Information on EC 1.2.1.2 - formate dehydrogenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
1.2.1.2
-
RECOMMENDED NAME
GeneOntology No.
formate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
formate + NAD+ = CO2 + NADH
show the reaction diagram
ordered bi-bi mechanism, NAD+ is the first substrate and NADH is the last product
-
formate + NAD+ = CO2 + NADH
show the reaction diagram
ordered kinetic mechanism with NAD+ adding before formate
-
formate + NAD+ = CO2 + NADH
show the reaction diagram
sequential mechanism
-
formate + NAD+ = CO2 + NADH
show the reaction diagram
sequential ordered bi-bi mechanism
Candida methanolica
-
formate + NAD+ = CO2 + NADH
show the reaction diagram
ordered mechanism
-
formate + NAD+ = CO2 + NADH
show the reaction diagram
hydride-transfer step is rate-limiting
-
formate + NAD+ = CO2 + NADH
show the reaction diagram
ordered BiBi mechanism with NAD+ and NADH being the first substrate and the second product, resp.
-
formate + NAD+ = CO2 + NADH
show the reaction diagram
reaction mechanism: step I, formate binds directly to Mo, displacing Se-Cys140. Step II, the alpha-proton from formate may be transferred to the nearby His141 that acts as general base. Alternatively, step II may involve a selenium-carboxylated intermediate. Step III, electrons from MoIV are transferred via the 4Fe-4S center to an external electron acceptor and the catalytic cycle is completed
P07658
formate + NAD+ = CO2 + NADH
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
formate oxidation to CO2
-
Glyoxylate and dicarboxylate metabolism
-
Metabolic pathways
-
Methane metabolism
-
Microbial metabolism in diverse environments
-
oxalate degradation III
-
purine nucleobases degradation I (anaerobic)
-
purine nucleobases degradation II (anaerobic)
-
SYSTEMATIC NAME
IUBMB Comments
formate:NAD+ oxidoreductase
The enzyme from most aerobic organisms is devoid of redox-active centres but that from the proteobacterium Methylosinus trichosporium contains iron-sulfur centres, flavin and a molybdenum centre [3]. Together with EC 1.12.1.2 hydrogen dehydrogenase, forms a system previously known as formate hydrogenlyase.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dehydrogenase, formate
-
-
-
-
FDB2
A9ZNT9
isozyme
FDB2
Ceriporiopsis subvermispora CS105
A9ZNT9
isozyme
-
FDH
-
-
-
-
FDH
D6CJK0
-
FDH
D6CJK0
-
-
FDH
Q00498
-
FDH
O08375
-
FDH
Moraxella sp. C-1
O08375
-
-
FDH
Mycobacterium vaccae N10
-
-
-
FDH
E7RAN7
-
FDH
Ogataea angusta DL-1
E7RAN7
-
-
FDH I
-
-
-
-
FDH II
-
-
-
-
Fdh-H
-
isozyme
Fdh-N
-
isozyme
FDH-O
-
isozyme
FDH1
O13437
-
FDH1
A9ZNT8
isozyme
FDH1
Ceriporiopsis subvermispora CS105
A9ZNT8
isozyme
-
FDH1
B6VPZ9
-
FDHH
Clostridium carboxidivorans P7T
E2IQB0
-
-
formate benzyl-viologen oxidoreductase
-
-
-
-
formate dehydrogenase
-
-
formate dehydrogenase
-
-
-
formate dehydrogenase (NAD)
-
-
-
-
formate dehydrogenase H
E2IQB0
-
formate dehydrogenase H
Clostridium carboxidivorans P7T
E2IQB0
-
-
formate-NAD oxidoreductase
-
-
-
-
formate:NAD oxidoreductase
-
-
-
-
formic acid dehydrogenase
-
-
-
-
MycFDH
Mycobacterium vaccae N10
-
-
-
N-FDH
-
-
-
-
NAD+-dependent formate dehydrogenase
D6CJK0
-
NAD+-dependent formate dehydrogenase
D6CJK0
-
-
NAD+-dependent formate dehydrogenase
-
-
NAD+-dependent formate dehydrogenase
O13437
-
NAD+-dependent formate dehydrogenase
-
-
NAD+-dependent formate dehydrogenase
Q00498
-
NAD+-dependent formate dehydrogenase
O08375
-
NAD+-dependent formate dehydrogenase
Moraxella sp. C-1
O08375
-
-
NAD+-dependent formate dehydrogenase
-
-
NAD+-dependent formate dehydrogenase
-
-
-
NAD-dependent formate dehydrogenase
-
-
-
-
NAD-dependent formate dehydrogenase
Q845T0
-
NAD-dependent formate dehydrogenase
Ancylobacter aquaticus KNK607M
Q845T0
-
-
NAD-dependent formate dehydrogenase
A9ZNT8, A9ZNT9
-
NAD-dependent formate dehydrogenase
Ceriporiopsis subvermispora CS105
A9ZNT8, A9ZNT9
-
-
NAD-formate dehydrogenase
-
-
-
-
NAD-linked formate dehydrogenase
-
-
-
-
NAD-specific formate dehydrogenase
-
-
PseFDH
-
-
PseFDH
-
-
-
tungsten-containing formate dehydrogenase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9028-85-7
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Achromobacter parvulus
-
-
-
Manually annotated by BRENDA team
strain KNK607M
SwissProt
Manually annotated by BRENDA team
Ancylobacter aquaticus KNK607M
strain KNK607M
SwissProt
Manually annotated by BRENDA team
comparison of thermal stability with enzymes from Pseudomonas sp. strain 101, Moraxella sp. C1, Candida boidinii, and Glycine max, all recombinant proteins, expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
Arthrobacter sp. KM 62
KM 62
-
-
Manually annotated by BRENDA team
comparison of thermal stability with enzymes from Pseudomonas sp. strain 101, Moraxella sp. C1, Arabidopsis thaliana, and Glycine max, all recombinant proteins, expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
expression in Escherichia coli
-
-
Manually annotated by BRENDA team
isolation of mutants with increased residual activity after entrapment in polyacrylamide gels
-
-
Manually annotated by BRENDA team
strain ATCC 18810
UniProt
Manually annotated by BRENDA team
strain ATCC 32195
-
-
Manually annotated by BRENDA team
Candida methanolica
-
-
-
Manually annotated by BRENDA team
Ceriporiopsis subvermispora CS105
strain CS105
UniProt
Manually annotated by BRENDA team
Clostridium carboxidivorans P7T
-
UniProt
Manually annotated by BRENDA team
strain OX 1
-
-
Manually annotated by BRENDA team
Cupriavidus oxalaticus OX
strain OX 1
-
-
Manually annotated by BRENDA team
isoform H
SwissProt
Manually annotated by BRENDA team
comparison of thermal stability with enzymes from Pseudomonas sp. strain 101, Moraxella sp. C1, Candida boidinii, and Arabidopsis thaliana, all recombinant proteins, expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
var Beeson
-
-
Manually annotated by BRENDA team
II J58/1
-
-
Manually annotated by BRENDA team
Hyphomicrobium sp. II J58/1
II J58/1
-
-
Manually annotated by BRENDA team
Kloeckera sp.
No. 2201
-
-
Manually annotated by BRENDA team
Kloeckera sp. 2201
No. 2201
-
-
Manually annotated by BRENDA team
NRRL Y-7556
-
-
Manually annotated by BRENDA team
Komagataella pastoris IFP 206
IFP 206
-
-
Manually annotated by BRENDA team
Komagataella pastoris NRRL Y-7556
NRRL Y-7556
-
-
Manually annotated by BRENDA team
alpha-subunit of Fdh1; strain AM1
SwissProt
Manually annotated by BRENDA team
alpha-subunit of Fdh2; strain AM1
SwissProt
Manually annotated by BRENDA team
alpha-subunit of Fdh3; strain AM1
SwissProt
Manually annotated by BRENDA team
beta-subunit of Fdh1; strain AM1
SwissProt
Manually annotated by BRENDA team
beta-subunit of Fdh2; strain AM1
SwissProt
Manually annotated by BRENDA team
beta-subunit of Fdh3; strain AM1
SwissProt
Manually annotated by BRENDA team
delta-subunit of Fdh2; strain AM1
SwissProt
Manually annotated by BRENDA team
gamma-subunit of Fdh2; strain AM1
Q84FW3
SwissProt
Manually annotated by BRENDA team
gamma-subunit of Fdh3; strain AM1
SwissProt
Manually annotated by BRENDA team
Methylobacterium sp. RXM
RXM
-
-
Manually annotated by BRENDA team
methylotrophic bacterium
strain 1
-
-
Manually annotated by BRENDA team
methylotrophic bacterium 1
strain 1
-
-
Manually annotated by BRENDA team
strain C-1
-
-
Manually annotated by BRENDA team
strain C1, comparison with enzymes from Pseudomonas sp. strain 101, Candida boidinii, Arabidopsis thaliana, and Glycine max, all recombinant proteins, expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
Moraxella sp. C-1
-
UniProt
Manually annotated by BRENDA team
Moraxella sp. C-1
strain C-1
-
-
Manually annotated by BRENDA team
Mycobacterium vaccae N10
-
-
-
Manually annotated by BRENDA team
Mycobacterium vaccae N10
N10
-
-
Manually annotated by BRENDA team
no activity in Enterobacter aerogenes
-
-
-
Manually annotated by BRENDA team
formerly Ogataea parapolymorpha
E7RAN7
UniProt
Manually annotated by BRENDA team
Ogataea angusta DL-1
formerly Ogataea parapolymorpha
E7RAN7
UniProt
Manually annotated by BRENDA team
strain 12-A
-
-
Manually annotated by BRENDA team
Pseudomonas methylica
-
-
-
Manually annotated by BRENDA team
101 BKM B-1545D
-
-
Manually annotated by BRENDA team
101, strain VKM B1545D
-
-
Manually annotated by BRENDA team
3A2; 3ab; AM1; M27
-
-
Manually annotated by BRENDA team
; strain 101
-
-
Manually annotated by BRENDA team
strain 101
SwissProt
Manually annotated by BRENDA team
strain 101, comparison with enzymes from Moraxella sp. C1, Candida boidinii, Arabidopsis thaliana, and Glycine max, all recombinant proteins, expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
strain 101
SwissProt
Manually annotated by BRENDA team
strain 101, comparison with enzymes from Moraxella sp. C1, Candida boidinii, Arabidopsis thaliana, and Glycine max, all recombinant proteins, expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
Pseudomonas sp. 3A2
3A2
-
-
Manually annotated by BRENDA team
Pseudomonas sp. 3ab
3ab
-
-
Manually annotated by BRENDA team
Pseudomonas sp. AM1
AM1
-
-
Manually annotated by BRENDA team
strain KNK65MA
-
-
Manually annotated by BRENDA team
strain KNK65MA
-
-
Manually annotated by BRENDA team
Torulopsis candida
NRRL Y-11419
-
-
Manually annotated by BRENDA team
Torulopsis candida NRRL Y-11419
NRRL Y-11419
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-(formyloxy)butyl acetate + NAD+
?
show the reaction diagram
-
59% conversion
-
-
?
butyl formate + NAD+
?
show the reaction diagram
-
41% conversion
-
-
?
