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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 + H+
formate + NAD+ + OH-
HCO3- + NADH + H+
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 + H+
Achromobacter parvulus
-
-
-
-
?
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+
Arabidopsis thaliana cv. Xanthi
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
the enzyme shows strict substrate specificity for formate
-
-
?
formate + NAD+
CO2 + NADH + H+
the enzyme shows strict substrate specificity for formate
-
-
?
formate + NAD+
CO2 + NADH + H+
Candida methanolica
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
Candida methanolica
-
one of the key enzymes in the assimilation of C1 compounds, such as methanol
-
-
?
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+
-
-
-
-
r
formate + NAD+
CO2 + NADH + H+
-
equilibrium strongly favors dehydrogenation of formate
-
-
r
formate + NAD+
CO2 + NADH + H+
-
enzyme catalyzes formate oxidation about 30times faster than the CO2 reduction
-
-
r
formate + NAD+
CO2 + NADH + H+
-
enzyme provides NADH for synthesis
-
-
?
formate + NAD+
CO2 + NADH + H+
-
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 + H+
-
equilibrium strongly favors dehydrogenation of formate
-
-
r
formate + NAD+
CO2 + NADH + H+
-
-
-
-
r
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
r
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
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+
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH + H+
Kloeckera sp.
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
Kloeckera sp.
-
last step of methanol oxidation system
-
-
?
formate + NAD+
CO2 + NADH + H+
Kloeckera sp. 2201
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
Kloeckera sp. 2201
-
last step of methanol oxidation system
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
FDH1 exhibits absolute specificity for formate and NAD+
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
induced by methanol and formate
-
-
?
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+
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 + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
?
formate + NAD+
CO2 + NADH + H+
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 + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
methylotrophic bacterium
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
methylotrophic bacterium 1
-
-
-
-
?
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+
-
-
-
ir
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
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 + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
Pseudomonas methylica
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
Pseudomonas methylica
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
ir
formate + NAD+
CO2 + NADH + H+
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
role of formate dehydrogenase in detoxification of exogenous formate
-
-
?
formate + NAD+
CO2 + NADH + H+
wild-type enzyme shows no activity with NADP+, mutant enzyme D196A/Y197R shows higher activity with NADP+ than with NAD+
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
Thermochaetoides thermophila
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
Thermochaetoides thermophila
-
-
-
?
formate + NAD+
CO2 + NADH + H+
Thermochaetoides thermophila DSM 1495
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
r
formate + NAD+
CO2 + NADH + H+
-
-
-
r
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
the enzyme exhibits a dramatic preference for the CO2 reduction reaction over the oxidation reaction of formate
-
-
r
formate + NAD+
CO2 + NADH + H+
-
the enzyme exhibits a dramatic preference for the CO2 reduction reaction over the oxidation reaction of formate
-
-
r
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
?
formate + NAD+
CO2 + NADH + H+
Torulopsis candida
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
Torulopsis candida NRRL Y-11419
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
287875, 287889, 288099, 288108, 288110, 288119, 656695, 686449, 687304, 699307, 700012, 711548, 711549, 713421, 725739, 740947, 742266 -
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
ir
formate + NAD+
CO2 + NADH + H+
-
-
-
-
r
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+
CO2 + NADH + H+
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
?
formate + NAD+
CO2 + NADH + H+
high activity
-
-
?
formate + NAD+
CO2 + NADH + H+
-
last enzyme of the dissimilatory pathway of the methanol metabolism
-
-
?
formate + NAD+
CO2 + NADH + H+
FDH is highly specific to NAD+ and virtually fails to catalyze the reaction with NADP+
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
Q00498
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
induced by methanol and formate
-
-
?
formate + NAD+ + OH-
HCO3- + NADH + H+
Thermochaetoides thermophila
-
-
-
-
?
formate + NAD+ + OH-
HCO3- + 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
-
-
-
?
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+
-
-
-
-
?
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+
Thermochaetoides thermophila
-
-
-
-
?
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
?
-
-
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
?
-
Thermochaetoides thermophila
no activity with NADP+
-
-
?
additional information
?
-
Thermochaetoides thermophila DSM 1495
no activity with NADP+
-
-
?
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+
-
-
?
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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
-
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
Thermochaetoides thermophila
-
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
Thermochaetoides thermophila
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
formate
-
with NAD+ as cosubstrate, at pH 7.0 and 25°C
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
100
formate
-
with NADP+ as cosubstrate, at pH 7.0 and 25°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-
Thermochaetoides thermophila
-
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
0.0137
NAD+
-
mutant enzyme F290E, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
0.014
NAD+
-
mutant enzyme F290N, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
0.0143
NAD+
-
mutant enzyme F290T, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
0.015
NAD+
wild type enzyme, in 0.1 M potassium phosphate buffer (pH 7.5)
0.015
NAD+
wild type enzyme, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
0.021
NAD+
at pH 7.5 and 25°C
0.025
NAD+
mutant enzyme K328V, at pH 7.5 and 25°C
0.0259
NAD+
in 0.1 M potassium phosphate buffer, pH 7.5, at 30°C
0.026
NAD+
pH 7.5, 30°C, fusion enzyme F-S3-L
0.028
NAD+
-
pH 6.5, 30°C
0.0303
NAD+
recombinant enzyme, at pH 7.5 and 25°C
0.035
NAD+
-
pH 7.5, 30°C, heated DE-52-fraction
0.035
NAD+
mutant enzyme A198G, pH and temperature not specified in the publication
0.0365
NAD+
pH 7.0, 30°C, wild-type enzyme
0.037
NAD+
pH 7.5, 30°C, fusion enzyme F-R1-L
0.03839
NAD+
-
at pH 7.5, 25°C
0.039
NAD+
pH 7.5, 30°C, fusion enzyme F-DL-L
0.041
NAD+
-
wild type enzyme, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
0.043
NAD+
-
wild type enzyme, in the absence of 1-methyl-3-methylimidazolium dimethylphosphate, in 50 mM carbonate buffer, pH 9.7, at 30°C
0.045
NAD+
mutant enzyme A198G, pH and temperature not specified in the publication
0.045
NAD+
pH 7.5, 30°C, fusion enzyme F-R3-L
0.048
NAD+
-
pH 7.0, 30°C
0.051
NAD+
pH 7.5, 30°C, fusion enzyme F-R2-L
0.052
NAD+
pH 7.5, 30°C, fusion enzyme F-S2-L
0.0536
NAD+
wild type enzyme, at 30°C and pH 7.0
0.054
NAD+
-
pH 7.0, 30°C, recombinant enzyme
0.055
NAD+
-
mutant enzyme F311Y, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
0.06
NAD+
-
at pH 7.0 and 25°C
0.06
NAD+
wild type enzyme, pH and temperature not specified in the publication
0.066
NAD+
pH 7.5, 30°C, fusion enzyme F-S1-L
0.07
NAD+
-
wild-type enzyme and mutant enzyme Q313E
0.0742
NAD+
mutant enzyme A10C, at 30°C and pH 7.0
0.075
NAD+
-
pH 7.5, 30°C, enzyme from DE-52 chromatography
0.075
NAD+
-
pH 7.5, 30°C, enzyme from Sephadex G-15 desalted fraction
0.076
NAD+
-
pH 7.5, 30°C, mitochondrial enzyme
0.078
NAD+
-
pH 7.5, 30°C, enzyme expressed in tobacco
0.08
NAD+
in 0.1 M potassium phosphate buffer pH 7.0, at 30°C
0.08
NAD+
wild type enzyme, pH and temperature not specified in the publication
0.083
NAD+
at pH 6.5 and 30°C
0.091
NAD+
in 100 mM Tris-HCl (pH 7.0), at 30°C
0.1
NAD+
Kloeckera sp.
