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CO2 + NADPH
formate + NADP+
formate + NAD+
CO2 + NADH + H+
formate + NADP+
CO2 + NADPH
formate + NADP+
CO2 + NADPH + H+
formate + reduced methyl viologen
CO2 + oxidized methyl viologen
-
-
-
-
r
additional information
?
-
CO2 + NADPH
formate + NADP+
-
-
-
-
?
CO2 + NADPH
formate + NADP+
-
-
-
-
r
CO2 + NADPH
formate + NADP+
-
enzyme also catalyzes: 1. reversible electron transfer between methyl viologen and NADPH, 2. reduction of FMN or FAD with NADPH (caused by a contaminating protein)
-
-
?
CO2 + NADPH
formate + NADP+
-
reduction of FMN or FAD with NADPH caused by a contaminating protein
-
-
?
CO2 + NADPH
formate + NADP+
-
enzyme also catalyzes: 3. oxidation of NADPH with O2
-
-
r
CO2 + NADPH
formate + NADP+
-
also reacts with: methyl viologen, benzyl viologen
-
-
r
CO2 + NADPH
formate + NADP+
-
first enzyme in pathway of reduction of CO2 to acetate: CO2 serves as electron acceptor generated during fermentation
-
?
formate + NAD+
CO2 + NADH + H+
the activity to NAD+ is 38% of that to NADP+
-
-
?
formate + NAD+
CO2 + NADH + H+
the activity to NAD+ is 38% of that to NADP+
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
?
formate + NAD+
CO2 + NADH + H+
-
-
-
?
formate + NADP+
CO2 + NADPH
-
-
-
-
?
formate + NADP+
CO2 + NADPH
NADP+ is the preferred cofactor
-
-
?
formate + NADP+
CO2 + NADPH
NADP+ is the preferred cofactor
-
-
?
formate + NADP+
CO2 + NADPH
-
-
-
-
?
formate + NADP+
CO2 + NADPH
-
-
-
-
?
formate + NADP+
CO2 + NADPH
-
-
-
-
?
formate + NADP+
CO2 + NADPH
-
-
-
-
?
formate + NADP+
CO2 + NADPH
-
-
-
-
?
formate + NADP+
CO2 + NADPH
-
-
-
-
?
formate + NADP+
CO2 + NADPH
-
-
-
-
?
formate + NADP+
CO2 + NADPH + H+
the enzyme acts only on formate as the substrate
-
-
?
formate + NADP+
CO2 + NADPH + H+
the enzyme acts only on formate as the substrate
-
-
?
additional information
?
-
-
no activity with NAD+
-
-
?
additional information
?
-
methanol, formaldehyde, acetic acid, ethanol, propanol and glycerol are inert. When artificial electron acceptors are used, ferricyanide, nitro blue tetrazolium, phenazine methosulfate, riboflavin, ATP and FAD are not reduced in the presence of formate
-
-
?
additional information
?
-
methanol, formaldehyde, acetic acid, ethanol, propanol and glycerol are inert. When artificial electron acceptors are used, ferricyanide, nitro blue tetrazolium, phenazine methosulfate, riboflavin, ATP and FAD are not reduced in the presence of formate
-
-
?
additional information
?
-
no activity is detected with malic acid, sodium citrate, sodium nitrate, succinic acid, sodium bicarbonate, sodium phosphite, ethanol, methanol, formaldehyde, sodium acetate, or sodium lactate
-
-
?
additional information
?
-
no activity is detected with malic acid, sodium citrate, sodium nitrate, succinic acid, sodium bicarbonate, sodium phosphite, ethanol, methanol, formaldehyde, sodium acetate, or sodium lactate
-
-
?
additional information
?
-
-
no activity with NAD+
-
-
?
additional information
?
-
-
no activity with NAD+
-
-
?
additional information
?
-
-
no activity with NAD+
-
-
?
additional information
?
-
-
no activity with NAD+
-
-
?
additional information
?
-
-
no activity with NAD+
-
-
?