CO2 + NADH
formate + NAD+
show the reaction diagram
-
-
-
-
?
CO2 + NADH
formate + NAD+
show the reaction diagram
-, E2IQB0
-
-
-
r
CO2 + NADH
formate + NAD+
show the reaction diagram
Mycobacterium vaccae N10
-
-
-
-
?
CO2 + NADH
formate + NAD+
show the reaction diagram
Clostridium carboxidivorans P7T
E2IQB0
-
-
-
r
ethyl formate + NAD+
?
show the reaction diagram
-
-
-
-
?
ethyl formate + NAD+
?
show the reaction diagram
-
26% conversion
-
-
?
formate + 2,6-dichloroindophenol
CO2 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
?
formate + 2,6-dichloroindophenol
CO2 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
?
formate + 2,6-dichloroindophenol
CO2 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
54% of the activity with NAD+
-
-
?
formate + 2,6-dichloroindophenol
CO2 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
33% of the activity with NAD+
-
-
?
formate + 2,6-dichlorophenolindophenol
CO2 + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
-
formate + 3-pyridinecarboxaldehyde-NAD+
CO2 + 3-pyridinecarboxaldehyde-NADH
show the reaction diagram
-
-
-
-
?
formate + benzyl viologen
CO2 + reduced benzyl viologen
show the reaction diagram
-
-
-
-
?
formate + benzyl viologen
CO2 + reduced benzyl viologen
show the reaction diagram
-
-
-
-
?
formate + benzyl viologen
CO2 + reduced benzyl viologen
show the reaction diagram
-
-
-
-
?
formate + benzyl viologen
CO2 + reduced benzyl viologen
show the reaction diagram
-
113% of the activity with NAD+
-
-
?
formate + benzyl viologen
CO2 + reduced benzyl viologen + H+
show the reaction diagram
-
-
-
-
?
formate + cytochrome c
CO2 + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
formate + dextran-NAD+
CO2 + dextran-NADH
show the reaction diagram
-
enzyme immobilized on glyoxyl agarose, 60% of the activity with NAD+
-
-
?
formate + FAD
CO2 + FADH2
show the reaction diagram
-
-
-
-
?
formate + ferricyanide
CO2 + ferrocyanide
show the reaction diagram
-
-
-
-
?
formate + ferricyanide
CO2 + ferrocyanide
show the reaction diagram
-
-
-
-
?
formate + ferricyanide
CO2 + ferrocyanide
show the reaction diagram
-
10% of the activity with NAD+
-
-
?
formate + FMN
CO2 + FMNH2
show the reaction diagram
-
-
-
-
?
formate + FMN
CO2 + FMNH2
show the reaction diagram
-
-
-
-
-
formate + methyl viologen
CO2 + reduced methyl viologen
show the reaction diagram
-
-
-
-
?
formate + methyl viologen
CO2 + reduced methyl viologen
show the reaction diagram
-
74% of the activity with NAD+
-
-
?
formate + methylene blue
CO2 + reduced methylene blue
show the reaction diagram
-
-
-
-
?
formate + methylene blue
CO2 + reduced methylene blue
show the reaction diagram
-
119% of the activity with NAD+
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
ir
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
r
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Torulopsis candida
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
-
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
r
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Kloeckera sp.
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
ir
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Pseudomonas methylica
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
methylotrophic bacterium
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Candida methanolica
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Achromobacter parvulus
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Q84FW0, Q84FW1, Q84FW2, Q84FW3, Q84FZ6, Q84FZ7, Q84FZ8, Q8KTI7, Q8KTI8
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-, Q845T0
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
O13437
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
E7RAN7
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Q00498
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
O13437
high activity
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
equilibrium strongly favors dehydrogenation of formate
-
-
r
formate + NAD+
CO2 + NADH
show the reaction diagram
-
enzyme catalyzes formate oxidation about 30times faster than the CO2 reduction
-
-
r
formate + NAD+
CO2 + NADH
show the reaction diagram
-
enzyme provides NADH for synthesis
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
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
show the reaction diagram
Kloeckera sp.
-
last step of methanol oxidation system
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Candida methanolica
-
one of the key enzymes in the assimilation of C1 compounds, such as methanol
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
last enzyme of the dissimilatory pathway of the methanol metabolism
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
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
show the reaction diagram
Q84FW0, Q84FW1, Q84FW2, Q84FW3, Q84FZ6, Q84FZ7, Q84FZ8, Q8KTI7, Q8KTI8
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
show the reaction diagram
-
role of formate dehydrogenase in detoxification of exogenous formate
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Q08911
wild-type enzyme shows no activity with NADP+, mutant enzyme D196A/Y197R shows higher activity with NADP+ than with NAD+
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
O13437
FDH is highly specific to NAD+ and virtually fails to catalyze the reaction with NADP+
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
B6VPZ9, -
FDH1 exhibits absolute specificity for formate and NAD+
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-, D6CJK0
the enzyme shows strict substrate specificity for formate
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Hyphomicrobium sp. II J58/1
-
-, induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Komagataella pastoris NRRL Y-7556
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Kloeckera sp. 2201
-
-, last step of methanol oxidation system
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Pseudomonas sp. 3A2
-
-, induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Mycobacterium vaccae N10
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Komagataella pastoris IFP 206
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Ancylobacter aquaticus KNK607M
Q845T0
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Cupriavidus oxalaticus OX
-
equilibrium strongly favors dehydrogenation of formate
-
-
r
formate + NAD+
CO2 + NADH
show the reaction diagram
Methylobacterium sp. RXM
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Arthrobacter sp. KM 62
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Pseudomonas sp. AM1
-
-, induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Pseudomonas sp. 3ab
-
-, induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Torulopsis candida NRRL Y-11419
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Moraxella sp. C-1
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
methylotrophic bacterium 1
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
D6CJK0
the enzyme shows strict substrate specificity for formate
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Ogataea angusta DL-1
E7RAN7
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-, induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH + H+
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
show the reaction diagram
P33160
-
-
-
ir
formate + NAD+
CO2 + NADH + H+
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
show the reaction diagram
O13437
-
-
-
?
formate + NAD+
CO2 + NADH + H+
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
show the reaction diagram
O08375
-
-
-
?
formate + NAD+
CO2 + NADH + H+
show the reaction diagram
A9ZNT8, A9ZNT9, -
100% specificity
-
-
?
formate + NAD+
CO2 + NADH + H+
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH + H+
show the reaction diagram
Moraxella sp. C-1
O08375
-
-
-
?
formate + NAD+
CO2 + NADH + H+
show the reaction diagram
Ceriporiopsis subvermispora CS105
A9ZNT8, A9ZNT9
100% specificity
-
-
?
formate + NADP+
CO2 + NADH
show the reaction diagram
-
4% of the activity with NAD+
-
-
?
formate + NADP+
CO2 + NADH
show the reaction diagram
-, Q845T0
activity with NADP+ is 2.4% of the activity with NAD+
-
-
?
formate + NADP+
CO2 + NADH
show the reaction diagram
-
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 + NADH
show the reaction diagram
Ancylobacter aquaticus KNK607M
Q845T0
activity with NADP+ is 2.4% of the activity with NAD+
-
-
?
formate + NADP+
CO2 + NADH
show the reaction diagram
-
4% of the activity with NAD+
-
-
?
formate + NADP+
CO2 + NADPH
show the reaction diagram
-, D6CJK0
-
-
-
?
formate + NADP+
CO2 + NADPH
show the reaction diagram
Q08911
wild-type enzyme shows no activity, mutant enzyme D196A/Y197R shows higher activity with NADP+ than with NAD+
-
-
?
formate + NADP+
CO2 + NADPH
show the reaction diagram
O13437
FDH is highly specific to NAD+ and virtually fails to catalyze the reaction with NADP+
-
-
?
formate + NADP+
CO2 + NADPH
show the reaction diagram
B6VPZ9, -
FDH1 uses NADP+ with low specificity compared to NAD+
-
-
?
formate + NADP+
CO2 + NADPH
show the reaction diagram
Mycobacterium vaccae, Mycobacterium vaccae N10
-
NADP+ is substrate for several mutant enzymes
-
-
?
formate + NADP+
CO2 + NADPH
show the reaction diagram
D6CJK0
-
-
-
?
formate + NADP+
CO2 + NADPH + H+
show the reaction diagram
O13437
low activity, the wild type enzyme virtually fails to catalyze the reaction with NADP+
-
-
?
formate + nitrobluetetrazolium
CO2 + reduced nitrobluetetrazolium
show the reaction diagram
-
-
-
-
?
formate + nitrobluetetrazolium
CO2 + reduced nitrobluetetrazolium
show the reaction diagram
-
54% of the activity with NAD+
-
-
?
formate + O2
CO2 + H2O2
show the reaction diagram
-
-
-
?
formate + phenazine methosulfate
CO2 + reduced phenazine methosulfate
show the reaction diagram
-
-
-
-
?
formate + phenazine methosulfate
CO2 + reduced phenazine methosulfate
show the reaction diagram
-
no activity
-
-
-
formate + riboflavin
CO2 + reduced riboflavin
show the reaction diagram
-
-
-
-
?
glyoxylate + NAD+
? + NADH
show the reaction diagram
-
wild-type, low activity towards glyoxylate
-
-
?
NADH + 2,6-dichloroindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
?
NADH + 2,6-dichloroindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
?
NADH + benzyl viologen
NAD+ + reduced benzyl viologen
show the reaction diagram
-
-
-
-
-
NADH + ferricyanide
NAD+ + ferrocyanide
show the reaction diagram
-
-
-
-
-
NADH + ferricyanide
NAD+ + ferrocyanide
show the reaction diagram
-
-
-
-
-
phenyl formate + NAD+
?
show the reaction diagram
-
86% conversion
-
-
?
propyl formate + NAD+
?
show the reaction diagram
-
39% conversion
-
-
?
S-formylglutathione + NAD+
?
show the reaction diagram
-
about 40fold lower Km-value than with formate
-
-
?
S-formylglutathione + NAD+
?
show the reaction diagram
-
lower KM-value than for formate but maximal activity is only 5.5% of that of formate
-
-
?
S-formylthioglycolate + NAD+
?
show the reaction diagram
-
-
-
-
?
methyl formate + NAD+
?
show the reaction diagram
-
23% conversion
-
-
?
additional information
?