-
-
0.1
NAD+
-
wild-type enzyme
0.105
NAD+
-
formate dehydrogenase I, reaction with formate
0.11
NAD+
methylotrophic bacterium
-
-
0.11
NAD+
Candida methanolica
-
-
0.11
NAD+
-
formate dehydrogenase II, reaction with formate
0.11
NAD+
-
pH 7.0, 37°C, wild-type enzyme
0.1191
NAD+
mutant enzyme A10C/I239C, at 30°C and pH 7.0
0.13
NAD+
mutant enzyme D195Q/Y196P, in 0.1 M potassium phosphate buffer (pH 7.5)
0.13
NAD+
mutant enzyme D195Q/Y196P, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
0.13
NAD+
-
mutant enzyme D195S/Y196A, at pH 8.0 and 25°C
0.1322
NAD+
mutant enzyme I239C, at 30°C and pH 7.0
0.16
NAD+
-
in presence of formate
0.168
NAD+
-
mutant enzyme F311N, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
0.17
NAD+
-
mutant enzyme F311S, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
0.173
NAD+
-
at pH 9.0 and 30°C
0.177
NAD+
-
wild type enzyme, in the presence of 30% (v/v) 1-methyl-3-methylimidazolium dimethylphosphate, in 50 mM carbonate buffer, pH 9.7, at 30°C
0.22
NAD+
-
mutant enzyme D195S/Q197T, at pH 8.0 and 25°C
0.23
NAD+
-
mutant enzyme F311D, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
0.3
NAD+
-
mutant enzyme C255S
0.54
NAD+
mutant enzyme A198G/D221S, pH and temperature not specified in the publication
0.6
NAD+
-
mutant enzyme C255M
0.62
NAD+
-
wild type enzyme, at pH 8.0 and 25°C
0.623
NAD+
pH 7.5, 30°C, wild-type enzyme
0.62322
NAD+
at pH 7.5 and 30°C
0.7
NAD+
-
mutant enzyme D195S/Y196L, at pH 8.0 and 25°C
0.71
NAD+
mutant enzyme D221S, pH and temperature not specified in the publication
0.96
NAD+
mutant enzyme D195Q, in 0.1 M potassium phosphate buffer (pH 7.5)
0.96
NAD+
mutant enzyme D195Q, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
1.09
NAD+
-
mutant enzyme C145S/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 30°C
1.1
NAD+
-
mutant enzyme D195S, at pH 8.0 and 25°C
1.2
NAD+
25°C, pH not specified in the publication
1.2
NAD+
at pH 10.5 and 35°C
1.5
NAD+
mutant enzyme D195S, in 0.1 M potassium phosphate buffer (pH 7.5)
1.5
NAD+
mutant enzyme D195S, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
1.79
NAD+
Thermochaetoides thermophila
at pH 7.4 and 25°C
1.8
NAD+
mutant enzyme D195Q/Y196H, in 0.1 M potassium phosphate buffer (pH 7.5)
1.8
NAD+
mutant enzyme D195Q/Y196H, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
2.02
NAD+
mutant enzyme V120S/N187D, at pH 9.5 and 30°C
2.3
NAD+
-
mutant enzyme D195S/Y196S, at pH 8.0 and 25°C
3.3
NAD+
-
mutant enzyme Q197V, at pH 8.0 and 25°C
3.4
NAD+
wild type enzyme, at pH 9.5 and 30°C
3.8
NAD+
mutant enzyme N187D, at pH 9.5 and 30°C
3.9
NAD+
-
mutant enzyme D195S/Q197V, at pH 8.0 and 25°C
4.1
NAD+
-
mutant enzyme C145S/A198G/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 30°C
4.7
NAD+
-
mutant enzyme D195S
4.7
NAD+
-
pH 8.0, 20°C, mutant enzyme D195S
4.8
NAD+
mutant enzyme D195A, in 0.1 M potassium phosphate buffer (pH 7.5)
4.8
NAD+
mutant enzyme D195A, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
5.01
NAD+
mutant enzyme D195N, in 0.1 M potassium phosphate buffer (pH 7.5)
5.01
NAD+
mutant enzyme D195N, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
5.1
NAD+
mutant enzyme D195Q/Y196S, in 0.1 M potassium phosphate buffer (pH 7.5)
5.1
NAD+
mutant enzyme D195Q/Y196S, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
5.5
NAD+
-
wild-type enzyme
5.5
NAD+
-
pH 8.0, 20°C, wild-type enzyme
7.6
NAD+
pH 7.0, 30°C, mutant enzyme D196A/Y197R, with 0.25 M formate
8.4
NAD+
pH 7.0, 30°C, mutant enzyme D196A/Y197R, with 0.5 M formate
8.8
NAD+
mutant enzyme V120S, at pH 9.5 and 30°C
9.1
NAD+
-
mutant enzyme F290S, in 0.1 M sodium phosphate buffer, pH 7.0, at 30°C
9.1
NAD+
-
mutant enzyme F290S, at pH 8.0 and 37°C
9.9
NAD+
-
mutant enzyme A267M, at pH 8.0 and 37°C
12.8
NAD+
-
mutant enzyme F290D, in 0.1 M sodium phosphate buffer, pH 7.0, at 30°C
12.8
NAD+
-
mutant enzyme F290D, at pH 8.0 and 37°C
13.3
NAD+
-
wild type enzyme, at pH 8.0 and 37°C
13.3
NAD+
-
wild type enzyme, in 0.1 M sodium phosphate buffer, pH 7.0, at 30°C
13.3
NAD+
-
mutant enzyme A267M/I272V, at pH 8.0 and 37°C
14
NAD+
-
mutant enzyme F290N, in 0.1 M sodium phosphate buffer, pH 7.0, at 30°C
14
NAD+
-
mutant enzyme F290N, at pH 8.0 and 37°C
14.1
NAD+
-
mutant enzyme A267M/I272V/F290N, at pH 8.0 and 37°C
16.1
NAD+
-
mutant enzyme A267M/I272V/F290S, at pH 8.0 and 37°C
20.3
NAD+
-
mutant enzyme A267M/I272V/F290D, at pH 8.0 and 37°C
25
NAD+
mutant enzyme K328V, at 20°C, after 2 weeks of enzyme storage
25
NAD+
mutant enzyme K47E, at 20°C, after 2 weeks of enzyme storage
30
NAD+
mutant enzyme K328V, at 20°C, after 4 months of enzyme storage
40
NAD+
mutant enzyme K47E, at 20°C, after 4 months of enzyme storage
50
NAD+
native wild type enzyme, at 20°C, after 2 weeks of enzyme storage
90
NAD+
native wild type enzyme, at 20°C, after 4 months of enzyme storage
0.003
NADH
at pH 6.0 and 35°C
0.05
NADH
in 0.1 M sodium phosphate (pH 6.8), at 37°C
0.18
NADH
25°C, pH not specified in the publication
0.037
NADP+
-
mutant enzyme D221A, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
0.04
NADP+
-
Km above 0.04 mM, wild type enzyme, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
0.084
NADP+
-
mutant enzyme C145S/A198G/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
0.13
NADP+
pH 7.0, 30°C, mutant enzyme D196A/Y197R, with 0.25 M formate
0.147
NADP+
-
mutant enzyme C145S/A198G/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 30°C
0.16
NADP+
pH 7.0, 30°C, mutant enzyme D196A/Y197R, with 0.5 M formate
0.19
NADP+
mutant enzyme D221S, pH and temperature not specified in the publication
0.24
NADP+
-
mutant enzyme D221G/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
0.27
NADP+
-
mutant enzyme A198G/D221Q, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
0.31
NADP+
-
mutant enzyme D221G, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
0.39
NADP+
-
mutant enzyme D221Q, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
0.43
NADP+
-
mutant enzyme D221S, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
0.57
NADP+
-
mutant enzyme C145S/D221G/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
0.59
NADP+
-
mutant enzyme C145S/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
0.74
NADP+
-
mutant enzyme C145S/D221A/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
0.92
NADP+
-
mutant enzyme C145S/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 30°C
1.4
NADP+
-
mutant enzyme Q197V, at pH 8.0 and 25°C
1.7
NADP+
mutant enzyme D195Q/Y196H, in 0.1 M potassium phosphate buffer (pH 7.5)
1.7
NADP+
mutant enzyme D195Q/Y196H, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
2
NADP+
-
mutant enzyme D195S/Y196L, at pH 8.0 and 25°C
2.2
NADP+
-
mutant enzyme D195S/Q197V, at pH 8.0 and 25°C
3.3
NADP+
mutant enzyme D195A, in 0.1 M potassium phosphate buffer (pH 7.5)
3.3
NADP+
mutant enzyme D195A, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
3.5
NADP+
in 100 mM Tris-HCl (pH 7.0), at 30°C
3.7
NADP+
mutant enzyme D195Q/Y196P, in 0.1 M potassium phosphate buffer (pH 7.5)
3.7
NADP+
mutant enzyme D195Q/Y196P, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
4.5
NADP+
mutant enzyme D195Q, in 0.1 M potassium phosphate buffer (pH 7.5)
4.5
NADP+
mutant enzyme D195Q, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
4.6
NADP+
-
mutant enzyme D195S/Q197T, at pH 8.0 and 25°C
5
NADP+
-
mutant enzyme D195S, at pH 8.0 and 25°C
6.2
NADP+
mutant enzyme D195Q/Y196S, in 0.1 M potassium phosphate buffer (pH 7.5)
6.2
NADP+
