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
287875, 287889, 288099, 288108, 288110, 288119, 656695, 700012, 725739, 740947, 742266 -
-
?
formate + NAD+
CO2 + NADH
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
ir
formate + NAD+
CO2 + NADH
-
-
-
-
r
formate + NAD+
CO2 + NADH
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
?
formate + NAD+
CO2 + NADH
high activity
-
-
?
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
-
-
-
-
?
formate + NAD+
CO2 + NADH
Q00498
-
-
-
?
formate + NAD+
CO2 + NADH
-
induced by methanol and formate
-
-
?
formate + NAD+

CO2 + NADH + H+
100% specificity
-
-
?
formate + NAD+
CO2 + NADH + H+
100% specificity
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
ir
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+

HCO3- + NADH
-
-
-
-
?
formate + NAD+
HCO3- + NADH
-
-
-
-
?
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
-
-
-
?
formate + NADP+
CO2 + NADPH
-
-
-
?
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
-
4% of the activity with NAD+
-
-
?
formate + NADP+
CO2 + NADPH
-
4% of the activity 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+
low activity
-
-
?
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
-
-
?
HCO3- + NADH

formate + NAD+
-
-
-
-
?
HCO3- + NADH
formate + NAD+
-
-
-
-
?
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
?
-
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
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
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+
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CO2 + NADH
formate + NAD+
formate + NAD+
CO2 + NADH
formate + NADP+
CO2 + NADPH
formate + NADP+
CO2 + NAPDH
-
NADP+ is a substrate for mutant enzymes only
-
-
?
additional information
?
-
CO2 + NADH

formate + NAD+
-
-
-
r
CO2 + NADH
formate + NAD+
-
-
-
r
CO2 + NADH
formate + NAD+
-
-
-
-
r
CO2 + NADH
formate + NAD+
-
-
-
-
r
CO2 + NADH
formate + NAD+
-
-
-
-
?
CO2 + NADH
formate + NAD+
-
-
-
-
?
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
CO2 + NADH
formate + NAD+
-
-
-
?
formate + NAD+

CO2 + NADH
-
-
-
?
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
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
enzyme provides NADH for synthesis
-
-
?
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
-
-
-
-
r
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
r
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
Kloeckera sp.
-
last step of methanol oxidation system
-
-
?
formate + NAD+
CO2 + NADH
Kloeckera sp. 2201
-
last step of methanol oxidation system
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
ir
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
Pseudomonas methylica
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
?
formate + NAD+
CO2 + NADH
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
role of formate dehydrogenase in detoxification of exogenous formate
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
?
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
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
ir
formate + NAD+
CO2 + NADH
-
-
-
-
r
formate + NAD+
CO2 + NADH
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
?
formate + NAD+
CO2 + NADH
-
last enzyme of the dissimilatory pathway of the methanol metabolism
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
?
formate + NAD+
CO2 + NADH
-
-
-
-
?
formate + NAD+
CO2 + NADH
Q00498
-
-
-
?
formate + NAD+
CO2 + NADH
-
induced by methanol and formate
-
-
?
formate + NADP+

CO2 + NADPH
-
-
-
?
formate + NADP+
CO2 + NADPH
-
-
-
?
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+
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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1-chloro-2-oxopropane
-
20 mM, pH 6.5, 30°C, 5 h, 76% loss of activity
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
4-hydroxybutyl acetate
-
IC50 of 15.6 vol%
5,5'-dithio-bis(2-nitrobenzoic acid)
-
-
5-Nitro-8-hydroxyquinoline
-
-
ADP-beta-D-ribose
-
competitive with NAD+, mixed-type with formate
benzaldehyde
Candida methanolica
-
slight inhibition
bicarbonate
-
mixed-type inhibition of NAD+ and formate
Ca2+
61.51% residual activity at 10 mM
CO32-
16.93% residual activity at 100 mM
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
EDTA
-
50 mM, slight inhibition
ethanol
-
IC50 of 4.8 vol%
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
Fe3+
83.5% inhibition at 1 mM
H2PO4-
78.54% residual activity at 100 mM
iodoacetate
-
strong inhibition
Isonicotinyl hydrazide
-
weak
Isopropanol
-
IC50 of 4.7 vol%
KF
-
1 mM, 80% inhibition
Mg2+
89.93% residual activity at 10 mM
n-butanol
-
IC50 of 1.4 vol%
n-Propanol
-
IC50 of 2.5 vol%
NADP+
-
strong inhibition
nitrate
-
competitive inhibitor
o-nitrobenzaldehyde
Candida methanolica
-
slight inhibition
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
p-chloromercuribenzoate
-
strong inhibition
p-chloromercuriphenylsulfonic acid
-
-
phenol
-
IC50 of 0.32 vol%
phenylmercuric acetate
-
-
PO43-
30.9% residual activity at 100 mM
pyridoxal 5'-phosphate
Candida methanolica
-
slight inhibition
Sodium azide
94% inhibition at 1 mM; 99% inhibition at 1 mM
sodium hypophosphite
-
1 mM, 80% inhibition
1,10-phenanthroline