-
-
S-formylglutathione rather than free formate is an intermediate in oxidation of methanol by yeast
-
-
-
additional information
?
-
-
possible role of enzyme in oxalate metabolism, no substrate: acetate, pyruvate, malate, oxalate, succinate, methanol, isocitrate, fumarate
-
-
-
additional information
?
-
A9ZNT8, A9ZNT9, -
no activity with malate, lactate, glycolate, pyruvate, and glyoxylate
-
-
-
additional information
?
-
-, D6CJK0
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
?
-
D6CJK0
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
?
-
Ceriporiopsis subvermispora CS105
A9ZNT8, A9ZNT9
no activity with malate, lactate, glycolate, pyruvate, and glyoxylate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
CO2 + NADH
formate + NAD+
show the reaction diagram
-
-
-
-
?
CO2 + NADH
formate + NAD+
show the reaction diagram
-, E2IQB0
-
-
-
r
CO2 + NADH
formate + NAD+
show the reaction diagram
Mycobacterium vaccae N10
-
-
-
-
?
CO2 + NADH
formate + NAD+
show the reaction diagram
Clostridium carboxidivorans P7T
E2IQB0
-
-
-
r
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
ir
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
r
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
E7RAN7
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Q00498
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
enzyme provides NADH for synthesis
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
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
show the reaction diagram
Kloeckera sp.
-
last step of methanol oxidation system
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Candida methanolica
-
one of the key enzymes in the assimilation of C1 compounds, such as methanol
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
last enzyme of the dissimilatory pathway of the methanol metabolism
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
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
show the reaction diagram
Q84FW0, Q84FW1, Q84FW2, Q84FW3, Q84FZ6, Q84FZ7, Q84FZ8, Q8KTI7, Q8KTI8
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
show the reaction diagram
-
role of formate dehydrogenase in detoxification of exogenous formate
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-, D6CJK0
the enzyme shows strict substrate specificity for formate
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Hyphomicrobium sp. II J58/1
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Kloeckera sp. 2201
-
last step of methanol oxidation system
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Pseudomonas sp. 3A2
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Mycobacterium vaccae N10
-
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Pseudomonas sp. AM1, Pseudomonas sp. 3ab
-
induced by methanol and formate
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
D6CJK0
the enzyme shows strict substrate specificity for formate
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
Ogataea angusta DL-1
E7RAN7
-
-
-
?
formate + NAD+
CO2 + NADH
show the reaction diagram
-
induced by methanol and formate
-
-
?
formate + NADP+
CO2 + NADPH
show the reaction diagram
-, D6CJK0
-
-
-
?
formate + NADP+
CO2 + NADPH
show the reaction diagram
Mycobacterium vaccae, Mycobacterium vaccae N10
-
NADP+ is substrate for several mutant enzymes
-
-
?
formate + NADP+
CO2 + NADPH
show the reaction diagram
D6CJK0
-
-
-
?
additional information
?
-
-
S-formylglutathione rather than free formate is an intermediate in oxidation of methanol by yeast
-
-
-
additional information
?
-
-
possible role of enzyme in oxalate metabolism
-
-
-
additional information
?
-
-, D6CJK0
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
?
-
D6CJK0
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
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
FMN
-
enzyme contains at least 1 mol of FMN per mol of enzyme
FMN
-
formate dehydrogenase I contains 1 mol of FMN per mol of enzyme, formate dehydrogenase II contains 2 mol of FMN per mol of enzyme
FMN
-
0.9 mol of FMN per mol of enzyme
FMN
-
contains 0.6 mol of noncovalently bound FMN per mol of enzyme. The beta-subunit contains a putative binding motif for NAD+
molybdopterin
-
the alpha-subunit contains a putative binding motif for the molybdopterin cofactor
NAD+
Hyphomicrobium sp., Pseudomonas methylica
-
-
NAD+
methylotrophic bacterium
-
-
NAD+
Candida methanolica
-
-
NAD+
Achromobacter parvulus
-
-
NAD+
Torulopsis candida
-
-
NAD+
-
enzyme binds one NAD+ molecule per subunit
NAD+
Kloeckera sp.
-
-
NAD+
Q08911
wild-type enzyme shows no activity with NADP+, mutant enzyme D196A/Y197R shows higher activity with NADP+ than with NAD+
NAD+
-
the beta-subunit contains a putative binding motif for NAD+. No activity with NADP+
NAD+
-
no activity with NADP+
NAD+
-
specific for NAD+ as electron acceptor
NAD+
-
highly specific to NAD+; most efficient cofactor
NAD+
A9ZNT8, A9ZNT9, -
;
NAD+
B6VPZ9, -
FDH1 shows activity using NAD+ or NADP+, FDH1 is highly specific to NAD+ compared to NADP+
NAD+
-, D6CJK0
preferred cofactor
NADP+
-
no reaction is catalyzed with wild-type enzyme, activity is detected with mutant enzyme D195S. The ratio of the catalytic efficiencies for NAD+ versus NADP+ for the mutant protein is 40:1 in favor of NAD+
NADP+
Q08911
wild-type enzyme shows no activity with NADP+, mutant enzyme D196A/Y197R shows higher activity with NADP+ than with NAD+
NADP+
-
4.2% of the activity with NAD+
NADP+
-, Q845T0
activity is 2.4% of the activity with NAD+
NADP+
-
low activity compared to NADP+; the wild type enzyme virtually fails to use NADP+ as a cofacor
NADP+
B6VPZ9, -
FDH1 shows activity using NAD+ or NADP+, FDH1 is highly specific to NAD+ compared to NADP+
NADP+
-, D6CJK0
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
E7RAN7
1 mM Ca2+ improves the enzyme activity by 77%
Ca2+
-, D6CJK0
the enzyme activity is increased 13.8% over the control by 1 mM Ca2+
Co2+
E7RAN7
1 mM Co2+ improves the enzyme activity by 46%
Co2+
-, D6CJK0
the enzyme activity is increased 9.8% over the control by 1 mM Co2+
Fe
-
contains 11-18 gatoms of non-heme iron per mol of enzyme
Fe
-
5-8 mol of iron per mol of enzyme
Fe
-
formate dehydrogenase I contains 18-25 mol of iron per mol of enzyme. Formate dehydrogenase II contains 6-10 mol of iron per mol of enzyme
Fe
-
two distinct [Fe-S] centres
Fe2+
-, D6CJK0
the enzyme activity is increased 49.4% over the control by 1 mM Fe2+
Iron
-
contains 5 mol nonheme iron per mol of enzyme. The beta-subunit contains a putative binding motif for an iron-sulfur cluster. The alpha-subunit contains at least one iron-sulfur cluster
K+
-, D6CJK0
the enzyme activity is increased 6.7% over the control by 1 mM K+
Li+
-, D6CJK0
the enzyme activity is increased 13.8% over the control by 1 mM Li+
Mg2+
-, D6CJK0
the enzyme activity is increased 7.6% over the control by 1 mM Mg2+
Mn2+
-, D6CJK0
the enzyme activity is increased 29.8% over the control by 1 mM Mn2+
Molybdenum
-
0.64 gatom per mol of enzyme. The enzyme contains molybdopterin guanine dinucleotide
Tungsten
-
contains 1.8 mol tungsten per mol of enzyme
Molybdenum
P07658
molybdoenzyme
additional information
A9ZNT8, A9ZNT9, -
no divalent metal cation is needed as a cofactor for enzyme activity; no divalent metal cation is needed as a cofactor for enzyme activity
additional information
E7RAN7
Mn2+, Ba2+, and Mg2+ do not significantly change the enzyme activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
1-chloro-2-oxopropane
-
20 mM, pH 6.5, 30C, 5 h, 76% loss of activity
1-methyl-3-methylimidazolium dimethylphosphate
-
adding more than 40% (v/v) of 1-methyl-3-methylimidazolium dimethylphosphate inactivates formate dehydrogenase. In the presence of 30% (v/v) 1-methyl-3-methylimidazolium dimethylphosphate, the catalytic efficiency of the wild type enzyme is reduced by 2.8fold
-
2,3-Butanedione
Achromobacter parvulus
-
modification of 12 Arg residues per molecule results in complete inactivation. NAD+ protects
2-chloro-1-(3-pyridyl)-ethanone
-
20 mM, pH 6.5, 30C, 5 h, 10% loss of activity
4-hydroxybutyl acetate
-
IC50 of 15.6 vol%
-
5,5'-dithio-bis(2-nitrobenzoic acid)
-
-
5-Nitro-8-hydroxyquinoline
-
-
ADP
-
inhibition is greater at acidic pH than at neutral pH
ADP
A9ZNT8, A9ZNT9, -
86% inhibition at 50 mM; 90% inhibition at 50 mM
ADP-beta-D-ribose
-
competitive with NAD+, mixed-type with formate
AgNO3
-
0.01 mM
AgNO3
-
1 mM; 80% inhibition
ATP
-
inhibition is greater at acidic pH than at neutral pH
ATP
A9ZNT8, A9ZNT9, -
45% inhibition at 50 mM; 56% inhibition at 50 mM
azide
-
0.9 mM, 50% inhibition
azide
-
uncompetitive with NAD+, competitive with formate
azide
-
potent inhibitor
azide
O08375
-
azide
-
a transition-state analogue inhibitor of FDH
benzaldehyde
Candida methanolica
-
slight inhibition
bicarbonate
-
mixed-type inhibition of NAD+ and formate
Cd2+
Candida methanolica
-
CdCl2
Cd2+
-
1 mM CdSO4, 39% inhibition
Cd2+
-, D6CJK0
complete inhibition at 1 mM
CN-
methylotrophic bacterium
-
-
CN-
-
1 mM KCN, complete inhibition
CN-
-
0.1 mM NaCN, 90% inhibition
CN-
Candida methanolica
-
NaCN
CN-
-
1 mM KCN, 50% inhibition
CN-
Kloeckera sp.
-
-
Cu2+
-
1 mM CuCl2, 81% inhibition
Cu2+
Kloeckera sp.