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5,5'-dithio-bis(2-nitrobenzoic acid)
complete inhibition at 1 mM
AgNO3
complete inhibition at 1 mM
azide
-
competitive inhibitor
CdCl2
slight inhibition at 1 mM
CoCl2
slight inhibition at 1 mM
CuSO4
slight inhibition at 1 mM
DMSO
1-33% residual activity at 40% (v/v)
ethanol
complete inhibition at 40% (v/v)
ethyl 4-chloroacetoacetate
-
-
FeCl2
complete inhibition at 1 mM
formaldehyde
79.8% residual activity at 0.1 M
HgCl2
complete inhibition at 1 mM
hydroxylamine
slight inhibition at 10 mM
Isopropanol
33-66% residual activity at 20 and 40% (v/v)
methanol
complete inhibition at 40% (v/v)
NADP+
-
substrate inhibition at 5 mM or higher concentration
NaNO3
slight inhibition at 1 mM
Sodium nitrate
44.3% residual activity at 0.1 M
sulfite
-
inhibition of activity with NADP+ but not with methyl viologen
tert-butanol
33-66% residual activity at 10, 20 and 40% (v/v)
Triton X-100
33-66% residual activity at 5 and 10% (v/v)
2,3-Butanedione
-
sodium azide and NADP+ protect
2,3-Butanedione
-
reversible, reacts with an arginine residue at the NADP binding site, no inactivation with methyl viologen as electron acceptor
cyanide
-
50% inhibition at 0.01 mM, 100% inhibition at 10 mM
EDTA
-
50% inhibition at 25 mM, 100% inhibition at 100 mM
FeSO4
slight inhibition at 1 mM
hypophosphite
-
competitive inhibitor
hypophosphite
-
inhibition removed by formate
O2
-
-
Sodium azide
complete inhibition at 1 mM
Sodium azide
complete inhibition at 1 mM
additional information
ZnCl2 (1 mM), 10 mM of Mg2SO4, dithiothreitol, mercaptoethanol and phenylmethylsulfonyl fluoride do not affect enzyme activity
-
additional information
-
enzyme is rapidly inactivated by oxygen: 93% loss of activity within 2 min
-
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2.35
reduced methyl viologen
-
-
0.083
formate
-
-
0.083
formate
-
cosubstrate methyl viologen
0.23
formate
-
cosubstrate NADP+
0.277
formate
-
cosubstrate NADP+
2 - 3
formate
-
mutant D221A, at pH 7.0 and 22°C
40
formate
-
mutant D221G, at pH 7.0 and 22°C
41
formate
-
mutant D221S, at pH 7.0 and 22°C
46
formate
-
mutant D221Q, at pH 7.0 and 22°C
55.5
formate
wild type enzyme, in 1 M potassium phosphate buffer (pH 7.0), at 30°C
62
formate
-
mutant D221G/C255V, at pH 7.0 and 22°C
63
formate
-
at pH 7.5 and 30°C
69
formate
-
mutant C145S/D221G/C255V, at pH 7.0 and 22°C
80
formate
with NAD+ as cosubstrate, at pH 7.0 and 30°C
96
formate
-
at pH 7.5 and 30°C
120
formate
-
at pH 7.5 and 30°C
127
formate
-
mutant A198G/D221Q, at pH 7.0 and 22°C
150
formate
-
at pH 7.5 and 30°C
200
formate
with NADP+ as cosubstrate, at pH 7.0 and 30°C
0.06
NAD+
mutant enzyme Q223E, in 1 M potassium phosphate buffer (pH 7.0), at 30°C
1.43
NAD+
wild type enzyme, in 1 M potassium phosphate buffer (pH 7.0), at 30°C
6.5
NAD+
at pH 7.0 and 30°C
0.084
NADP+
-
mutant C145S/D221Q/C255V, at pH 7.0 and 22°C
0.147
NADP+
-
mutant C145S/A198G/D221Q/C255V, at pH 7.0 and 22°C
0.16
NADP+
wild type enzyme, in 1 M potassium phosphate buffer (pH 7.0), at 30°C
0.18
NADP+
-
at pH 7.5 and 30°C
0.24
NADP+
-
mutant D221G/C255V, at pH 7.0 and 22°C
0.27
NADP+
-
mutant A198G/D221Q, at pH 7.0 and 22°C
0.31
NADP+
-
mutant D221G, at pH 7.0 and 22°C
0.35
NADP+
-
at pH 7.5 and 30°C
0.37
NADP+
-
mutant D221A, at pH 7.0 and 22°C
0.39
NADP+
-
mutant D221Q, at pH 7.0 and 22°C
0.43
NADP+
-
mutant D221S, at pH 7.0 and 22°C
0.57
NADP+
-
mutant C145S/D221G/C255V, at pH 7.0 and 22°C
0.62
NADP+
-
at pH 7.5 and 30°C
0.83
NADP+
mutant enzyme Q223E, in 1 M potassium phosphate buffer (pH 7.0), at 30°C
0.85
NADP+
at pH 7.0 and 30°C
0.91
NADP+
-
at pH 7.5 and 30°C
0.92
NADP+
-
mutant C145S/D221A/C255V, at pH 7.0 and 22°C