-
-
ADP

86% inhibition at 50 mM; 90% inhibition at 50 mM
ADP
-
inhibition is greater at acidic pH than at neutral pH
AgNO3

-
0.01 mM
AgNO3
-
1 mM; 80% inhibition
ATP

45% inhibition at 50 mM; 56% inhibition at 50 mM
ATP
-
inhibition is greater at acidic pH than at neutral pH
azide

-
-
azide
-
uncompetitive with NAD+, competitive with formate
azide
-
0.9 mM, 50% inhibition
azide
-
a transition-state analogue inhibitor of FDH
azide
nanomolar inhibitor
Cd2+

complete inhibition at 1 mM
Cd2+
Candida methanolica
-
CdCl2
Cd2+
-
1 mM CdSO4, 39% inhibition
CN-

Candida methanolica
-
NaCN
CN-
-
1 mM KCN, complete inhibition
CN-
-
0.1 mM NaCN, 90% inhibition
CN-
-
1 mM KCN, 50% inhibition
CN-
methylotrophic bacterium
-
-
Cu2+

1 mM, 37% inhibition
Cu2+
94.2% inhibition at 1 mM
Cu2+
82 inhibition at 1 mM; complete inhibition at 1 mM
Cu2+
1 mM Cu2+ inhibits the enzyme activity by 79%
Cu2+
-
1 mM CuCl2, 81% inhibition
Cu2+
-
0.2 mM, 13.6% inhibition
Cu2+
the wild type enzyme is completely inactivated by 5 mM Cu2+
Dithionitrobenzoate

-
-
Dithionitrobenzoate
methylotrophic bacterium
-
-
HCO3-

-
-
Hg2+

1 mM, complete inhibition
Hg2+
Candida methanolica
-
-
Hg2+
98% inhibition at 1 mM; 98% inhibition at 1 mM
Hg2+
-
1 mM, complete inhibition
iodoacetamide

Candida methanolica
-
-
iodoacetamide
methylotrophic bacterium
-
-
methanol

-
-
methanol
-
IC50 of 10.2 vol%
N3-

Candida methanolica
-
-
N3-
-
0.25 mM. Inhibition is partly overcome by addition of formate or NAD+
N3-
-
1 mM NaN3, 90% inhibition
N3-
-
0.25 mM. Inhibition is partly overcome by addition of formate or NAD+
N3-
methylotrophic bacterium
-
-
NADH

-
inhibition is partly overcome by addition of formate or NAD+
NADH
-
competitive with NADH, mixed-type with formate
NADH
66% inhibition at 0.12 mM; 73% inhibition at 0.12 mM
NADH
Pseudomonas methylica
-
competitive versus NAD+; noncompetitive versus formate
NADH
-
competitive versus NAD+
NADPH

-
competitive
NADPH
-
strong inhibition
NADPH
26% inhibition at 0.24 mM; 58% inhibition at 0.24 mM
NaN3

1 mM, complete inhibition
NaN3
-
1 mM, 80% inhibition
NaN3
-
1 mM, complete inhibition
NEM

1 mM, 25.3% inhibition
Ni2+

12.4% inhibition at 1 mM
Ni2+
Candida methanolica
-
NiCl2
Ni2+
1 mM Ni2+ inhibits the enzyme activity by 28%
NO2-

-
1 mM, 5% inhibition
NO3-

-
10 mM KNO3, 38% inhibition
NO3-
-
0.25 mM. Inhibition is partly overcome by addition of formate or NAD+
NO3-
-
1 mM, 13% inhibition
NO3-
40.89% residual activity at 100 mM
OCN-