-
-
Cu2+
-
0.2 mM, 13.6% inhibition
Cu2+
-, Q845T0
1 mM, 37% inhibition
Cu2+
A9ZNT8, A9ZNT9, -
82 inhibition at 1 mM; complete inhibition at 1 mM
Cu2+
E7RAN7
1 mM Cu2+ inhibits the enzyme activity by 79%
Cu2+
-, D6CJK0
94.2% inhibition at 1 mM
Cycloserine
-
weak
dimethylimidazolium dimethyl phosphate
-
FDh is inactivated and unstable in the presence of high concentration (above 50%) of the water soluble dimethylimidazolium dimethyl phosphate ionic liquid
-
Dithionitrobenzoate
methylotrophic bacterium
-
-
Dithionitrobenzoate
-
-
Dithionitrobenzoate
-
-
Dithionitrobenzoate
-
-
EDTA
-
50 mM, slight inhibition
ethanol
-
IC50 of 4.8 vol%
ethyl 4-chloroacetoacetate
-
the D221G mutant is extremely sensitive to ethyl 4-chloroacetoacetate with half-lives shorter than 6 min
ethyl-4-chloroacetoacetate
-
wild-type, 7.43% residual activity at 20 mM
Fe3+
-, D6CJK0
83.5% inhibition at 1 mM
-
Hg2+
Candida methanolica
-
-
Hg2+
Kloeckera sp.
-
-
Hg2+
-
1 mM, complete inhibition
Hg2+
-, Q845T0
1 mM, complete inhibition
Hg2+
-
strong inhibition
Hg2+
A9ZNT8, A9ZNT9, -
98% inhibition at 1 mM; 98% inhibition at 1 mM
hydrazine
-
-
hydroxylamine
-
-
iodoacetamide
methylotrophic bacterium
-
-
iodoacetamide
Candida methanolica
-
-
iodoacetamide
-
weak
iodoacetate
-
strong inhibition
iodoacetic acid
-
weak
Isonicotinyl hydrazide
-
weak
Isopropanol
-
IC50 of 4.7 vol%
KF
-
1 mM, 80% inhibition
n-butanol
-
IC50 of 1.4 vol%
n-Propanol
-
IC50 of 2.5 vol%
N3-
methylotrophic bacterium
-
-
N3-
-
1 mM NaN3, 90% inhibition
N3-
-
0.25 mM. Inhibition is partly overcome by addition of formate or NAD+
N3-
Candida methanolica
-
-
N3-
Kloeckera sp.
-
-
NADH
-
competitive versus NAD+
NADH
Pseudomonas methylica
-
competitive versus NAD+; noncompetitive versus formate
NADH
-
inhibition is partly overcome by addition of formate or NAD+
NADH
-
competitive with NADH, mixed-type with formate
NADH
A9ZNT8, A9ZNT9, -
66% inhibition at 0.12 mM; 73% inhibition at 0.12 mM
NADP+
-
strong inhibition
NADPH
-
competitive
NADPH
-
strong inhibition
NADPH
A9ZNT8, A9ZNT9, -
26% inhibition at 0.24 mM; 58% inhibition at 0.24 mM
NaN3
-
1 mM, 80% inhibition
NaN3
-
1 mM, complete inhibition
NaN3
-, Q845T0
1 mM, complete inhibition
NEM
-, Q845T0
1 mM, 25.3% inhibition
Ni2+
Candida methanolica
-
NiCl2
Ni2+
E7RAN7
1 mM Ni2+ inhibits the enzyme activity by 28%
Ni2+
-, D6CJK0
12.4% inhibition at 1 mM
NO2-
-
1 mM, 5% inhibition
NO3-
-
0.25 mM. Inhibition is partly overcome by addition of formate or NAD+
NO3-
-
1 mM, 13% inhibition
NO3-
-
10 mM KNO3, 38% inhibition
o-nitrobenzaldehyde
Candida methanolica
-
slight inhibition
oxidized ADP
-
inactivates by specific reaction at the nucleotide binding site, with negative cooperativity between subunits accounting for appearance of two phases of inactivation, protection by NAD+, NADH and ADP
p-chloromercuribenzoate
-
strong inhibition
p-Chloromercuriphenylsulfonic acid
-
-
p-hydroxymercuribenzoate
-
0.25 mM
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
Pb2+
Kloeckera sp.
-
-
PCMB
methylotrophic bacterium
-
-
PCMB
Candida methanolica
-
-
PCMB
Kloeckera sp.
-
-
PCMB
-
0.2 mM, 10.7% inhibition
PCMB
-, Q845T0
0.2 mM, complete inhibition
Phenol
-
IC50 of 0.32 vol%
phenylmercuric acetate
-
-
pyridoxal 5'-phosphate
Candida methanolica
-
slight inhibition
Semicarbazide
-
-
Sodium azide
A9ZNT8, A9ZNT9, -
94% inhibition at 1 mM; 99% inhibition at 1 mM
sodium hypophosphite
-
1 mM, 80% inhibition
Thiosemicarbazide
-
-
Zn2+
-
1 mM 63% inhibition
Zn2+
-, D6CJK0
55.5% inhibition at 1 mM
methanol
-
IC50 of 10.2 vol%
additional information
-
no loss of activity after 5 h at pH 6.5, 30C, after 5 h with 20 mM ethyl 4-chloro-3-oxobutanoate, 20 mM ethyl-4-bromo-3-oxobutanoate, 20 mM ethyl 2-chloro-3-oxobutanoate, or 20 mM 2,3'-dichloroacetophenone
-
additional information
-
not inhibitory: Mg2+, Mn2+, Co2+, Ni2+, Cd2+, Zn2+, Ca2+, Fe2+, Fe3+, Cu2+
-
additional information
-, D6CJK0
no notable effect on the enzyme activity is observed when adding NH4+ or HPO2-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Dioxane
-
increases maximal reaction rate
EDTA
-, D6CJK0
the enzyme activity is increased 12% over the control by 1 mM EDTA
ethanol
-
increases maximal reaction rate
ethyl acetate
-
wild-type, 21% increase of activity
FAD
-
requirement for either FMN or FAD
FMN
-
restores activity of the formate-inactivated enzyme
FMN
-
requirement for either FMN or FAD
formate
-
activates in a slow reaction of which the velocity is dependent on the concentration of formate
glycerol
-
increases maximal reaction rate
Isopropanol
-
increases maximal reaction rate
KCl
-
adding 5 mM NAD+ in 0.2 M KCl improves the FDH elution and increases the specific FDH activity by 1.38fold as compared to elution with 1 M KCl
methanol
-
increases maximal reaction rate
Propanol
-
increases maximal reaction rate
tert-butanol
-
increases maximal reaction rate
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.16
-
3-acetylpyridine-NAD+
-
-
0.19
-
3-pyridinecarboxaldehyde-NAD+
-
-
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
0.54
-
deamino-NAD+
-
-
0.037
-
dichloroindophenol
-
formate dehydrogenase I, reaction with formate
0.042
-
dichloroindophenol
-
formate dehydrogenase II, reaction with formate
0.2
-
dichloroindophenol
-
formate dehydrogenase I or formate dehydrogenase II, reaction with NADH
4.1
-
ethyl formate
-
in 100 mM potassium phosphate buffer at pH 7.5, at 30C
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, 30C, heated DE-52-fraction
0.011
-
formate
-
pH 7.5, 30C, enzyme expressed in tobacco; pH 7.5, 30C, enzyme from Sephadex G-15 desalted fraction; pH 7.5, 30C, mitochondrial enzyme
0.012
-
formate
-
pH 7.5, 30C, enzyme from DE-52 chromatography
0.077
-
formate
-
-
0.13
-
formate
-
formate dehydrogenase II, reaction with NAD+
0.135
-
formate
-
formate dehydrogenase I, reaction with NAD+
0.17
-
formate
-
pH 7.0, 37C, mutant enzyme R284Q
0.26
-
formate
-
reduction of NAD+
0.472
-
formate
-
at pH 7.5, 25C
0.6
-
formate
-
-
0.62
-
formate
-
in presence of NAD+
0.82
-
formate
E7RAN7
at pH 6.5 and 30C
1.5
-
formate
-
wild type enzyme, in 0.1 M sodium phosphate buffer, pH 7.0, at 30C
1.6
-
formate
-
pH 7.0, 30C
1.67
-
formate
-
and 6.25 mM at the second catalytic site
1.67
-
formate
-
pH 7.0, 30C
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 22C
2.1
-
formate
-
-
2.3
-
formate
Q00498
mutant enzyme Y160E, at pH 8.0 and 25C
2.4
-
formate
-, Q845T0
pH 7.0, 30C
2.5
-
formate
-
pH 6.5, 30C
2.7
-
formate
Q00498
mutant enzyme Y160R, at pH 8.0 and 25C
3
-
formate
Candida methanolica
-
-
3.1
-
formate
-
20C, pH 8, mutant enzyme T69V
3.3
-
formate
-
-
3.6
-
formate
A9ZNT8, A9ZNT9, -
isozyme FDH2
3.9
-
formate
Q00498
mutant enzyme N187E, at pH 8.0 and 25C
4
-
formate
-
mutant enzyme Q313E
4.1
-
formate
A9ZNT8, A9ZNT9, -
isozyme FDH1
4.1
-
formate
-
mutant enzyme F290S, in 0.1 M sodium phosphate buffer, pH 7.0, at 30C
4.2
-
formate
-
wild type enzyme, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
4.4
-
formate
Q00498
mutant enzyme N147R, at pH 8.0 and 25C; mutant enzyme Y302R, at pH 8.0 and 25C
4.4
-
formate
-
in 100 mM potassium phosphate buffer at pH 7.5, at 30C
4.5
-
formate
-
mutant enzyme F290N, in 0.1 M sodium phosphate buffer, pH 7.0, at 30C
4.75
-
formate
Q00498
wild type enzyme, at pH 8.0 and 25C
5
-
formate
-
mutant enzyme K328V, at 20C, 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 30C
5.1
-
formate
Q00498
mutant enzyme Q105R, at pH 8.0 and 25C
5.3
-
formate
Q00498
mutant enzyme H13E, at pH 8.0 and 25C
5.5
-
formate
Q08911
pH 7.0, 30C, wild-type enzyme
5.5
-
formate
Q00498
mutant enzyme N187E/Q105R, at pH 8.0 and 25C
5.6
-
formate
-
pH 7.0, 30C, recombinant enzyme
5.6
-
formate
-
20C, pH 8, wild-type enzyme
5.6
-
formate
-
wild-type, 30C, pH 7.0
5.63
-
formate
-
wild type enzyme, at 20C, in 20 mM triethanolamine at pH 8
5.8
-
formate
-
20C, pH 8, mutant enzyme T226V
5.9
-
formate
Q00498
mutant enzyme N187E/N147R, at pH 8.0 and 25C
6
-
formate
-
oxidized mutant enzyme T169C/T226C, at 20C, in 20 mM triethanolamine at pH 8
6.1
-
formate
B6VPZ9, -
in 0.1 M potassium phosphate buffer, pH 7.5, at 30C
6.25
-
formate
-
and 1.67 mM at the second catalytic site
7
-
formate
-
wild-type enzyme
7.5
-
formate
-
wild-type enzyme and mutant enzyme C255S
7.6
-
formate
-
with thio-NAD+ as electron acceptor
7.7
-
formate
O08375
in 0.1 M potassium phosphate buffer pH 7.0, at 30C
9.3
-
formate
-
20C, pH 8, mutant enzyme T69V/T226V
10
-
formate
-
-
10.8
-
formate
-
reduced mutant enzyme T169C/T226C, at 20C, in 20 mM triethanolamine at pH 8
13
-
formate
-
-
13
-
formate
-
-
13
-
formate
-
-
15
-
formate
methylotrophic bacterium
-
-
15
-
formate
-
pH 7.0, 37C, wild-type enzyme
16
-
formate
-
mutant enzyme K47E, at 20C, after 2 weeks of enzyme storage
19.6
-
formate
-, D6CJK0
with NAD+ as cosubstrate, in 100 mM Tris-HCl (pH 7.0), at 30C
20
-
formate
-
mutant enzyme C255M
20
-
formate
-
mutant enzyme K47E, at 20C, after 4 months of enzyme storage; native wild type enzyme, at 20C, after 2 weeks of enzyme storage
22
-
formate
Kloeckera sp.