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1.25
NAD+
mutant enzyme Q223E, in 1 M potassium phosphate buffer (pH 7.0), at 30°C
1.66
NAD+
wild type enzyme, in 1 M potassium phosphate buffer (pH 7.0), at 30°C
5.77
NAD+
at pH 7.0 and 30°C
0.13
NADP+
mutant enzyme Q223E, in 1 M potassium phosphate buffer (pH 7.0), at 30°C
0.52
NADP+
-
mutant D221G, at pH 7.0 and 22°C
0.55
NADP+
-
mutant D221S, at pH 7.0 and 22°C
0.62
NADP+
-
mutant D221G/C255V, at pH 7.0 and 22°C
0.79
NADP+
-
mutant A198G/D221Q, at pH 7.0 and 22°C
1.04
NADP+
-
mutant D221Q, at pH 7.0 and 22°C
1.05
NADP+
-
mutant D221A, at pH 7.0 and 22°C
1.5
NADP+
-
mutant C145S/D221Q/C255V, at pH 7.0 and 22°C
1.64
NADP+
-
mutant C145S/D221G/C255V, at pH 7.0 and 22°C
3.08
NADP+
-
mutant C145S/A198G/D221Q/C255V, at pH 7.0 and 22°C
3.96
NADP+
at pH 7.0 and 30°C
4.75
NADP+
wild type enzyme, in 1 M potassium phosphate buffer (pH 7.0), at 30°C
7.89
NADP+
-
mutant C145S/D221A/C255V, at pH 7.0 and 22°C
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1.16
NAD+
wild type enzyme, in 1 M potassium phosphate buffer (pH 7.0), at 30°C
20
NAD+
mutant enzyme Q223E, in 1 M potassium phosphate buffer (pH 7.0), at 30°C
0.16
NADP+
mutant enzyme Q223E, in 1 M potassium phosphate buffer (pH 7.0), at 30°C
1.29
NADP+
-
mutant D221S, at pH 7.0 and 22°C
1.69
NADP+
-
mutant D221G, at pH 7.0 and 22°C
2.58
NADP+
-
mutant D221G/C255V, at pH 7.0 and 22°C
2.67
NADP+
-
mutant D221Q, at pH 7.0 and 22°C
2.83
NADP+
-
mutant D221A, at pH 7.0 and 22°C
2.88
NADP+
-
mutant C145S/D221G/C255V, at pH 7.0 and 22°C
2.94
NADP+
-
mutant A198G/D221Q, at pH 7.0 and 22°C
8.58
NADP+
-
mutant C145S/D221A/C255V, at pH 7.0 and 22°C
17.9
NADP+
-
mutant C145S/D221Q/C255V, at pH 7.0 and 22°C
21
NADP+
-
mutant C145S/A198G/D221Q/C255V, at pH 7.0 and 22°C
30
NADP+
wild type enzyme, in 1 M potassium phosphate buffer (pH 7.0), at 30°C
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A198G/D221Q
-
the mutant has the highest catalytic efficiency with NADP+
C145S/A198G/D221Q/C255V
-
the mutant has high catalytic efficiency with NADP+
C145S/D221A/C255V
-
the mutant has high catalytic efficiency with NADP+
C145S/D221Q/C255V
-
the mutant shows the highest specific activity for a NADP+-accepting formate dehydrogenase
D221A
-
the mutant has high catalytic efficiency with NADP+
D221G
-
the mutant has high catalytic efficiency with NADP+
D221Q
-
the mutant has high catalytic efficiency with NADP+
D221S
-
the mutant has high catalytic efficiency with NADP+
Q223E
the mutated enzyme shows an 18fold increment in catalytic efficiency with NAD+ with a concomitant 185fold reduction in the efficiency with NADP+, drastically shifting the cofactor preference from NADP+ to NAD+
Q223E
-
the mutated enzyme shows an 18fold increment in catalytic efficiency with NAD+ with a concomitant 185fold reduction in the efficiency with NADP+, drastically shifting the cofactor preference from NADP+ to NAD+
-
additional information
-
mutant recombinant form of a NAD+ dependent formate dehydrogenase, EC 1.2.1.2 is NADP+ dependent
additional information
-
mutant recombinant form of a NAD+ dependent formate dehydrogenase, EC 1.2.1.2 is NADP+ dependent
additional information
-
mutant recombinant form of a NAD+ dependent formate dehydrogenase, EC 1.2.1.2 is NADP+ dependent
additional information
-
large scale production of mutant FDH expression in Escherichia coli
additional information
-
activity of the NADP+-specific mutant FDH is 60% of the activity of wild-type NAD+-dependent FDH
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Ljungdahl, L.G.; Andreesen, J.R.
Formate dehydrogenase, a selenium-tungsten enzyme from Clostridium thermoaceticum
Methods Enzymol.