mutant enzyme D195S, in 0.1 M potassium phosphate buffer (pH 7.5)
6.2
NADP+
mutant enzyme D195Q/Y196S, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
6.2
NADP+
mutant enzyme D195S, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
8.2
NADP+
-
mutant enzyme D195S/Y196S, at pH 8.0 and 25°C
8.5
NADP+
-
mutant enzyme D195S/Y196A, at pH 8.0 and 25°C
13.2
NADP+
mutant enzyme D195N, in 0.1 M potassium phosphate buffer (pH 7.5)
13.2
NADP+
mutant enzyme D195N, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
29.5
NADP+
in 0.1 M potassium phosphate buffer, pH 7.5, at 30°C
37
NADP+
-
at pH 7.0 and 25°C
38
NADP+
Km above 38 mM, wild type enzyme, in 0.1 M potassium phosphate buffer (pH 7.5)
38
NADP+
Km above 38 mM, wild type enzyme, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
0.45
S-formylglutathione
-
-
1.1
S-formylglutathione
-
-
additional information
additional information
-
-
-
additional information
additional information
-
the enzyme has two sites with about equal catalytic activity. The Km-values for formate are different for the two catalytic sites: 1.67 mM and 6.25 mM
-
additional information
additional information
-
effect of organic solvents of formate dehydrogenase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.072
reduced 1,1'-diaminoethyl-4,4'-bipyridinium salt
at pH 7.4, temperature not specified in the publication
0.005
reduced 1,1'-dicarboxyl-4,4'-bipyridinium salt
at pH 7.4, temperature not specified in the publication
0.038
reduced 1-methyl-1'-aminoethyl-4,4'-bipyridinium salt
at pH 7.4, temperature not specified in the publication
0.025
reduced 1-methyl-1'-carboxymethyl-4,4'-bipyridinium salt
at pH 7.4, temperature not specified in the publication
0.032
reduced methyl viologen
at pH 7.4, temperature not specified in the publication
additional information
additional information
-
0.1
CO2
25°C, pH not specified in the publication
0.1
CO2
at pH 6.0 and 35°C
1.5
CO2
-
with NADH as cosubstrate, at pH 9.0 and 30°C
46.6
CO2
-
at pH 7.0 and 22°C
0.01
formate
-
mutant E141N, 30°C, pH 7.0
0.054
formate
-
mutant E141Q, 30°C, pH 7.0
0.21
formate
wild type enzyme, at pH 7.2 and 30°C
0.25
formate
Q00498
mutant enzyme Y302R, at pH 8.0 and 25°C
0.29
formate
-
oxidized mutant enzyme T169C/T226C, at 20°C, in 20 mM triethanolamine at pH 8
0.3
formate
-
20°C, pH 8, mutant enzyme T69V
0.3
formate
-
20°C, pH 8, mutant enzyme T69V/T226V
0.3
formate
Q00498
mutant enzyme Y160R, at pH 8.0 and 25°C
0.3
formate
at pH 10.5 and 35°C
0.31
formate
-
pH 7.0, 37°C, mutant enzyme R284Q
0.32
formate
25°C, pH not specified in the publication
0.4
formate
-
with NADP+ as cosubstrate, at pH 7.0 and 25°C
0.44
formate
mutant enzyme T321S, at pH 7.2 and 30°C
0.5
formate
-
reduced mutant enzyme T169C/T226C, at 20°C, in 20 mM triethanolamine at pH 8
0.5
formate
Q00498
mutant enzyme N187E/N147R, at pH 8.0 and 25°C
0.55
formate
Q00498
mutant enzyme H13E, at pH 8.0 and 25°C
0.6
formate
Q00498
mutant enzyme N187E/Q105R, at pH 8.0 and 25°C
0.7
formate
Q00498
mutant enzyme N187E, at pH 8.0 and 25°C
0.7
formate
mutant enzyme V120S/N187D, at pH 9.5 and 30°C
0.71
formate
mutant enzyme N187S/T321S, at pH 7.2 and 30°C
0.8
formate
Q00498
mutant enzyme Y160E, at pH 8.0 and 25°C
0.81
formate
Thermochaetoides thermophila
at pH 7.4 and 25°C
0.85
formate
Q00498
mutant enzyme N147R, at pH 8.0 and 25°C
0.9
formate
-
mutant enzyme H387K, at pH 9.0 and 25°C
1.1
formate
-
20°C, pH 8, mutant enzyme T226V
1.1
formate
-
wild type enzyme, at pH 8.0 and 25°C
1.13
formate
Q00498
wild type enzyme, at pH 8.0 and 25°C
1.2
formate
-
20°C, pH 8, wild-type enzyme
1.2
formate
-
wild type enzyme, at 20°C, in 20 mM triethanolamine at pH 8
1.2
formate
Q00498
mutant enzyme Q105R, at pH 8.0 and 25°C
1.25
formate
mutant enzyme N187S, at pH 7.2 and 30°C
1.3
formate
in 0.1 M potassium phosphate buffer, pH 7.5, at 30°C
1.31
formate
-
at pH 7.0 and 25°C
1.53
formate
wild type enzyme, at pH 9.5 and 30°C
1.77
formate
-
at pH 7.0 and 25°C
1.78
formate
at pH 7.5 and 25°C
2.039
formate
Thermochaetoides thermophila
-
at pH 7.0 and 25°C
2.2
formate
-
mutant enzyme A267M/I272V, at pH 8.0 and 37°C
2.32
formate
at pH 6.5 and 30°C
2.8
formate
-
mutant enzyme F290N, in 0.1 M sodium phosphate buffer, pH 7.0, at 30°C
2.8
formate
-
mutant enzyme F290N, at pH 8.0 and 37°C
2.9
formate
-
wild type enzyme, at pH 8.0 and 37°C
2.9
formate
-
wild type enzyme, in 0.1 M sodium phosphate buffer, pH 7.0, at 30°C
2.9
formate
-
mutant enzyme A267M/I272V/F290D, at pH 8.0 and 37°C
3.2
formate
-
mutant enzyme A267M/I272V/F290N, at pH 8.0 and 37°C
3.29
formate
mutant enzyme N187D, at pH 9.5 and 30°C
3.7
formate
-
mutant enzyme A267M/I272V/F290S, at pH 8.0 and 37°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
5
formate
-
mutant enzyme A267M, at pH 8.0 and 37°C
5.1
formate
-
mutant enzyme F290D, in 0.1 M sodium phosphate buffer, pH 7.0, at 30°C
5.1
formate
-
mutant enzyme F290D, at pH 8.0 and 37°C
5.34
formate
mutant enzyme V120S, at pH 9.5 and 30°C
5.6
formate
recombinant enzyme, at pH 7.5 and 25°C
6.1
formate
-
wild-type, 30°C, pH 7.0
6.8
formate
mutant enzyme K328V, at pH 7.5 and 25°C
7.3
formate
in 0.1 M potassium phosphate buffer pH 7.0, at 30°C
10
formate
-
pH 7.0, 37°C, wild-type enzyme
11.2
formate
-
mutant enzyme R587K, at pH 9.0 and 25°C
31
formate
-
with NAD+ as cosubstrate, at pH 7.0 and 25°C
32
formate
-
with 2,6-dichlorophenolindophenol as cosubstrate, at pH 9.0 and 30°C
33.7
formate
-
mutant enzyme H387M, at pH 9.0 and 25°C
35.4
formate
-
wild type enzyme, at pH 9.0 and 25°C
36.5
formate
-
with NAD+ as cosubstrate, at pH 9.0 and 30°C
39.7
formate
-
with ferricyanide as cosubstrate, at pH 9.0 and 30°C
76
formate
-
at pH 7.0 and 30°C
543
formate
-
at pH 8.0 and 22°C
0.007
glyoxylate
-
wild-type, 30°C, pH 7.0
0.023
glyoxylate
-
mutant E141Q, 30°C, pH 7.0
0.36
glyoxylate
-
mutant E141N, 30°C, pH 7.0
0.008
HCO3-
-
at pH 7.0 and 25°C
0.023
HCO3-
Thermochaetoides thermophila
-
at pH 7.0 and 25°C
0.095
NAD+
pH 7.0, 30°C, mutant enzyme D196A/Y197R
0.12
NAD+
pH 7.0, 30°C, mutant enzyme D196A/Y197R, with 0.5 M formate
0.16
NAD+
-
mutant enzyme D195S/Q197V, at pH 8.0 and 25°C
0.2
NAD+
-
wild type enzyme, at pH 8.0 and 25°C
0.2
NAD+
-
mutant enzyme D195S/Q197T, at pH 8.0 and 25°C
0.2
NAD+
-
mutant enzyme D195S/Y196A, at pH 8.0 and 25°C
0.2
NAD+
-
mutant enzyme D195S/Y196L, at pH 8.0 and 25°C
0.2
NAD+
-
mutant enzyme D195S/Y196S, at pH 8.0 and 25°C
0.21
NAD+
mutant enzyme D195N, in 0.1 M potassium phosphate buffer (pH 7.5)
0.21
NAD+
mutant enzyme D195N, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
0.22
NAD+
-
mutant enzyme D195S, at pH 8.0 and 25°C
0.22
NAD+
-
mutant enzyme Q197V, at pH 8.0 and 25°C
0.26
NAD+
mutant enzyme D195Q, in 0.1 M potassium phosphate buffer (pH 7.5)
0.26
NAD+
mutant enzyme D195Q, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
0.34
NAD+
mutant enzyme D195S, in 0.1 M potassium phosphate buffer (pH 7.5)
0.34
NAD+
mutant enzyme D195S, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
0.4
NAD+
mutant enzyme D195Q/Y196S, in 0.1 M potassium phosphate buffer (pH 7.5)
0.4
NAD+
mutant enzyme D195Q/Y196S, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
0.49
NAD+
mutant enzyme D195Q/Y196H, in 0.1 M potassium phosphate buffer (pH 7.5)
0.49
NAD+
mutant enzyme D195Q/Y196H, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
0.65
NAD+
Thermochaetoides thermophila
at pH 7.4 and 25°C
0.76
NAD+
mutant enzyme D195A, in 0.1 M potassium phosphate buffer (pH 7.5)
0.76
NAD+
mutant enzyme D195A, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