-
-
25
-
formate
-
mutant E141N, 30C, pH 7.0
30
-
formate
-
with 3-pyridinecarboxaldehyde-NAD+ as electron acceptor
31
-
formate
-
mutant E141Q, 30C, pH 7.0
35
-
formate
-
native wild type enzyme, at 20C, after 4 months of enzyme storage
39.1
-
formate
-, D6CJK0
with NADP+ as cosubstrate, in 100 mM Tris-HCl (pH 7.0), at 30C
40
-
formate
-
-
40
-
formate
-
mutant enzyme D221G, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
41
-
formate
-
mutant enzyme D221S, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
46
-
formate
-
mutant enzyme D221Q, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
57
-
formate
-
mutant enzyme C145S/D221A/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
62
-
formate
-
mutant enzyme D221G/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
69
-
formate
-
mutant enzyme C145S/D221G/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
81
-
formate
-
mutant enzyme C145S/A198G/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
83
-
formate
-
mutant enzyme C145S/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
98
-
formate
-
mutant enzyme C145S/A198G/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 30C
113
-
formate
-
mutant enzyme C145S/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 30C
127
-
formate
-
mutant enzyme A198G/D221Q, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
145
-
formate
-
pH 7.0, 37C, mutant enzyme R284Q
335
-
formate
-
with 3-acetylpyridine-NAD+ as electron acceptor
1000
-
formate
Q08911
pH 7.0, 30C, mutant enzyme D196A/Y197R, reaction with NADP+
2.6
-
glyoxylate
-
mutant E141Q, 30C, pH 7.0
4.6
-
glyoxylate
-
mutant E141N, 30C, pH 7.0
7.5
-
glyoxylate
-
wild-type, 30C, pH 7.0
0.0057
-
NAD+
-
-
0.015
-
NAD+
-
wild type enzyme, in 0.1 M potassium phosphate buffer (pH 7.5); wild type enzyme, in 0.1 M potassium phosphate buffer (pH 7.5); wild type enzyme, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C
0.0259
-
NAD+
B6VPZ9, -
in 0.1 M potassium phosphate buffer, pH 7.5, at 30C
0.028
-
NAD+
-
pH 6.5, 30C
0.035
-
NAD+
-
pH 7.5, 30C, heated DE-52-fraction
0.0365
-
NAD+
Q08911
pH 7.0, 30C, wild-type enzyme
0.03839
-
NAD+
-
at pH 7.5, 25C
0.043
-
NAD+
-
wild type enzyme, in the absence of 1-methyl-3-methylimidazolium dimethylphosphate, in 50 mM carbonate buffer, pH 9.7, at 30C
0.048
-
NAD+
-
pH 7.0, 30C
0.054
-
NAD+
-
pH 7.0, 30C, recombinant enzyme
0.057
-
NAD+
-, Q845T0
pH 7.0, 30C
0.068
-
NAD+
-
-
0.07
-
NAD+
-
-
0.07
-
NAD+
-
wild-type enzyme and mutant enzyme Q313E
0.07
-
NAD+
-
pH 7.0, 30C
0.075
-
NAD+
-
pH 7.5, 30C, enzyme from DE-52 chromatography; pH 7.5, 30C, enzyme from Sephadex G-15 desalted fraction
0.076
-
NAD+
-
pH 7.5, 30C, mitochondrial enzyme
0.078
-
NAD+
-
pH 7.5, 30C, enzyme expressed in tobacco
0.08
-
NAD+
O08375
in 0.1 M potassium phosphate buffer pH 7.0, at 30C
0.083
-
NAD+
E7RAN7
at pH 6.5 and 30C
0.09
-
NAD+
-
-
0.091
-
NAD+
-, D6CJK0
in 100 mM Tris-HCl (pH 7.0), at 30C
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+
-
formate dehydrogenase II, reaction with formate
0.11
-
NAD+
Candida methanolica
-
-
0.11
-
NAD+
-
pH 7.0, 37C, wild-type enzyme
0.13
-
NAD+
-
mutant enzyme D195Q/Y196P, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q/Y196P, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q/Y196P, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C
0.16
-
NAD+
-
in presence of formate
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 30C
0.18
-
NAD+
-
-
0.3
-
NAD+
-
mutant enzyme C255S
0.6
-
NAD+
-
mutant enzyme C255M
0.96
-
NAD+
-
mutant enzyme D195Q, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C
1.09
-
NAD+
-
mutant enzyme C145S/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 30C
1.5
-
NAD+
-
mutant enzyme D195S, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195S, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195S, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C
1.8
-
NAD+
-
mutant enzyme D195Q/Y196H, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q/Y196H, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q/Y196H, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C
4.1
-
NAD+
-
mutant enzyme C145S/A198G/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 30C
4.7
-
NAD+
-
mutant enzyme D195S; pH 8.0, 20C, mutant enzyme D195S
4.8
-
NAD+
-
mutant enzyme D195A, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195A, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195A, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C
5.01
-
NAD+
-
mutant enzyme D195N, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195N, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195N, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C
5.1
-
NAD+
-
mutant enzyme D195Q/Y196S, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q/Y196S, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q/Y196S, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C
5.5
-
NAD+
-
pH 8.0, 20C, wild-type enzyme; wild-type enzyme
7.6
-
NAD+
Q08911
pH 7.0, 30C, mutant enzyme D196A/Y197R, with 0.25 M formate
8.4
-
NAD+
Q08911
pH 7.0, 30C, mutant enzyme D196A/Y197R, with 0.5 M formate
9.1
-
NAD+
-
mutant enzyme F290S, in 0.1 M sodium phosphate buffer, pH 7.0, at 30C
12.8
-
NAD+
-
mutant enzyme F290D, in 0.1 M sodium phosphate buffer, pH 7.0, at 30C
13.3
-
NAD+
-
wild type enzyme, in 0.1 M sodium phosphate buffer, pH 7.0, at 30C
14
-
NAD+
-
mutant enzyme F290N, in 0.1 M sodium phosphate buffer, pH 7.0, at 30C
25
-
NAD+
-
mutant enzyme K328V, at 20C, after 2 weeks of enzyme storage; mutant enzyme K47E, at 20C, after 2 weeks of enzyme storage
30
-
NAD+
-
mutant enzyme K328V, at 20C, after 4 months of enzyme storage
40
-
NAD+
-
mutant enzyme K47E, at 20C, after 4 months of enzyme storage
50
-
NAD+
-
native wild type enzyme, at 20C, after 2 weeks of enzyme storage
74.6
-
NAD+
A9ZNT8, A9ZNT9, -
isozyme FDH1
90
-
NAD+
-
native wild type enzyme, at 20C, after 4 months of enzyme storage
140
-
NAD+
A9ZNT8, A9ZNT9, -
isozyme FDH2
0.05
-
NADH
-, E2IQB0
in 0.1 M sodium phosphate (pH 6.8), at 37C
0.037
-
NADP+
-
mutant enzyme D221A, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
0.04
-
NADP+
-
Km above 0.04 mM, wild type enzyme, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
0.084
-
NADP+
-
mutant enzyme C145S/A198G/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
0.13
-
NADP+
Q08911
pH 7.0, 30C, 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 30C
0.16
-
NADP+
Q08911
pH 7.0, 30C, mutant enzyme D196A/Y197R, with 0.5 M formate
0.24
-
NADP+
-
mutant enzyme D221G/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
0.27
-
NADP+
-
mutant enzyme A198G/D221Q, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
0.31
-
NADP+
-
mutant enzyme D221G, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
0.39
-
NADP+
-
mutant enzyme D221Q, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
0.43
-
NADP+
-
mutant enzyme D221S, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
0.57
-
NADP+
-
mutant enzyme C145S/D221G/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
0.59
-
NADP+
-
mutant enzyme C145S/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
0.74
-
NADP+
-
mutant enzyme C145S/D221A/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
0.92
-
NADP+
-
mutant enzyme C145S/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 30C
1.7
-
NADP+
-
mutant enzyme D195Q/Y196H, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q/Y196H, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q/Y196H, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C
3.3
-
NADP+
-
mutant enzyme D195A, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195A, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195A, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C
3.5
-
NADP+
-, D6CJK0
in 100 mM Tris-HCl (pH 7.0), at 30C
3.7
-
NADP+
-
mutant enzyme D195Q/Y196P, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q/Y196P, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q/Y196P, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C
4.5
-
NADP+
-
mutant enzyme D195Q, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C
6.2
-
NADP+
-
mutant enzyme D195Q/Y196S, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q/Y196S, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q/Y196S, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C; mutant enzyme D195S, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195S, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195S, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C
13.2
-
NADP+
-
mutant enzyme D195N, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195N, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195N, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C
29.5
-
NADP+
B6VPZ9, -
in 0.1 M potassium phosphate buffer, pH 7.5, at 30C
38
-
NADP+
-
Km above 38 mM, wild type enzyme, in 0.1 M potassium phosphate buffer (pH 7.5); Km above 38 mM, wild type enzyme, in 0.1 M potassium phosphate buffer (pH 7.5); Km above 38 mM, wild type enzyme, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C
1.7
-
phenyl formate
-
in 100 mM potassium phosphate buffer at pH 7.5, at 30C
4.7
-
propyl formate
-
in 100 mM potassium phosphate buffer at pH 7.5, at 30C
0.45
-
S-formylglutathione
-
-
1.1
-
S-formylglutathione
-
-
2.9
-
methyl formate
-
in 100 mM potassium phosphate buffer at pH 7.5, at 30C
additional information
-
additional information
-
effect of organic solvents of formate dehydrogenase
-
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
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.01
-
formate
-
mutant E141N, 30C, pH 7.0
0.054
-
formate
-
mutant E141Q, 30C, pH 7.0
0.25
-
formate
Q00498
mutant enzyme Y302R, at pH 8.0 and 25C
0.29
-
formate
-
oxidized mutant enzyme T169C/T226C, at 20C, in 20 mM triethanolamine at pH 8
0.3
-
formate
-
20C, pH 8, mutant enzyme T69V; 20C, pH 8, mutant enzyme T69V/T226V
0.3
-
formate
Q00498
mutant enzyme Y160R, at pH 8.0 and 25C
0.31
-
formate
-
pH 7.0, 37C, mutant enzyme R284Q
0.5
-
formate
-
reduced mutant enzyme T169C/T226C, at 20C, in 20 mM triethanolamine at pH 8
0.5
-
formate
Q00498
mutant enzyme N187E/N147R, at pH 8.0 and 25C
0.55
-
formate
Q00498
mutant enzyme H13E, at pH 8.0 and 25C
0.6
-
formate
Q00498
mutant enzyme N187E/Q105R, at pH 8.0 and 25C
0.7
-
formate
Q00498
mutant enzyme N187E, at pH 8.0 and 25C
0.8
-
formate
Q00498
mutant enzyme Y160E, at pH 8.0 and 25C
0.85
-
formate
Q00498
mutant enzyme N147R, at pH 8.0 and 25C
1.1
-
formate
-
20C, pH 8, mutant enzyme T226V
1.13
-
formate
Q00498