53
360-372
1970
Moorella thermoacetica
brenda
Wetherbee, P.J.; Thornton, L.S.; Durfor, C.N.
The reversible inactivation of the Clostridium thermoaceticum formate dehydrogenase by butanedione
Biochim. Biophys. Acta
870
12-19
1986
Moorella thermoacetica
-
brenda
Yamamoto, I.; Saiki, T.; Liu, S.M.; Ljungdahl, L.G.
Purification and properties of NADP-dependent formate dehydrogenase from Clostridium thermoaceticum, a tungsten-selenium-iron protein
J. Biol. Chem.
258
1826-1832
1983
Moorella thermoacetica
brenda
Durfor, C.N.; Wetherbee, P.J.
Characterization and spectroscopic properties of reduced Mo and W formate dehydrogenase from C. thermoaceticum
Biochem. Biophys. Res. Commun.
115
61-67
1983
Moorella thermoacetica
brenda
Ljungdahl, L.G.; Andreesen, J.R.
Tungsten, a component of active formate dehydrogenase from Clostridium thermoacetium
FEBS Lett.
54
279-282
1975
Moorella thermoacetica
brenda
Andreesen, J.R.; Ljungdahl, L.G.
Formate dehydrogenase of Clostridium thermoaceticum: incorporation of selenium-75, and the effects of selenite, molybdate, and tungstate on the enzyme
J. Bacteriol.
116
867-873
1973
Moorella thermoacetica
brenda
Andreesen, J.R.; Ljungdahl, L.G.
Nicotinamide adenine dinucleotide phosphate-dependent formate dehydrogenase from Clostridium thermoaceticum: purification and properties
J. Bacteriol.
120
6-14
1974
Moorella thermoacetica
brenda
Schulz, M.; Bayer, M.; White, H.; Guenther, H.; Simon, H.
Application of high enzyme activities present in Clostridium thermoaceticum for the efficient regeneration of NADPH, NADP+, NADH and NAD+
Biocatalysis
10
25-36
1994
Moorella thermoacetica
-
brenda
Klyushnichenko, V.; Tishkov, V.; Kula, M.R.
Rapid SDS-Gel capillary electrophoresis for the analysis of recombinant NADP(+)-dependent formate dehydrogenase during expression in Escherichia coli cells and its purification
J. Biotechnol.
58
187-195
1997
Pseudomonas sp.
brenda
Seelbach, K.; Riebel, B.; Hummel, W.; Kula, M.R.; Tishkov, V.I.; Egorov, A.M.; Wandrey, C.
A novel, efficient regenerating method of NADPH using a new formate dehydrogenase
Tetrahedron Lett.
37
1377-1380
1996
Pseudomonas sp.
-
brenda
Tishkov, V.I.; Galkin, A.G.; Fedorchuk, V.V.; Savitsky, P.A.; Rojkova, A.M.; Gieren, H.; Kula, M.R.
Pilot scale production and isolation of recombinant NAD+- and NADP+-specific formate dehydrogenases
Biotechnol. Bioeng.
64
187-193
1999
Pseudomonas sp.
brenda
Hatrongjit, R.; Packdibamrung, K.
A novel NADP+-dependent formate dehydrogenase from Burkholderia stabilis 15516: Screening, purification and characterization
Enzyme Microb. Technol.
46
557-561
2010
Burkholderia stabilis (B5A8W5), Burkholderia stabilis 15516 (B5A8W5)
-
brenda
Hoelsch, K.; Suehrer, I.; Heusel, M.; Weuster-Botz, D.
Engineering of formate dehydrogenase: synergistic effect of mutations affecting cofactor specificity and chemical stability
Appl. Microbiol. Biotechnol.
97
2473-2481
2013
Mycolicibacterium vaccae, Mycolicibacterium vaccae N10
brenda
Fogal, S.; Beneventi, E.; Cendron, L.; Bergantino, E.
Structural basis for double cofactor specificity in a new formate dehydrogenase from the acidobacterium Granulicella mallensis MP5ACTX8
Appl. Microbiol. Biotechnol.
99
9541-9554
2015
Granulicella mallensis (G8NVB5), Granulicella mallensis MP5ACTX8 (G8NVB5)
brenda
Ihara, M.; Kawano, Y.; Urano, M.; Okabe, A.
Light driven CO2 fixation by using cyanobacterial photosystem I and NADPH-dependent formate dehydrogenase
PLoS ONE
8
e71581
2013
Arabidopsis thaliana, [Candida] boidinii, Pseudomonas sp., Solanum tuberosum, Thiobacillus sp., Thiobacillus sp. KNK65MA
brenda