0.76
NAD+
25°C, pH not specified in the publication
0.76
NAD+
at pH 10.5 and 35°C
0.87
NAD+
mutant enzyme D195Q/Y196P, in 0.1 M potassium phosphate buffer (pH 7.5)
0.87
NAD+
mutant enzyme D195Q/Y196P, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
1.2
NAD+
in 0.1 M potassium phosphate buffer, pH 7.5, at 30°C
1.4
NAD+
-
wild-type enzyme
1.4
NAD+
-
pH 8.0, 20°C, wild-type enzyme
1.6
NAD+
-
mutant enzyme S195S
1.6
NAD+
-
pH 8.0, 20°C, mutant enzyme D195S
2.03
NAD+
at pH 7.5 and 25°C
2.6
NAD+
mutant enzyme I239C, at 30°C and pH 7.0
2.8
NAD+
-
mutant enzyme F290N, in 0.1 M sodium phosphate buffer, pH 7.0, at 30°C
2.8
NAD+
-
mutant enzyme F290N, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
2.9
NAD+
-
wild type enzyme, in 0.1 M sodium phosphate buffer, pH 7.0, at 30°C
2.9
NAD+
-
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
NAD+
wild type enzyme, at 30°C and pH 7.0
3.5
NAD+
-
mutant enzyme F290Q, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
3.5
NAD+
-
mutant enzyme F290Y, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
3.7
NAD+
wild type enzyme, in 0.1 M potassium phosphate buffer (pH 7.5)
3.7
NAD+
wild type enzyme, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
3.8
NAD+
-
mutant enzyme F290A, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
4
NAD+
-
mutant enzyme F290T, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
4
NAD+
-
mutant enzyme F311D, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
4.1
NAD+
-
mutant enzyme F290S, in 0.1 M sodium phosphate buffer, pH 7.0, at 30°C
4.1
NAD+
-
mutant enzyme F290S, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
4.3
NAD+
mutant enzyme A10C/I239C, at 30°C and pH 7.0
4.7
NAD+
-
mutant enzyme F290E, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
5
NAD+
mutant enzyme D221S, pH and temperature not specified in the publication
5.1
NAD+
-
mutant enzyme F290D, in 0.1 M sodium phosphate buffer, pH 7.0, at 30°C
5.1
NAD+
-
mutant enzyme F290D, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
5.18
NAD+
-
mutant enzyme C145S/A198G/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 30°C
5.4
NAD+
-
mutant enzyme F311S, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
5.5
NAD+
-
mutant enzyme F311N, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
5.6
NAD+
recombinant enzyme, at pH 7.5 and 25°C
6.2
NAD+
mutant enzyme A10C, at 30°C and pH 7.0
6.5
NAD+
pH 7.0, 30°C, wild-type enzyme
6.67
NAD+
in 100 mM Tris-HCl (pH 7.0), at 30°C
6.8
NAD+
mutant enzyme K328V, at pH 7.5 and 25°C
7.3
NAD+
wild type enzyme, pH and temperature not specified in the publication
7.3
NAD+
wild type enzyme, pH and temperature not specified in the publication
7.3
NAD+
-
mutant enzyme F311Y, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
7.3
NAD+
-
wild type enzyme, in 0.1 M sodium phosphate buffer, 0.01 M EDTA, pH 7.0, temperature not specified in the publication
7.3
NAD+
mutant enzyme A198G, pH and temperature not specified in the publication
7.3
NAD+
mutant enzyme A198G, pH and temperature not specified in the publication
8.22
NAD+
-
mutant enzyme C145S/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 30°C
18.68
NAD+
mutant enzyme V120S/N187D, at pH 9.5 and 30°C
22.3
NAD+
wild type enzyme, at pH 9.5 and 30°C
28.99
NAD+
mutant enzyme N187D, at pH 9.5 and 30°C
31
NAD+
-
at pH 7.0 and 25°C
40.63
NAD+
mutant enzyme V120S, at pH 9.5 and 30°C
890
NAD+
-
wild type enzyme, in the absence of 1-methyl-3-methylimidazolium dimethylphosphate, in 50 mM carbonate buffer, pH 9.7, at 30°C
1300
NAD+
-
wild type enzyme, in the presence of 30% (v/v) 1-methyl-3-methylimidazolium dimethylphosphate, in 50 mM carbonate buffer, pH 9.7, at 30°C
0.03
NADH
25°C, pH not specified in the publication
0.03
NADH
at pH 6.0 and 35°C
0.08
NADH
in 0.1 M sodium phosphate (pH 6.8), at 37°C
0.00004
NADP+
wild type enzyme, in 0.1 M potassium phosphate buffer (pH 7.5)
0.00004
NADP+
wild type enzyme, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
0.005
NADP+
in 0.1 M potassium phosphate buffer, pH 7.5, at 30°C
0.01
NADP+
-
mutant enzyme D195S/Q197V, at pH 8.0 and 25°C
0.03
NADP+
-
mutant enzyme Q197V, at pH 8.0 and 25°C
0.04
NADP+
-
mutant enzyme D195S, at pH 8.0 and 25°C
0.052
NADP+
mutant enzyme D195A, in 0.1 M potassium phosphate buffer (pH 7.5)
0.052
NADP+
mutant enzyme D195A, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
0.1
NADP+
-
mutant enzyme D195S/Y196L, at pH 8.0 and 25°C
0.16
NADP+
-
mutant enzyme D195S/Y196S, at pH 8.0 and 25°C
0.17
NADP+
-
mutant enzyme D195S/Y196A, at pH 8.0 and 25°C
0.26
NADP+
mutant enzyme D195N, in 0.1 M potassium phosphate buffer (pH 7.5)
0.26
NADP+
mutant enzyme D195Q, in 0.1 M potassium phosphate buffer (pH 7.5)
0.26
NADP+
mutant enzyme D195N, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
0.26
NADP+
mutant enzyme D195Q, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
0.26
NADP+
-
mutant enzyme D195S/Q197T, at pH 8.0 and 25°C
0.34
NADP+
mutant enzyme D195Q/Y196P, in 0.1 M potassium phosphate buffer (pH 7.5)
0.34
NADP+
mutant enzyme D195Q/Y196S, in 0.1 M potassium phosphate buffer (pH 7.5)
0.34
NADP+
mutant enzyme D195S, in 0.1 M potassium phosphate buffer (pH 7.5)
0.34
NADP+
mutant enzyme D195Q/Y196P, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
0.34
NADP+
mutant enzyme D195Q/Y196S, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
0.34
NADP+
mutant enzyme D195S, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
0.4
NADP+
-
at pH 7.0 and 25°C
0.44
NADP+
mutant enzyme D195Q/Y196H, in 0.1 M potassium phosphate buffer (pH 7.5)
0.44
NADP+
mutant enzyme D195Q/Y196H, in 0.1 M potassium phosphate buffer (pH 7.5), at 37°C
0.52
NADP+
-
mutant enzyme D221G, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
0.55
NADP+
-
mutant enzyme D221S, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
0.62
NADP+
-
mutant enzyme D221G/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
0.79
NADP+
-
mutant enzyme A198G/D221Q, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
1.04
NADP+
-
mutant enzyme D221Q, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
1.05
NADP+
-
mutant enzyme D221A, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
1.07
NADP+
in 100 mM Tris-HCl (pH 7.0), at 30°C
1.5
NADP+
-
mutant enzyme C145S/A198G/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
1.64
NADP+
-
mutant enzyme C145S/D221G/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
1.91
NADP+
-
mutant enzyme C145S/D221A/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
2.76
NADP+
-
mutant enzyme C145S/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
3.08
NADP+
-
mutant enzyme C145S/A198G/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 30°C
4.5
NADP+
pH 7.0, 30°C, mutant enzyme D196A/Y197R
7.89
NADP+
-
mutant enzyme C145S/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 30°C
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4.17
reduced 1,1'-diaminoethyl-4,4'-bipyridinium salt
at pH 7.4, temperature not specified in the publication
1.55
reduced 1,1'-dicarboxyl-4,4'-bipyridinium salt
at pH 7.4, temperature not specified in the publication
0.32
reduced 1-methyl-1'-aminoethyl-4,4'-bipyridinium salt
at pH 7.4, temperature not specified in the publication
0.09
reduced 1-methyl-1'-carboxymethyl-4,4'-bipyridinium salt
at pH 7.4, temperature not specified in the publication
0.15
reduced methyl viologen
at pH 7.4, temperature not specified in the publication
0.23
CO2
25°C, pH not specified in the publication