-
-
p-hydroxymercuribenzoate

-
0.25 mM
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
Pb2+

Kloeckera sp.
-
-
Pb2+
24.33% residual activity at 10 mM
PCMB

0.2 mM, complete inhibition
PCMB
Candida methanolica
-
-
PCMB
methylotrophic bacterium
-
-
PCMB
-
0.2 mM, 10.7% inhibition
SCN-

-
-
Zn2+

55.5% inhibition at 1 mM
Zn2+
-
1 mM 63% inhibition
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.037 - 0.2
2,6-dichlorophenolindophenol
1.16
3-acetylpyridine-NAD+
-
-
0.19
3-pyridinecarboxaldehyde-NAD+
-
-
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
0.45 - 1.1
S-formylglutathione
additional information
additional information
-
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
0.1
benzyl viologen

-
-
0.24
benzyl viologen
-
formate dehydrogenase II, reaction with formate
0.25
benzyl viologen
-
formate dehydrogenase I, reaction with formate
2
benzyl viologen
-
formate dehydrogenase II, reaction with NADH
0.0157
CO2

-
at pH 7.0 and 22°C
0.4
CO2
at pH 6.0 and 35°C
0.43
CO2
25°C, pH not specified in the publication
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
7.7
CO2
wild type enzyme, pH and temperature not specified in the publication
8
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
0.0033
formate