wild type enzyme, at pH 8.0 and 25C
1.2
-
formate
-
20C, pH 8, wild-type enzyme
1.2
-
formate
-
wild type enzyme, at 20C, in 20 mM triethanolamine at pH 8
1.2
-
formate
Q00498
mutant enzyme Q105R, at pH 8.0 and 25C
1.3
-
formate
B6VPZ9, -
in 0.1 M potassium phosphate buffer, pH 7.5, at 30C
2.32
-
formate
E7RAN7
at pH 6.5 and 30C
2.8
-
formate
-
mutant enzyme F290N, in 0.1 M sodium phosphate buffer, pH 7.0, at 30C
2.9
-
formate
-
wild type enzyme, in 0.1 M sodium phosphate buffer, pH 7.0, at 30C
4.1
-
formate
-
mutant enzyme F290S, in 0.1 M sodium phosphate buffer, pH 7.0, at 30C
5.1
-
formate
-
mutant enzyme F290D, in 0.1 M sodium phosphate buffer, pH 7.0, at 30C
6.1
-
formate
-
wild-type, 30C, pH 7.0
7.3
-
formate
O08375
in 0.1 M potassium phosphate buffer pH 7.0, at 30C
10
-
formate
-
pH 7.0, 37C, wild-type enzyme
0.007
-
glyoxylate
-
wild-type, 30C, pH 7.0
0.023
-
glyoxylate
-
mutant E141Q, 30C, pH 7.0
0.095
-
NAD+
Q08911
pH 7.0, 30C, mutant enzyme D196A/Y197R
0.12
-
NAD+
Q08911
pH 7.0, 30C, mutant enzyme D196A/Y197R, with 0.5 M formate
0.21
-
NAD+
-
mutant enzyme D195N, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195N, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195N, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C
0.26
-
NAD+
-
mutant enzyme D195Q, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C
0.34
-
NAD+
-
mutant enzyme D195S, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195S, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195S, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C
0.4
-
NAD+
-
mutant enzyme D195Q/Y196S, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q/Y196S, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q/Y196S, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C
0.49
-
NAD+
-
mutant enzyme D195Q/Y196H, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q/Y196H, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q/Y196H, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C
0.76
-
NAD+
-
mutant enzyme D195A, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195A, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195A, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C
0.87
-
NAD+
-
mutant enzyme D195Q/Y196P, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q/Y196P, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q/Y196P, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C
1.2
-
NAD+
B6VPZ9, -
in 0.1 M potassium phosphate buffer, pH 7.5, at 30C
1.4
-
NAD+
-
pH 8.0, 20C, wild-type enzyme; wild-type enzyme
1.6
-
NAD+
-
mutant enzyme S195S; pH 8.0, 20C, mutant enzyme D195S
2.8
-
NAD+
-
mutant enzyme F290N, in 0.1 M sodium phosphate buffer, pH 7.0, at 30C
2.9
-
NAD+
-
wild type enzyme, in 0.1 M sodium phosphate buffer, pH 7.0, at 30C
3.7
-
NAD+
-
wild type enzyme, in 0.1 M potassium phosphate buffer (pH 7.5); wild type enzyme, in 0.1 M potassium phosphate buffer (pH 7.5); wild type enzyme, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C
4.1
-
NAD+
-
mutant enzyme F290S, in 0.1 M sodium phosphate buffer, pH 7.0, at 30C
5.1
-
NAD+
-
mutant enzyme F290D, in 0.1 M sodium phosphate buffer, pH 7.0, at 30C
5.18
-
NAD+
-
mutant enzyme C145S/A198G/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 30C
6.5
-
NAD+
Q08911
pH 7.0, 30C, wild-type enzyme
6.67
-
NAD+
-, D6CJK0
in 100 mM Tris-HCl (pH 7.0), at 30C
8.22
-
NAD+
-
mutant enzyme C145S/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 30C
890
-
NAD+
-
wild type enzyme, in the absence of 1-methyl-3-methylimidazolium dimethylphosphate, in 50 mM carbonate buffer, pH 9.7, at 30C
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 30C
0.08
-
NADH
-, E2IQB0
in 0.1 M sodium phosphate (pH 6.8), at 37C
0.00004
-
NADP+
-
wild type enzyme, in 0.1 M potassium phosphate buffer (pH 7.5); wild type enzyme, in 0.1 M potassium phosphate buffer (pH 7.5); wild type enzyme, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C
0.005
-
NADP+
B6VPZ9, -
in 0.1 M potassium phosphate buffer, pH 7.5, at 30C
0.052
-
NADP+
-
mutant enzyme D195A, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195A, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195A, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C
0.26
-
NADP+
-
mutant enzyme D195N, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195N, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195N, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C; mutant enzyme D195Q, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C
0.34
-
NADP+
-
mutant enzyme D195Q/Y196P, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q/Y196P, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q/Y196P, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C; mutant enzyme D195Q/Y196S, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q/Y196S, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q/Y196S, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C; mutant enzyme D195S, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195S, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195S, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C
0.44
-
NADP+
-
mutant enzyme D195Q/Y196H, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q/Y196H, in 0.1 M potassium phosphate buffer (pH 7.5); mutant enzyme D195Q/Y196H, in 0.1 M potassium phosphate buffer (pH 7.5), at 37C
0.52
-
NADP+
-
mutant enzyme D221G, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
0.55
-
NADP+
-
mutant enzyme D221S, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
0.62
-
NADP+
-
mutant enzyme D221G/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
0.79
-
NADP+
-
mutant enzyme A198G/D221Q, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
1.04
-
NADP+
-
mutant enzyme D221Q, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
1.05
-
NADP+
-
mutant enzyme D221A, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
1.07
-
NADP+
-, D6CJK0
in 100 mM Tris-HCl (pH 7.0), at 30C
1.5
-
NADP+
-
mutant enzyme C145S/A198G/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
1.64
-
NADP+
-
mutant enzyme C145S/D221G/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
1.91
-
NADP+
-
mutant enzyme C145S/D221A/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
2.76
-
NADP+
-
mutant enzyme C145S/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
3.08
-
NADP+
-
mutant enzyme C145S/A198G/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 30C
4.5
-
NADP+
Q08911
pH 7.0, 30C, mutant enzyme D196A/Y197R
7.89
-
NADP+
-
mutant enzyme C145S/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 30C
0.36
-
glyoxylate
-
mutant E141N, 30C, pH 7.0
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.06
-
formate
Q00498
mutant enzyme Y302R, at pH 8.0 and 25C
10572
0.08
-
formate
Q00498
mutant enzyme N187E/N147R, at pH 8.0 and 25C
10572
0.1
-
formate
Q00498
mutant enzyme H13E, at pH 8.0 and 25C
10572
0.11
-
formate
Q00498
mutant enzyme N187E/Q105R, at pH 8.0 and 25C; mutant enzyme Y160R, at pH 8.0 and 25C
10572
0.18
-
formate
Q00498
mutant enzyme N187E, at pH 8.0 and 25C
10572
0.2
-
formate
Q00498
mutant enzyme N147R, at pH 8.0 and 25C
10572
0.24
-
formate
Q00498
mutant enzyme Q105R, at pH 8.0 and 25C; wild type enzyme, at pH 8.0 and 25C
10572
0.35
-
formate
Q00498
mutant enzyme Y160E, at pH 8.0 and 25C
10572
0.62
-
formate
-
mutant enzyme F290N, in 0.1 M sodium phosphate buffer, pH 7.0, at 30C
10572
1
-
formate
-
mutant enzyme F290S, in 0.1 M sodium phosphate buffer, pH 7.0, at 30C
10572
1.02
-
formate
-
mutant enzyme F290D, in 0.1 M sodium phosphate buffer, pH 7.0, at 30C
10572
1.93
-
formate
-
wild type enzyme, in 0.1 M sodium phosphate buffer, pH 7.0, at 30C
10572
2.83
-
formate
E7RAN7
at pH 6.5 and 30C
10572
73.3
-
NAD+
-, D6CJK0
in 100 mM Tris-HCl (pH 7.0), at 30C
14330
200
-
NAD+
-
mutant enzyme F290N, in 0.1 M sodium phosphate buffer, pH 7.0, at 30C
14330
220
-
NAD+
-
wild type enzyme, in 0.1 M sodium phosphate buffer, pH 7.0, at 30C
14330
400
-
NAD+
-
mutant enzyme F290D, in 0.1 M sodium phosphate buffer, pH 7.0, at 30C
14330
450
-
NAD+
-
mutant enzyme F290S, in 0.1 M sodium phosphate buffer, pH 7.0, at 30C
14330
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 30C
14330
20600
-
NAD+
-
wild type enzyme, in the absence of 1-methyl-3-methylimidazolium dimethylphosphate, in 50 mM carbonate buffer, pH 9.7, at 30C
14330
1.6
-
NADH
-, E2IQB0
in 0.1 M sodium phosphate (pH 6.8), at 37C
14331
0.306
-
NADP+
-, D6CJK0
in 100 mM Tris-HCl (pH 7.0), at 30C
27497
1.29
-
NADP+
-
mutant enzyme D221S, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
27497
1.69
-
NADP+
-
mutant enzyme D221G, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
27497
2.58
-
NADP+
-
mutant enzyme C145S/D221A/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C; mutant enzyme D221G/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
27497
2.67
-
NADP+
-
mutant enzyme D221Q, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
27497
2.83
-
NADP+
-
mutant enzyme D221A, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
27497
2.88
-
NADP+
-
mutant enzyme C145S/D221G/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
27497
2.94
-
NADP+
-
mutant enzyme A198G/D221Q, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
27497
4.68
-
NADP+
-
mutant enzyme C145S/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
27497
8.58
-
NADP+
-
mutant enzyme C145S/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 30C
27497
17.9
-
NADP+
-
mutant enzyme C145S/A198G/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 22C
27497
21
-
NADP+
-
mutant enzyme C145S/A198G/D221Q/C255V, in 0.1 M sodium phosphate buffer (pH 7.0), at 30C
27497
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0228
-
ADP-beta-D-ribose
-
substrate formate, pH 6.5, 30C
0.0369
-
ADP-beta-D-ribose
-
substrate NAD+, pH 6.5, 30C
0.000007
-
azide
-
-
0.0000239
-
azide
-
substrate formate, pH 6.5, 30C
0.00015
-
azide
-
pH 7.0, 37C, wild-type enzyme
0.00095
-
azide
-
substrate NAD+, pH 6.5, 30C
0.024
-
azide
-
pH 7.0, 37C, mutant enzyme R284Q
0.053
-
bicarbonate
-
substrate formate, pH 6.5, 30C
1.2
-
bicarbonate
-
substrate formate, pH 6.5, 30C
5.6
-
bicarbonate
-
substrate NAD+, pH 6.5, 30C
78.14
-
NAD+
-
at pH 7.5, 25C
0.06
-
NADH
-
substrate NAD+, pH 6.5, 30C
0.1175
-
NADH
-
at pH 7.5, 25C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0013
-
-
pH 7.5, 30C, enzyme from Sephadex G-15 desalted fraction
0.043
-
-
pH 7.5, 30C, enzyme from DE-52 chromatography
0.058
-
-
pH 7.5, 30C, mitochondrial enzyme
0.094
-
-
pH 7.5, 30C, heated DE-52-fraction
0.143
-
Kloeckera sp.