0.23
CO2
at pH 6.0 and 35°C
0.0019
formate
-
with NADP+ as cosubstrate, at pH 7.0 and 25°C
0.032
formate
-
mutant enzyme R587K, at pH 9.0 and 25°C
0.033
formate
-
mutant enzyme H387K, at pH 9.0 and 25°C
0.04
formate
25°C, pH not specified in the publication
0.04
formate
at pH 10.5 and 35°C
0.06
formate
Q00498
mutant enzyme Y302R, at pH 8.0 and 25°C
0.08
formate
Q00498
mutant enzyme N187E/N147R, at pH 8.0 and 25°C
0.1
formate
Q00498
mutant enzyme H13E, at pH 8.0 and 25°C
0.11
formate
Q00498
mutant enzyme N187E/Q105R, at pH 8.0 and 25°C
0.11
formate
Q00498
mutant enzyme Y160R, at pH 8.0 and 25°C
0.16
formate
Thermochaetoides thermophila
at pH 7.4 and 25°C
0.18
formate
Q00498
mutant enzyme N187E, at pH 8.0 and 25°C
0.187
formate
-
at pH 7.0 and 25°C
0.2
formate
Q00498
mutant enzyme N147R, at pH 8.0 and 25°C
0.24
formate
-
wild type enzyme, at pH 8.0 and 25°C
0.24
formate
Q00498
wild type enzyme, at pH 8.0 and 25°C
0.24
formate
Q00498
mutant enzyme Q105R, at pH 8.0 and 25°C
0.275
formate
mutant enzyme V120S/N187D, at pH 9.5 and 30°C
0.35
formate
Q00498
mutant enzyme Y160E, at pH 8.0 and 25°C
0.423
formate
wild type enzyme, at pH 9.5 and 30°C
0.491
formate
mutant enzyme N187D, at pH 9.5 and 30°C
0.618
formate
Thermochaetoides thermophila
-
at pH 7.0 and 25°C
0.62
formate
-
mutant enzyme F290N, in 0.1 M sodium phosphate buffer, pH 7.0, at 30°C
0.62
formate
-
mutant enzyme F290D, at pH 8.0 and 37°C
0.676
formate
mutant enzyme V120S, at pH 9.5 and 30°C
0.92
formate
-
mutant enzyme A267M/I272V, at pH 8.0 and 37°C
1
formate
-
mutant enzyme F290S, in 0.1 M sodium phosphate buffer, pH 7.0, at 30°C
1
formate
-
mutant enzyme F290S, at pH 8.0 and 37°C
1.02
formate
-
mutant enzyme F290D, in 0.1 M sodium phosphate buffer, pH 7.0, at 30°C
1.02
formate
-
mutant enzyme F290N, at pH 8.0 and 37°C
1.36
formate
-
mutant enzyme A267M/I272V/F290S, at pH 8.0 and 37°C
1.4
formate
recombinant enzyme, at pH 7.5 and 25°C
1.4
formate
mutant enzyme K328V, at pH 7.5 and 25°C
1.45
formate
-
mutant enzyme A267M/I272V/F290N, at pH 8.0 and 37°C
1.61
formate
-
mutant enzyme A267M/I272V/F290D, at pH 8.0 and 37°C
1.93
formate
-
wild type enzyme, in 0.1 M sodium phosphate buffer, pH 7.0, at 30°C
1.93
formate
-
wild type enzyme, at pH 8.0 and 37°C
2.38
formate
-
mutant enzyme A267M, at pH 8.0 and 37°C
2.8
formate
wild type enzyme, at pH 7.2 and 30°C
2.83
formate
at pH 6.5 and 30°C
3
formate
-
with NAD+ as cosubstrate, at pH 7.0 and 25°C
5.1
formate
mutant enzyme T321S, at pH 7.2 and 30°C
9.38
formate
-
mutant enzyme H387M, at pH 9.0 and 25°C
15.5
formate
mutant enzyme N187S, at pH 7.2 and 30°C
19
formate
mutant enzyme N187S/T321S, at pH 7.2 and 30°C
173
formate
-
at pH 7.0 and 30°C
186.4
formate
-
wild type enzyme, at pH 9.0 and 25°C
820
formate
at pH 7.5 and 25°C
0.01
HCO3-
-
at pH 7.0 and 25°C
0.069
HCO3-
Thermochaetoides thermophila
-
at pH 7.0 and 25°C
0.36
NAD+
Thermochaetoides thermophila
at pH 7.4 and 25°C
0.63
NAD+
25°C, pH not specified in the publication
0.63
NAD+
at pH 10.5 and 35°C
5.008
NAD+
mutant enzyme V120S, at pH 9.5 and 30°C
6.618
NAD+
wild type enzyme, at pH 9.5 and 30°C
7.04
NAD+
mutant enzyme D221S, pH and temperature not specified in the publication
9.26
NAD+
mutant enzyme A198G/D221S, pH and temperature not specified in the publication
9.808
NAD+
mutant enzyme N187D, at pH 9.5 and 30°C
9.934
NAD+
mutant enzyme V120S/N187D, at pH 9.5 and 30°C
20
NAD+
mutant enzyme I239C, at 30°C and pH 7.0
36
NAD+
mutant enzyme A10C/I239C, at 30°C and pH 7.0
40
NAD+
-
mutant enzyme D195S/Q197V, at pH 8.0 and 25°C
60
NAD+
-
mutant enzyme Q197V, at pH 8.0 and 25°C
62
NAD+
wild type enzyme, at 30°C and pH 7.0
70
NAD+
at pH 7.5 and 30°C
73.3
NAD+
in 100 mM Tris-HCl (pH 7.0), at 30°C
84
NAD+
mutant enzyme A10C, at 30°C and pH 7.0
90
NAD+
-
mutant enzyme D195S/Y196S, at pH 8.0 and 25°C
91.3
NAD+
wild type enzyme, pH and temperature not specified in the publication
122
NAD+
wild type enzyme, pH and temperature not specified in the publication
140
NAD+
-
mutant enzyme A267M/I272V/F290D, at pH 8.0 and 37°C
162
NAD+
mutant enzyme A198G, pH and temperature not specified in the publication
170
NAD+
-
mutant enzyme A267M/I272V, at pH 8.0 and 37°C
180
NAD+
recombinant enzyme, at pH 7.5 and 25°C
200
NAD+
-
mutant enzyme F290N, in 0.1 M sodium phosphate buffer, pH 7.0, at 30°C
200
NAD+
-
mutant enzyme F290D, at pH 8.0 and 37°C
209
NAD+
mutant enzyme A198G, pH and temperature not specified in the publication
220
NAD+
-
wild type enzyme, in 0.1 M sodium phosphate buffer, pH 7.0, at 30°C
220
NAD+
-
wild type enzyme, at pH 8.0 and 37°C
220
NAD+
-
mutant enzyme D195S, at pH 8.0 and 25°C
230
NAD+
-
mutant enzyme A267M/I272V/F290N, at pH 8.0 and 37°C
230
NAD+
-
mutant enzyme A267M/I272V/F290S, at pH 8.0 and 37°C
260
NAD+
-
mutant enzyme D195S/Y196L, at pH 8.0 and 25°C
270
NAD+
mutant enzyme K328V, at pH 7.5 and 25°C
320
NAD+
-
wild type enzyme, at pH 8.0 and 25°C
400
NAD+
-
mutant enzyme F290D, in 0.1 M sodium phosphate buffer, pH 7.0, at 30°C
400
NAD+
-
mutant enzyme F290N, at pH 8.0 and 37°C
450
NAD+
-
mutant enzyme F290S, in 0.1 M sodium phosphate buffer, pH 7.0, at 30°C
450
NAD+
-
mutant enzyme F290S, at pH 8.0 and 37°C
479
NAD+
-
at pH 7.0 and 25°C
510
NAD+
-
mutant enzyme A267M, at pH 8.0 and 37°C
900
NAD+
-
mutant enzyme D195S/Q197T, at pH 8.0 and 25°C
1460
NAD+
-
mutant enzyme D195S/Y196A, at pH 8.0 and 25°C
7333
NAD+
-
wild type enzyme, in the presence of 30% (v/v) 1-methyl-3-methylimidazolium dimethylphosphate, in 50 mM carbonate buffer, pH 9.7, at 30°C
20600
NAD+
-
wild type enzyme, in the absence of 1-methyl-3-methylimidazolium dimethylphosphate, in 50 mM carbonate buffer, pH 9.7, at 30°C
97000
NAD+
at pH 7.5 and 25°C
0.17
NADH
25°C, pH not specified in the publication
0.17
NADH
at pH 6.0 and 35°C
1.6
NADH
in 0.1 M sodium phosphate (pH 6.8), at 37°C
0.011
NADP+
-
at pH 7.0 and 25°C
0.306
NADP+
in 100 mM Tris-HCl (pH 7.0), at 30°C
1.29
NADP+
-
mutant enzyme D221S, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
1.69
NADP+
-
mutant enzyme D221G, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
2.58
NADP+
-
mutant enzyme C145S/D221A/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
2.58
NADP+
-
mutant enzyme D221G/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
2.67
NADP+
-
mutant enzyme D221Q, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
2.83
NADP+
-
mutant enzyme D221A, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
2.88
NADP+
-
mutant enzyme C145S/D221G/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
2.94
NADP+
-
mutant enzyme A198G/D221Q, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
4.5
NADP+
-
mutant enzyme D195S/Q197V, at pH 8.0 and 25°C
4.68
NADP+
-
mutant enzyme C145S/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
8
NADP+
-
mutant enzyme D195S, at pH 8.0 and 25°C
8.58
NADP+
-
mutant enzyme C145S/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 30°C
17.9
NADP+
-
mutant enzyme C145S/A198G/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22°C
18
NADP+
-
mutant enzyme Q197V, at pH 8.0 and 25°C
19
NADP+
-
mutant enzyme D195S/Y196S, at pH 8.0 and 25°C
20
NADP+
-
mutant enzyme D195S/Y196A, at pH 8.0 and 25°C
21
NADP+
-
mutant enzyme C145S/A198G/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 30°C
50
NADP+
-
mutant enzyme D195S/Y196L, at pH 8.0 and 25°C
56
NADP+
-
mutant enzyme D195S/Q197T, at pH 8.0 and 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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.