-
pH 7.5, 30°C, heated DE-52-fraction
0.011
formate
-
pH 7.5, 30°C, enzyme expressed in tobacco
0.011
formate
-
pH 7.5, 30°C, enzyme from Sephadex G-15 desalted fraction
0.011
formate
-
pH 7.5, 30°C, mitochondrial enzyme
0.012
formate
-
pH 7.5, 30°C, enzyme from DE-52 chromatography
0.037
formate
mutant enzyme N187S/T321S, at pH 7.2 and 30°C
0.0571
formate
-
at pH 8.0 and 22°C
0.075
formate
wild type enzyme, at pH 7.2 and 30°C
0.08
formate
mutant enzyme N187S, at pH 7.2 and 30°C
0.084
formate
mutant enzyme T321S, at pH 7.2 and 30°C
0.13
formate
-
formate dehydrogenase II, reaction with NAD+
0.135
formate
-
formate dehydrogenase I, reaction with NAD+
0.17
formate
-
pH 7.0, 37°C, mutant enzyme R284Q
0.19
formate
-
wild type enzyme, at pH 9.0 and 25°C
0.26
formate
-
reduction of NAD+
0.277
formate
-
with 2,6-dichlorophenolindophenol as cosubstrate, at pH 9.0 and 30°C
0.278
formate
-
with ferricyanide as cosubstrate, at pH 9.0 and 30°C
0.281
formate
-
with NAD+ as cosubstrate, at pH 9.0 and 30°C
0.44
formate
-
at pH 7.0 and 30°C
0.472
formate
-
at pH 7.5, 25°C
0.62
formate
-
in presence of NAD+
0.82
formate
at pH 6.5 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, at pH 8.0 and 37°C
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
1.6
formate
-
pH 7.0, 30°C
1.67
formate
-
pH 7.0, 30°C
1.67
formate
-
and 6.25 mM at the second catalytic site
1.7
formate
-
with NAD+ as electron acceptor
2 - 3
formate
-
mutant enzyme D221A, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
2.1
formate
-
mutant enzyme A267M, at pH 8.0 and 37°C
2.2
formate
at pH 7.5 and 25°C
2.2
formate
-
mutant enzyme A267M/I272V/F290N, at pH 8.0 and 37°C
2.3
formate
Q00498
mutant enzyme Y160E, at pH 8.0 and 25°C
2.3
formate
-
mutant enzyme A267M/I272V/F290S, at pH 8.0 and 37°C
2.4
formate
pH 7.0, 30°C
2.4
formate
-
mutant enzyme A267M/I272V, at pH 8.0 and 37°C
2.5
formate
-
pH 6.5, 30°C
2.5
formate
mutant enzyme V120S/N187D, at pH 9.5 and 30°C
2.7
formate
Q00498
mutant enzyme Y160R, at pH 8.0 and 25°C
2.8
formate
-
mutant enzyme A267M/I272V/F290D, at pH 8.0 and 37°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
formate
Candida methanolica
-
-
3.1
formate
-
20°C, pH 8, mutant enzyme T69V
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
3.3
formate
-
at pH 7.0 and 25°C
3.6
formate
-
mutant enzyme H387M, at pH 9.0 and 25°C
3.6
formate
wild type enzyme, at pH 9.5 and 30°C
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
3.9
formate
Q00498
mutant enzyme N187E, at pH 8.0 and 25°C
4
formate
-
mutant enzyme Q313E
4
formate
recombinant enzyme, at pH 7.5 and 25°C
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, at pH 8.0 and 37°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
4.4
formate
-
in 100 mM potassium phosphate buffer at pH 7.5, at 30°C
4.4
formate
Q00498
mutant enzyme N147R, at pH 8.0 and 25°C
4.4
formate
Q00498
mutant enzyme Y302R, at pH 8.0 and 25°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, at pH 8.0 and 37°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
4.75
formate
-
wild type enzyme, at pH 8.0 and 25°C
4.75
formate
Q00498
wild type enzyme, at pH 8.0 and 25°C
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, at pH 8.0 and 37°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
formate
mutant enzyme K328V, at pH 7.5 and 25°C
5.1
formate
Q00498
mutant enzyme Q105R, at pH 8.0 and 25°C
5.2
formate
at pH 7.4 and 25°C
5.2
formate
mutant enzyme I239C, at 30°C and pH 7.0
5.3
formate
Q00498
mutant enzyme H13E, at pH 8.0 and 25°C
5.5
formate
pH 7.0, 30°C, wild-type enzyme
5.5
formate
Q00498
mutant enzyme N187E/Q105R, at pH 8.0 and 25°C
5.6
formate
-
20°C, pH 8, wild-type enzyme
5.6
formate
-
pH 7.0, 30°C, recombinant enzyme
5.6
formate
-
wild-type, 30°C, pH 7.0
5.63
formate
-
wild type enzyme, at 20°C, in 20 mM triethanolamine at pH 8
5.8
formate
-
20°C, pH 8, mutant enzyme T226V
5.8
formate
mutant enzyme A10C/I239C, at 30°C and pH 7.0
5.9
formate
Q00498
mutant enzyme N187E/N147R, at pH 8.0 and 25°C
6
formate
-
oxidized mutant enzyme T169C/T226C, at 20°C, in 20 mM triethanolamine at pH 8
6.1
formate
in 0.1 M potassium phosphate buffer, pH 7.5, at 30°C
6.25
formate
-
and 1.67 mM at the second catalytic site
6.7
formate
mutant enzyme N187D, at pH 9.5 and 30°C
7
formate
-
wild-type enzyme
7.01
formate
-
at pH 7.0 and 25°C
7.2
formate
25°C, pH not specified in the publication
7.2
formate
at pH 10.5 and 35°C
7.3
formate
wild type enzyme, at 30°C and pH 7.0
7.5
formate
-
wild-type enzyme and mutant enzyme C255S
7.6
formate
-
with thio-NAD+ as electron acceptor
7.7
formate
in 0.1 M potassium phosphate buffer pH 7.0, at 30°C
7.9
formate
mutant enzyme V120S, at pH 9.5 and 30°C
8.2
formate
mutant enzyme A10C, at 30°C and pH 7.0
9.3
formate
-
20°C, pH 8, mutant enzyme T69V/T226V
10.8
formate
-
reduced mutant enzyme T169C/T226C, at 20°C, in 20 mM triethanolamine at pH 8
15
formate
methylotrophic bacterium
-
-
15
formate
-
pH 7.0, 37°C, wild-type enzyme
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 C255M
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
formate
Kloeckera sp.
-
-
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
25
formate
-
mutant E141N, 30°C, pH 7.0
27.5
formate
-
mutant enzyme H387K, at pH 9.0 and 25°C
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
31
formate
-
mutant E141Q, 30°C, pH 7.0
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
145
formate
-
pH 7.0, 37°C, mutant enzyme R284Q
335
formate
-
with 3-acetylpyridine-NAD+ as electron acceptor
362
formate
-
mutant enzyme R587K, at pH 9.0 and 25°C
1000
formate
pH 7.0, 30°C, mutant enzyme D196A/Y197R, reaction with NADP+
2.6
glyoxylate

-
mutant E141Q, 30°C, pH 7.0
4.6
glyoxylate
-
mutant E141N, 30°C, pH 7.0
7.5
glyoxylate
-
wild-type, 30°C, pH 7.0
0.32
HCO3-

-
at pH 7.0 and 25°C
0.78
HCO3-
-
at pH 7.0 and 25°C
0.0057
NAD+

-
-
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