-
-
0.18
-
-
native enzyme in 200 mM sodium formate and 2 mM NAD+, at 25C, the specific activity of FDH is insensitive to changes in any of the two cultivation parameters
0.285
-
-
mutant C6S/C256S, pH 6.5, 30C
0.5
-
-
crude extract, at pH 7.4 and 25C
0.504
-
-
mutant C6S/C256V, pH 6.5, 30C
0.635
-
-
mutant C6S/C256A, pH 6.5, 30C
1
-
O13437
crude extract, in 30 mM Tris-HCl, pH 7.5. at 25C
1.15
-
-
mutant C6A/C146A/C256V, pH 6.5, 30C
1.256
-
-
pH 7.5, 30C, enzyme expressed in tobacco
1.395
-
-
-
1.4
-
-
recombinant enzyme, in 200 mM sodium formate and 2 mM NAD+, at 25C
1.49
-
-
mutant C6A/C146V/C256V, pH 6.5, 30C
1.62
-
-
mutant C6V/C256S, pH 6.5, 30C
1.83
-
-
mutant C6A/C256V, pH 6.5, 30C
1.98
-
-
mutant C6A/C256S, pH 6.5, 30C
2.29
-
-
mutant C146S/C256V, pH 6.5, 30C
2.43
-
-
reaction with NAD+
2.58
-
-
mutant C256V, pH 6.5, 30C
2.63
-
-
after 5.5fold purification, at pH 7.4 and 25C
2.65
-
-
mutant C6A/C146S/C256V, pH 6.5, 30C
2.83
-
-
-
3.04
-
Pseudomonas methylica
-
-
3.24
-
-
wild-type, pH 6.5, 30C
3.68
-
-
-
4.09
-
-
-
4.4
-
O13437
recombinant enzyme, after 4.5fold purification, in 30 mM Tris-HCl, pH 7.5. at 25C
4.55
-
-
reaction with ferricyanide
5.97
-
-
-
6.03
-
-, D6CJK0
purified enzyme, in 100 mM Tris-HCl (pH 7.0), at 30C
7.52
-
Candida methanolica
-
-
9.47
-
-, Q845T0
-
11
-
methylotrophic bacterium
-
-
310
-
-
recombinant enzyme, at pH 7.5 and 30C
383.4
-
-
pH 6.5, 30C
439
-
-
native enzyme, at pH 7.5 and 30C
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.2
10.5
methylotrophic bacterium
-
-
5.7
6.5
-
-
6
7
E7RAN7
-
6
-
-, D6CJK0
-
6.3
-
-, Q845T0
-
6.5
9
-
-
6.5
9.5
Candida methanolica
-
-
6.6
-
-
carbonate reduction by enzyme I
6.7
-
-
CO2 reduction
6.8
-
-
reduction of cytochrome c and dichloroindophenol
7
-
-
maximum peak area due to NADH, in 0.1 M PIPES buffer
7.4
-
-
formate oxidation
7.4
-
-
formate dehydrogenation, enzyme I
7.5
8.5
-
-
7.5
-
-
mutant enzyme D195Q/Y196H
7.7
-
-
phosphate buffer
7.9
-
-
Tris-HCl buffer
8
8.5
-
in 120 mM potassium phosphate buffer
8
-
-
reduction of NAD+
8
-
Kloeckera sp.
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
10
Kloeckera sp.
-
pH 5.0: about 50% of maximal activity, pH 10.0: about 65% of maximal activity
5
10
-
completely inactive below pH 5.5 and above pH 10.0
5
10
-
pH 5.0: about 80% of maximal activity, pH 10.0: about 65% of maximal activity
5
10.5
-, Q845T0
pH 5.0: about 60% of maximal activity, pH 5.3: about 80% of maximal activity, pH 9.6: about 80% of maximal activity, pH 10.5: about 65% of maximal activity
5
6
-
no activity at pH 5.0 or lower, pH 6.0: optimum
5.3
10.1
-
50% of maximal activity at pH 5.3 and at pH 10.1
5.5
10
-
pH 5.5: about 25% of maximal activity, pH 10.0: about 40% of maximal activity
5.5
8.5
-
mutant enzyme D195Q/Y196H
5.5
8.5
-
-
5.5
9.5
-, D6CJK0
the specific activity at pH ranging from 5.5 to 9.5 is always more than 77% of the maximum activity
6
8
E7RAN7
the enzyme displays a relatively wide pH spectrum and shows more than 98% of relative activity from pH 6.0 to 7.0 and still has 81 and 75% of relative activity under pH 7.5 and 8.0, respectively
7.2
8.4
-
pH 7.2: about 45% of maximal activity, pH 8.4: about 65% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
free enzyme
50
-
Candida methanolica
-
-
50
-
Kloeckera sp.
-
-
50
-
-, Q845T0
-
50
-
-, D6CJK0
-
65
-
E7RAN7
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
60
-, D6CJK0
enzyme activity increases linearly from 25 to 50C and reaches the highest at 50C. The enzyme activity at temperatures ranging from 35 to 60C is always more than 60% of the maximum activity
30
60
Kloeckera sp.
-
30C: about 40% of maximal activity, 60C: about 80% of maximal activity
35
60
-, Q845T0
35C: about 50% of maximal activity, 60C: about 45% of maximal activity
40
65
-
40C: about 40% of maximal activity, 65C: about 30% of maximal activity
60
70
E7RAN7
the enzyme has more than 70% of relative activity when the temperature is between 60 and 70C, but the enzyme activity decreases abruptly when the temperature is controlled below 60C or above 70 C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.29
-
A9ZNT8, A9ZNT9, -
predicted from amino acid sequence; predicted from amino acid sequence
6.9
-
-, D6CJK0
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
of transgenic Arabidopsis and tobacco plants
Manually annotated by BRENDA team
B6VPZ9, -
detected in cells of the root vascular bundle adjacent to nodule, higher mRNA levels are detected in developing green seedpods and during the early stages of nodule development
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
of transgenic Arabidopsis and tobacco plants
Manually annotated by BRENDA team
-
of transgenic Arabidopsis and tobacco plants
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
39300
-
A9ZNT8, A9ZNT9, -
predicted from amino acid sequence; predicted from amino acid sequence
42000
-
-
monomer, SDS-PAGE
70000
-
methylotrophic bacterium
-
gel filtration
70000
-
-
gel filtration
70000
-
-
gel filtration
70000
-
-
gel filtration
71000
-
Candida methanolica
-
equilibrium sedimentation
72000
-
-
equilibrium sedimentation
74000
-
-
equilibrium sedimentation
74000
-
-
-
78000
-
E7RAN7
native enzyme, gel filtration
80300
-
-
gel filtration
82000
-
Candida methanolica
-
velocity sedimentation
82300
-
-
gel filtration
84000
-
Candida methanolica
-
gel filtration
84000
-
-
gel filtration
84000
-
P33160
SDS-PAGE
94000
-
-
gel filtration
98000
-
-
gel filtration
100000
-
-, Q845T0
gel filtration
155000
-
-
low-molecular weight form, non-denaturing PAGE
175000
-
-
formate dehydrogenase II, sucrose density gradient centrifugation
197000
-
-
non-denaturing gradient PAGE
200000
-
-
enzyme form FDHI, sucrose density gradient centrifugation
280000
-
-
gel filtration
300000
-
-
enzyme form FDHII, sucrose density gradient centrifugation
315000
-
-
high-molecular weight form, non-denaturing PAGE
315000
-
-
formate dehydrogenase I, sucrose density gradient centrifugation
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 43757, calculation from nucleotide sequence
?
-, E2IQB0
x * 80700, SDS-PAGE
?
Q00498
x * 42000, SDS-PAGE
?