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.
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.
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.
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.
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.
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A267M
-
the mutant shows increased catalytic efficiency compared to the wild type enzyme
A267M/I272V
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
A267M/I272V/F290D
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
A267M/I272V/F290N
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
A267M/I272V/F290S
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
F290A
-
the thermal stability of the mutant increases 1.3fold compared to the wild type enzyme
F290E
-
the thermal stability of the mutant increases 55fold compared to the wild type enzyme
F290Q
-
the thermal stability of the mutant increases 5.1fold compared to the wild type enzyme
F290T
-
the thermal stability of the mutant increases 5fold compared to the wild type enzyme
F290Y
-
the thermal stability of the mutant increases 1.4fold compared to the wild type enzyme
A198G
the mutant shows 1.8 fold increased activity compared to the wild type enzyme
A198G/D221Q
-
the mutant has the highest catalytic efficiency (kcat/Km) with NADP+
C145S/A198G/D221Q/C255V
-
the mutant confers a high resistance to ethyl 4-chloroacetoacetate (the half-life of this enzyme in 4 and 20 mM ethyl 4-chloroacetoacetate is over 200 h and 172 h, respectively) and shows 6fold enhanced catalytic efficiency with NADP+ compared to the wild type enzyme
C145S/D221A/C255V
-
the mutant has the lowest Km for formate
C145S/D221Q/C255V
-
the mutant shows the highest specific activity for a NADP+-accepting enzyme
C146S/C256V
-
85% increase of activity in presence of ethyl acetate, 104% residual activity in presence of 20 mM ethyl-4-chloroacetoacetate
C256V
-
11% increase of activity in presence of ethyl acetate, 100% residual activity in presence of 20 mM ethyl-4-chloroacetoacetate
C6A/C146A/C256V
-
119% increase of activity in presence of ethyl acetate, 106% residual activity in presence of 20 mM ethyl-4-chloroacetoacetate
C6A/C146S/C256V
-
37% increase of activity in presence of ethyl acetate, 108% residual activity in presence of 20 mM ethyl-4-chloroacetoacetate
C6A/C146V/C256V
-
15% decrease of activity in presence of ethyl acetate, 100% residual activity in presence of 20 mM ethyl-4-chloroacetoacetate
C6A/C256S
-
9% increase of activity in presence of ethyl acetate, 97% residual activity in presence of 20 mM ethyl-4-chloroacetoacetate
C6A/C256V
-
11% increase of activity in presence of ethyl acetate, 94.5% residual activity in presence of 20 mM ethyl-4-chloroacetoacetate
C6S/C256A
-
25% increase of activity in presence of ethyl acetate, 120% residual activity in presence of 20 mM ethyl-4-chloroacetoacetate
C6S/C256S
-
5% increase of activity in presence of ethyl acetate, 125% residual activity in presence of 20 mM ethyl-4-chloroacetoacetate
C6S/C256V
-
10% increase of activity in presence of ethyl acetate, 94% residual activity in presence of 20 mM ethyl-4-chloroacetoacetate
C6V/C256S
-
5% increase of activity in presence of ethyl acetate, 92% residual activity in presence of 20 mM ethyl-4-chloroacetoacetate
D221A
-
the mutant shows catalytic efficiency with NADP+ as compared to the wild type enzyme
D221G
-
the mutant is extremely sensitive to ethyl 4-chloroacetoacetate with half-lives shorter than 6 min
D221G/C255V
-
the mutant is inhibited by NADP+ (Ki of 15 mM)
D221Q
-
the mutant shows catalytic efficiency with NADP+ compared to the wild type enzyme
D221S
-
the mutant shows catalytic efficiency with NADP+ as compared to the wild type enzyme
E61K
-
rate constant of thermal inactivation at 54°C, 60°C, 62°C and 65°C is decreased compared to wild-type enzyme
E61P
-
rate constant of thermal inactivation at 54°C, 60°C, 62°C and 65°C is decreased compared to wild-type enzyme
E61Q
-
rate constant of thermal inactivation at 54°C, 60°C, 62°C and 65°C is decreased compared to wild-type enzyme
A198G/D221Q
-
the mutant has the highest catalytic efficiency (kcat/Km) with NADP+
-
C145S/A198G/D221Q/C255V
-
the mutant confers a high resistance to ethyl 4-chloroacetoacetate (the half-life of this enzyme in 4 and 20 mM ethyl 4-chloroacetoacetate is over 200 h and 172 h, respectively) and shows 6fold enhanced catalytic efficiency with NADP+ compared to the wild type enzyme
-
C145S/D221Q/C255V
-
the mutant shows the highest specific activity for a NADP+-accepting enzyme
-
D221A
-
the mutant shows catalytic efficiency with NADP+ as compared to the wild type enzyme
-
D221Q
-
the mutant shows catalytic efficiency with NADP+ compared to the wild type enzyme
-
E61K
-
rate constant of thermal inactivation at 54°C, 60°C, 62°C and 65°C is decreased compared to wild-type enzyme
-
E61P
-
rate constant of thermal inactivation at 54°C, 60°C, 62°C and 65°C is decreased compared to wild-type enzyme
-
E61Q
-
rate constant of thermal inactivation at 54°C, 60°C, 62°C and 65°C is decreased compared to wild-type enzyme
-
E141N
-
4.3fold decrease in Km value, 590fold decrease in kcat value for formate, marked enhancement of glyoxylate reducing activity, conversion of enzyme to a 2-hydroxy acid dehydrogenase
E141Q
-
5.5fold decrease in Km value, 110fold decrease in kcat value for formate
A191G
non-optimal residue located by Ramachandran-plot, mutation has no significant effect on enzyme stability. No significant change in enzyme kinetic properties
C255M
-
high resistance to inactivation by Hg2+, increase of enzyme stability at 25°C, decrease of thermostability above 45°C. Native enzyme preserves more than 80% of initial activity after 2 h in 7 M urea. The mutant enzyme is completely inactive
C255S
-
high resistance to inactivation by Hg2+, increase of enzyme stability at 25°C, decrease of thermostability above 45°C. Native enzyme preserves more than 80% of initial activity after 2 h in 7 M urea. The mutant enzyme is completely inactive
F311D
-
the thermal stability of the mutant increases 2.42fold compared to the wild type enzyme
F311N
-
the thermal stability of the mutant decreases 0.49fold compared to the wild type enzyme
F311S
-
the thermal stability of the mutant decreases 0.52fold compared to the wild type enzyme
F311Y
-
the thermal stability of the mutant increases 1.59fold compared to the wild type enzyme
H263G
non-optimal residue located by Ramachandran-plot, mutation causes destabilization of enzyme and a 1.3fold increase in the monomolecular inactivation rate constant. No significant change in enzyme kinetic properties
H332F
-
complete loss of activity. The mutant is still able to bind coenzyme, but not substrate or analogues
K61R
-
rate constant of thermal inactivation at 54°C and at 60°C is slightly decreased, at 62°C, and 65°C the constant is increased compared to wild-type enzyme
N136G
non-optimal residue located by Ramachandran-plot, mutation results in higher thermal stability and decreases the inactivation rate by 1.2fold. No significant change in enzyme kinetic properties
N234G
non-optimal residue located by Ramachandran-plot, mutation has no significant effect on enzyme stability. No significant change in enzyme kinetic properties
Q313E
-
mutation shifts the pK of the group controlling formate binding from less than 5.5 in wild-type enzyme to 7.6
Y144G
non-optimal residue located by Ramachandran-plot, mutation results in higher thermal stability and decreases the inactivation rate by 1.4fold. 75% increase in Km-value of formate compared to wild-type
A198G
the mutation reduces the KM value for NAD+ while the KM for CO2 remains practically unchanged, compared to the wild type enzyme
A198G/D221S
the mutant has its coenzyme specificity changed from NAD+ to NADP+ compared to the wild type enzyme
D221S
the mutant has its coenzyme specificity changed from NAD+ to NADP+ compared to the wild type enzyme
H387K
-
the mutant shows about 6200fold decreased catalytic efficiency compared to the wild type enzyme
H387M
-
the mutant shows about 20fold decreased catalytic efficiency compared to the wild type enzyme
R587K
-
the mutant shows about 6200fold decreased catalytic efficiency compared to the wild type enzyme
D196A/Y197R
coenzyme preference is shifted from NAD+ to NADP+, decreased thermal stability at 42°C
A10C
there are no significant changes in the optimum temperature and pH between variant and wild type enzyme but the mutant shows a significant increase in copper ion resistance and acid resistance, a 6.7fold increase in half-life at 60°C, and a 1.4fold increase in catalytic efficiency compared with the wild type
A10C/I239C
there are no significant changes in the optimum temperature and pH between variant and wild type enzyme
C23S
-
in biotechnological applications, enzyme mutant performs much better than wild-type in quiescent solution and reactors with little mechanical stress
C23S/C262A
-
in biotechnological applications, enzyme mutant performs much better than wild-type in quiescent solution and reactors with little mechanical stress. Less stable than wild-type at high stress levels in the Couette viscometer or the bubble column
D195/Y196P
the mutant shows an improvement in overall catalytic efficiency with NADP+ and a decrease in the efficiency with NAD+ as cofactors compared to the wild type enzyme
D195/Y196S
the mutant shows an improvement in overall catalytic efficiency with NADP+ and a decrease in the efficiency with NAD+ as cofactors compared to the wild type enzyme
E53V
-
90% residual activity in presence of 8% acrylamide and 0.1% TEMED, 4fold increase compared to wild-type
E53V/K56R
-
90% residual activity in presence of 8% acrylamide and 0.1% TEMED, 4.1fold increase compared to wild-type
E53V/K56R/C23S
-
90% residual activity in presence of 15% acrylamide and 0.1% TEMED, 42fold increase compared to wild-type
I239C
there are no significant changes in the optimum temperature and pH between variant and wild type enzyme
K35T
-
70% residual activity in presence of 8% acrylamide and 0.1% TEMED, 2.7fold increase compared to wild-type
K360A
-
unchanged turnover number and Km-values for formate, but shows reduced affinity for NAD+
K47E
the mutation improves the crystallizability of the protein and also the catalytic properties and the stability of the enzyme, the specific activity of freshly prepared mutant is similar to that of wild type and native protein
N187D
the mutant shows increased catalytic efficiency compared to the wild type enzyme
N187S
the mutation is responsible for improved activity through an enhancement of the kcat value by a factor of 5.8
N187S/T321S
the mutation is responsible for improved activity through an enhancement of the kcat value by a factor of 6.7
T321S
the mutation is responsible for improved activity through an enhancement of the kcat value by a factor of 1.8
V120S
the mutant has the highest catalytic efficiency with formate as it enhances the kcat and kcat/Km values 3.48fold and 1.6fold, respectively, compared to the wild type enzyme
V120S/N187D
the mutant has the highest catalytic efficiency with NAD+ as it displays an approximately 1.5fold increase in kcat/Km compared to the wild type enzyme
N187D
-
the mutant shows increased catalytic efficiency compared to the wild type enzyme
-
V120S
-
the mutant has the highest catalytic efficiency with formate as it enhances the kcat and kcat/Km values 3.48fold and 1.6fold, respectively, compared to the wild type enzyme
-
V120S/N187D
-
the mutant has the highest catalytic efficiency with NAD+ as it displays an approximately 1.5fold increase in kcat/Km compared to the wild type enzyme
-
D195S/Q197T
-
the mutant with increased activity with NAD+ compared to the wild type enzyme also shows activity with NADP+
D195S/Q197V
-
the mutant with decreased activity with NAD+ compared to the wild type enzyme also shows activity with NADP+
D195S/Y196A
-
the mutant with increased activity with NAD+ compared to the wild type enzyme also shows activity with NADP+
D195S/Y196L
-
the mutant with decreased activity with NAD+ compared to the wild type enzyme also shows activity with NADP+
D195S/Y196S
-
the mutant with decreased activity with NAD+ compared to the wild type enzyme also shows activity with NADP+
D62C
-
the mutant has 6% of the activity of the native enzyme in reducing conditions, but it has no observable activity in oxidizing conditions
H13E
Q00498
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
M156C/L159C
-
no FDH activity
M1C
-
the catalytic efficiency (kcat/KM) of the mutant is 63% better than that of the native enzyme and the Tm value of this mutant is significantly higher than that of the native enzyme. The affinity of the mutant for formate is increased 31% than that of the native enzyme
M1C/D62C
-
the mutant has only 3.75% and 1.6% of the catalytic efficiency of the native enzyme in oxidizing and reducing conditions, respectively
N147R
Q00498
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
N187E
Q00498
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
N187E/N147R
Q00498
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
N187E/Q105R
Q00498
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
N300E/N147R
Q00498
inactive
Q105R
Q00498
the mutant shows wild type catalytic efficiency
Q197V
-
the mutant with decreased activity with NAD+ compared to the wild type enzyme also shows activity with NADP+
T169C/T226C
-
mutant is less active and less thermostable than wild type FDH
T169V
-
Km-value for formate is 55% of the wild-type value, turnover-number is 25% of the wild-type value
T169V/T226V
-
Km-value for formate is increased 1.7fold compared to the wild-type value, turnover number is 25% of the wild-type value
T226V
-
Km-value for formate is 104% of the wild-type value, turnover-number is 91% of the wild-type value
V88C/V112C
-
no FDH activity
Y160E
Q00498
the mutant shows increased catalytic efficiency compared to the wild type enzyme
Y160R
Q00498
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
Y302R
Q00498
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
additional information
-
immobilization of enzyme with N-hydroxysuccinimidyl ester of methoxy polyethylene glycol propionic acid in order to reduce immunogenicity of enzyme when applied intravenously during detoxification of formate in methanol poisoning
F290D
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
F290D
-
the Km for formate is increased while KM for NAD+ does not change. The mutation increases the Tm values by 4.3°C. The catalytic efficiency for NAD+ is about 2fold higher compared to the wild type enzyme
F290D
-
the thermal stability of the mutant increases 61fold compared to the wild type enzyme
F290N
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
F290N
-
the Km for formate is increased while KM for NAD+ does not change. The mutation increases the Tm values by 2.9°C. The catalytic efficiency for NAD+ is about 2fold higher compared to the wild type enzyme
F290N
-
the thermal stability of the mutant increases 12.3fold compared to the wild type enzyme
F290S
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
F290S
-
the Km for formate is increased while Km for NAD+ slightly increases. The mutation increases the Tm values by 7.8°C. The catalytic efficiency for NAD+ is slightly decreased compared to the wild type enzyme
F290S
-
the thermal stability of the mutant increases 4.8fold compared to the wild type enzyme
R284A
-
change of the catalytic, thermodynamic and spectral properties of the enzyme. The affinity of the mutants for the substrate formate or the transition state analogue azide decreases
R284A
-
mutant enzyme is completely inactive
R284Q
-
change of the catalytic, thermodynamic and spectral properties of the enzyme. The affinity of the mutants for the substrate formate or the transition state analogue azide decreases
R284Q
-
Km-value for formate and Ki-value for azide decreases, KM-value for NAD+ is not affected
D195A
reduced activity
D195A
increased activity with NADP+, decreased activity with NAD+ compared to the wild type enzyme
D195A
mutant shows a noticeable decrease of Km for NADP+ (approximately 10fold) with concomitant increase of kcat (approximately 10000fold) for NADP+ compared to the wild type enzyme, in addition the Km for NAD+ is dramatically increased
D195N
reduced activity
D195N
increased activity with NADP+, decreased activity with NAD+ compared to the wild type enzyme
D195N
mutant shows a noticeable decrease of Km for NADP+ (approximately 10fold) with concomitant increase of kcat (approximately 10000fold) for NADP+ compared to the wild type enzyme, in addition the Km for NAD+ is dramatically increased
D195Q
reduced activity
D195Q
increased activity with NADP+, decreased activity with NAD+ compared to the wild type enzyme
D195Q
mutant shows a noticeable decrease of Km for NADP+ (approximately 10fold) with concomitant increase of kcat (approximately 10000fold) for NADP+ compared to the wild type enzyme, in addition the Km for NAD+ is dramatically increased
D195Q/Y196H
the double mutant shows a more than 20000000fold improvement in overall catalytic efficiency with NADP+ and a more than 900fold decrease in the efficiency with NAD+ as cofactors
D195Q/Y196H
the mutant shows a more than 20000000fold improvement in overall catalytic efficiency with NADP+ and a more than 900fold decrease in the efficiency with NAD+ as cofactors compared to the wild type enzyme
D195Q/Y196H
the double mutant shows a more than 20000000fold improvement in overall catalytic efficiency with NADP+ and a more than 900fold decrease in the efficiency with NAD+ as cofactors, exhibits high catalytic activity with NADP+ as coenzyme (14% of the catalytic activity of the wild type for NAD+)
D195Q/Y196P
the double mutant shows increased activity with NADP+, decreased activity with NAD+ compared to the wild type enzyme
D195Q/Y196P
the double mutant shows an improvement in overall catalytic efficiency with NADP+ and a decrease in the efficiency with NAD+ as cofactors
D195Q/Y196S
the double mutant shows decreased activity with NADP+ and NAD+ compared to the wild type enzyme
D195Q/Y196S
the double mutant shows an improvement in overall catalytic efficiency with NADP+ and a decrease in the efficiency with NAD+ as cofactors
D195S
reduced activity
D195S
increased activity with NADP+, decreased activity with NAD+ compared to the wild type enzyme
D195S
mutant shows a noticeable decrease of Km for NADP+ (approximately 10fold) with concomitant increase of kcat (approximately 10000fold) for NADP+ compared to the wild type enzyme, in addition the Km for NAD+ is dramatically increased
K328V
the mutation improves the crystallizability of the protein and also the catalytic properties and the stability of the enzyme, the specific activity of freshly prepared mutant is similar to that of wild type and native protein
K328V
the mutant shows increased catalytic efficiency for NAD+ compared to the wild type enzyme
D195S
-
mutant enzyme also can use NADP+ as coenzyme
D195S
-
mutant enzyme shows similar catalytic constant to wild-type in the reaction with NAD+. In contrast with wild-type, the reaction of NADP+ catalyzed by the mutant is clearly discernible
D195S
-
the mutant with decreased activity with NAD+ compared to the wild type enzyme also shows activity with NADP+
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25 - 48
melting temperature is 48°C. The enzyme remains stable for up to 30 min at 25°C
25 - 50
-
the enzyme remains stable from 25-50°C and rapidly loses activity at higher temperatures (inactive at 60°C)
30
-
pH 5.2-9.0, 1 h, more than 90% of the activity is retained
30 - 40
the enzyme remains stable after 1 h at 30-40°C
30 - 52
the enzyme remains stable after 20 min at 30-52°C. The half-life temperature is 56.7°C. The enzyme is inactivated after 20 min at 60°C
37
methylotrophic bacterium
-
almost complete inactivation in 2-3 days, -SH compounds protect against inactivation, NAD+ or NADH decreases the inactivation rate, inactivation rate is significantly diminished in presence of formate, strongest stabilization by EDTA
4 - 50
the Escherichia coli cell-surface-displayed enzyme retains its original enzymatic activity after incubation at 4°C for 1 month with the half-life of 17 days at 40°C and 38 h at 50°C
40
after 2 h at 40°C and 60°C, the wild type enzyme retains 44% and 10% of its initial activity, respectively
40 - 60
the enzyme retains 93, 88, 83, and 71% of its initial activity after 4 h of exposure at 40, 50, 55, and 60 °C, respectively
42
wild-type enzyme loses 50% of its activity after 3.5 min, mutant enzyme D196A/Y197R loses 50% of its activity after 1.5 min
45
-
rapid inactivation above
52
methylotrophic bacterium
-
inactivation rate constant is zero
55 - 60
Thermochaetoides thermophila
the enzyme exhibits good stability up to 55°C. The activity is lost between 55°C and 60°C. The temperature at which half of the activity is left at pH 5.0 is determined as 58°C
57.9
-
melting temperature, medium stability of enzyme in comparison with enzymes from Moraxella sp. C1, Pseudomonas sp. 101, Candida boidinii, and Arabidosis thaliana. Irreversible inactivation according to first-order reaction kinetics
58
Kloeckera sp.
-
10 min, 60% loss of activity
61
methylotrophic bacterium
-
inactivation rate constant: 0.0114/min
63.4
-
melting temperature, medium stability of enzyme in comparison with enzymes from Pseudomonas sp., Candida boidinii, Arabidopsis thaliana, and Glycine max. Irreversible inactivation according to first-order reaction kinetics
64.5
-
melting temperature, medium stability of enzyme in comparison with enzymes from Moraxella sp. C1, Pseudomonas sp. 101, Arabidopsis thaliana, and Glycine max. Irreversible inactivation according to first-order reaction kinetics
64.9
-
melting temperature, medium stability of enzyme in comparison with enzymes from Moraxella sp. C1, Pseudomonas sp. 101, Candida boidinii, and Glycine max. Irreversible inactivation according to first-order reaction kinetics
65.5
methylotrophic bacterium
-
inactivation rate constant: 0.10/min
67.6
-
melting temperature, highest thermal stability of enzyme in comparison with enzymes from Moraxella sp. C1, Candida boidinii, Arabidopsis thaliana, and Glycine max. Irreversible inactivation according to first-order reaction kinetics
70
-
the enzyme has a half-life of activity of approximately 20 min at 70°C under anaerobic conditions
50
pH 7.0, 10 min, stable at or lower
50
Kloeckera sp.
-
10 min, stable
50
-
pH 9.0, 10 min, about 50% loss of activity
50
-
1 min, 50% loss of activity
50
-
native enzyme, pH 7.0, 10 h, fully active
50
-
pH 7.0, 10 min, stable at or below
50 - 60
the enzyme is stable at temperatures below 55°C for 30 min and retains 71% of the initial activity after incubation at 60°C for 30 min. The half-life at 60°C is 52.9 min
50 - 60
Q00498
the wild type enzyme retains full activity after 20 min incubation at 50°C and shows 85.5 and 6.6% activity after 20 min incubation at 55 and 60°C, respectively
54
-
10 min, 50% loss of activity
54
-
rate constant of thermal inactivation is 0.0000104 per sec for wild-type enzyme, 0.0000093 per sec for mutant enzyme E61Q, 0.00000754 per sec for mutant enzyme E61P and 0.00000766 per sec for mutant enzyme E61K
54
-
rate constant of thermal inactivation is 0.00000504 per sec for wild-type enzyme and 0.00000463 per sec for mutant enzyme K61R
55
Candida methanolica
-
10 min, pH 6.5-9.5, stable up to
55
-
10 min, stable up to
55
-
pH 9.0, 10 min, stable
55
-
1 h, 75% loss of activity
55
-
pH 7.0, 10 min, about 55% loss of activity
55
at 55°C, where native FDH loses 50% activity within 20 min incubation due to heat inactivation, the mutants preserve 84% (K47E) and 70% (K328V) residual activity
60
Candida methanolica
-
10 min, 36% loss of activity
60
-
10 min, 88% loss of activity
60
-
10 min, complete loss of activity
60
-
rate constant of thermal inactivation is per 0.000336 sec for wild-type enzyme, 0.000174 per sec for mutant enzyme E61Q, 0.000115 per sec for mutant enzyme E61P and 0.000117 per sec for mutant enzyme E61K
60
-
rate constant of thermal inactivation is 0.0000755 per sec for wild-type enzyme and 0.000071 per sec for mutant enzyme K61R
60
-
pH 7.0, 10 min, complete loss of activity
62
-
rate constant of thermal inactivation is per 0.000924 sec for wild-type enzyme, 0.000590 per sec for mutant enzyme E61Q, 0.000335 per sec for mutant enzyme E61P and 0.0004 per sec for mutant enzyme E61K
62
-
rate constant of thermal inactivation is 0.000155 per sec for wild-type enzyme and 0.000212 per sec for mutant enzyme K61R
62
wild-type, monomolecular inactivation rate constant 25000 per sec
63
-
rate constant of thermal inactivation is 0.000320 per sec for wild-type enzyme and 0.00000463 per sec for mutant enzyme K61R
63
-
native enzyme, pH 7.0, half-life 1 h
65
-
10 min, complete inactivation
65
-
rate constant of thermal inactivation is per 0.002860 sec for wild-type enzyme, 0.00224 per sec for mutant enzyme E61Q, 0.0012 per sec for mutant enzyme E61P and 0.00131 per sec for mutant enzyme E61K
65
-
rate constant of thermal inactivation is 0.000774 per sec for wild-type enzyme and 0.000813 per sec for mutant enzyme K61R
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