Clostridium carboxidivorans P7T
-
x * 80700, SDS-PAGE
-
dimer
-
2 * 36000, SDS-PAGE
dimer
methylotrophic bacterium
-
2 * 46000, SDS-PAGE
dimer
-
1 * 59000 + 1 * 100000, formate dehydrogenase II, SDS-PAGE
dimer
-
2 * 46000, SDS-PAGE
dimer
Candida methanolica
-
2 * 43000, SDS-PAGE
dimer
-
2 * 48000, SDS-PAGE
dimer
-
2 * 34000, SDS-PAGE
dimer
-
2 * 47000, SDS-PAGE
dimer
-
2 * 47000, SDS-PAGE
dimer
-, Q845T0
2 * 44000, SDS-PAGE
dimer
-
alpha1beta1, 1 * 107000 + 1 * 61000, SDS-PAGE, MALDI-TOF analysis
dimer
-
2 * 42000, SDS-PAGE
dimer
-
2 * 42400, SDS-PAGE
dimer
Ancylobacter aquaticus KNK607M
-
2 * 44000, SDS-PAGE
-
dimer
Komagataella pastoris IFP 206
-
2 * 34000, SDS-PAGE
-
dimer
Komagataella pastoris NRRL Y-7556
-
2 * 47000, SDS-PAGE
-
dimer
methylotrophic bacterium 1
-
2 * 46000, SDS-PAGE
-
dimer
Moraxella sp. C-1
-
2 * 48000, SDS-PAGE
-
homodimer
P33160
2 * 42000, SDS-PAGE
homodimer
-
x-ray crystallography
homodimer
E7RAN7
2 * 39994, calculated from amino acid sequence; 2 * 40000, SDS-PAGE
homodimer
-, D6CJK0
2 * 44000, calculated from amino acid sequence; 2 * 45000, SDS-PAGE
homodimer
-
2 * 44000, calculated from amino acid sequence; 2 * 45000, SDS-PAGE
-
homodimer
Ogataea angusta DL-1
-
2 * 39994, calculated from amino acid sequence; 2 * 40000, SDS-PAGE
-
tetramer
-
alpha2,beta2, 2 * 102600 + 2 * 54800, SDS-PAGE
tetramer
-
2 * 59000 + 2 * 100000, formate dehydrogenase I, SDS-PAGE
tetramer
-
4 * 75000, SDS-PAGE
tetramer
-
alpha,beta,gamma,delta, 1 * 110000 + 1 * 57000 + 1 * 19400 + 1 * 11600, SDS-PAGE
tetramer
Methylobacterium sp. RXM
-
4 * 75000, SDS-PAGE
-
monomer
-
1 * 42000, SDS-PAGE
additional information
-
formate dehydrogenase I is a dimer of formate dehydrogenase II
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
in complex with NAD+ and azide
-
sitting drop vapour diffusion method with 0.1 M sodium-cacodylate pH 6.5, 0.15 M ammonium sulfate, 30% (w/v) PEG 8K (mutant K47E), and 0.1 M sodium cacodylate pH 6.0, 0.2 M ammonium sulfate, and 32.5% (w/v) PEG 8K (mutant K328V)
-
by adding polyethylene glycol No. 6000
Candida methanolica
-
re-evaluation of crystallographic data
P07658
hanging drop vapor diffusion method, using 2.3 M ammonium sulfate in 0.1 M bis Tris buffer pH 6.5 (for the holoenzyme bound to NAD+ and azide) or 2.2 M ammonium sulfate and 2% (w/v) PEG 400 in 0.1 M HEPES buffer pH 7.5 (for the apoenzyme)
O08375
in complex with formate, molecular replacement method. Four protein molecules per asymmetric unit, forming two dimers identical to the dimer of apoenzyme. The sulfur atom of C354 exists in the oxidized state
-
in complex with NADH. The biologically active dimer is formed by the crystallograohic rotation axis. Comparison with structure of apoenzyme and enzyme-NAD+-azide triple complex
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
10.5
-, D6CJK0
the enzyme retains more than 80% of the activities after incubating in buffers with different pH ranging from 4.5 to 10.5 for 1 h
4.5
-
-
30C, 22h, about 75% loss of activity
5
-
-
30C, 22h, about 20% loss of activity
5
-
-, Q845T0
30C, 20 h, about 50% of initial activity
5.2
9
-
30C, 1 h, more than 90% of the activity is retained
5.2
-
-
37C, 15 min, 50% loss of activity
5.5
-
Candida methanolica
-
30C, 10 min, 61% loss of activity
5.6
-
-
optimal stability
6
8
-
30C, 22 h, stable
6.5
10
-
10 min, stable
6.5
9.5
Candida methanolica
-
10 min, 30C, stable
7
-
-, Q845T0
30C, 20 h, most stable at
7.5
-
-
optimal stability in presence of 10 mM KNO3
8
-
-
rapid decrease of stability above
8
-
-, Q845T0
30C, 20 h, about 25% of initial activity
8.5
-
-
30C, 22h, about 25% loss of activity
8.5
-
-, Q845T0
30C, 20 h, about 40% of initial activity
9
-
-
30C, 22h, about 55% loss of activity
9.9
-
-
37C, 15 min, 50% loss of activity
10.5
-
Candida methanolica
-
30C, 10 min, 41% loss of activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
50
-
the enzyme remains stable from 25-50C and rapidly loses activity at higher temperatures (inactive at 60C)
30
-
-
pH 5.2-9.0, 1 h, more than 90% of the activity is retained
35
-
-
10 min, stable
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
40
60
E7RAN7
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
-
Q08911
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
50
60
-, D6CJK0
the enzyme is stable at temperatures below 55C for 30 min and retains 71% of the initial activity after incubation at 60C for 30 min. The half-life at 60C is 52.9 min
50
60
Q00498
the wild type enzyme retains full activity after 20 min incubation at 50C and shows 85.5 and 6.6% activity after 20 min incubation at 55 and 60C, respectively
50
-
-
1 min, 50% loss of activity
50
-
-
pH 9.0, 10 min, about 50% loss of activity
50
-
-
10 min, stable
50
-
Kloeckera sp.
-
10 min, stable
50
-
-
1 h, stable
50
-
-
pH 7.0, 10 min, stable at or below
50
-
-, Q845T0
pH 7.0, 10 min, stable at or lower
50
-
-
native enzyme, pH 7.0, 10 h, fully active
52
-
methylotrophic bacterium
-
inactivation rate constant is zero
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
-
-
pH 9.0, 10 min, stable
55
-
-
10 min, stable up to
55
-
-
1 h, 75% loss of activity
55
-
-
pH 7.0, 10 min, about 55% loss of activity
55
-
-
at 55C, where native FDH loses 50% activity within 20 min incubation due to heat inactivation, the mutants preserve 84% (K47E) and 70% (K328V) residual activity
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
60
-
Candida methanolica
-
10 min, 36% loss of activity
60
-
-
10 min, complete loss of activity
60
-
-
10 min, 88% 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
61
-
methylotrophic bacterium
-
inactivation rate constant: 0.0114/min
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
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
-
-
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
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
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
after modification with either cholinium, hydroxyethyl-methylimidazolium, or hydroxypropyl-methylimidazolium cations, the FDH still presents 30-45% of activity in aqueous buffer in 70% (v/v) dimethylimidazolium dimethyl phosphate while the native enzyme is inactive at this ionic liquid concentration. The half-life of the modified enzyme is also increased by a 5fold factor after modification by cholinium (9 days) and by a 3fold factor after modification by hydroxyethyl-methylimidazolium or hydroxypropyl-methylimidazolium cations (6 and 5 days respectively) in aqueous solution. The half-life of the wild type FDH in aqueous solution is 1.5 days. When stored in 37.5% (v/v) dimethylimidazolium dimethyl phosphate, both modified and unmodified FDH have an increased half-life of 6-9 days
-
formate dehydrogenase immobilized on magnetic glyoxylagarose support suffers a decrease in formate conversion with the increase in immobilization time. MagNP-APTS/FDH (enzyme on a magnetic support containing a silica gel coated magnetite core which is further silanized with a minopropyltriethoxysilane minopropyltriethoxysilane) shows increased stability when incubated for up to 1 h at 60C and pH 7.5, while MagNP-APTS/glyoxyl-agarose/FDH (enzyme on a magnetic support consisting of magnetite-aminopropyltriethoxysilane coatedwith glyoxyl-agarose) is completely inactive after 20 min of incubation
-
the activities of liposomal FDH/cofactor systems are highly stable in the airlift regardless of the type of gas phase, whereas free FDH is deactivated in the airlift especially at high superficial gas velocity with CO2 bubbles (after 360 min at 45C)
-
instability to freezing and thawing
-
strong inhibition by light
-
N3- and NO3- stabilize
-
inactivated by light irradiation
-
both dithiothreitol, 10 mM, and glycerol, 10%, are required for stability during purification
-
rapid freezing in liquid nitrogen gives 75% recovery
-
enzyme immobilized on highly activated glyoxyl agarose, retains full activity after 24 h in 50% acetone or dioxane. At 75% acetone, immobilized enzyme keeps more than 65% of initial activity after 4 days
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3-methyl-1-butanol
-, D6CJK0
the enzyme retains 87% of the initial activity after incubating in 60% (v/v) 3-methyl-1-butanol for 1 h
Acetone
-, D6CJK0
the enzyme retains nearly 100% of the initial activity after incubating with up to 60% (v/v) acetone
Acetone
-
the enzyme retains nearly 100% of the initial activity after incubating with up to 60% (v/v) acetone
-
dimethyl sulfoxide
E7RAN7
the enzyme activity almost does not decrease after incubation in 20% (v/v) dimethyl sulfoxide
dimethyl sulfoxide
-, D6CJK0
the enzyme retains nearly 100% of the initial activity after incubating with up to 20% (v/v) dimethyl sulfoxide
dimethyl sulfoxide
-
the enzyme retains nearly 100% of the initial activity after incubating with up to 20% (v/v) dimethyl sulfoxide
-
dimethyl sulfoxide
Ogataea angusta DL-1
-
the enzyme activity almost does not decrease after incubation in 20% (v/v) dimethyl sulfoxide
-
Ethanol
-, D6CJK0
the enzyme retains nearly 100% of the initial activity after incubating with up to 20% (v/v) ethanol
Ethanol
-
the enzyme retains nearly 100% of the initial activity after incubating with up to 20% (v/v) ethanol
-
isopropanol
-, D6CJK0
the enzyme retains nearly 100% of the initial activity after incubating with up to 60% (v/v) isopropanol
isopropanol
-
the enzyme retains nearly 100% of the initial activity after incubating with up to 60% (v/v) isopropanol
-
Methanol
-, D6CJK0
the enzyme retains nearly 100% of the initial activity after incubating with up to 10% (v/v) methanol
Methanol
-
the enzyme retains nearly 100% of the initial activity after incubating with up to 10% (v/v) methanol
-
n-Butanol
E7RAN7
the enzyme activity almost does not decrease after incubation in 20% (v/v) n-butanol
n-Butanol
Ogataea angusta DL-1
-
the enzyme activity almost does not decrease after incubation in 20% (v/v) n-butanol
-
n-hexane
E7RAN7
the enzyme activity almost does not decrease after incubation in 20% (v/v) n-hexane
n-hexane
-, D6CJK0
the enzyme retains nearly 100% of the initial activity after incubating with up to 20% (v/v) n-hexane
n-hexane
Ogataea angusta DL-1
-
the enzyme activity almost does not decrease after incubation in 20% (v/v) n-hexane
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
strong inhibition by O2
-
288094
unstable under oxygen
-
288120
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, native enzyme in 150 mM NaCl in 20 mM bis-Tris-propane pH 7.4, 1 day, no loss of activity
-
4C, native enzyme in 150 mM NaCl in 20 mM bis-Tris-propane pH 7.4, 2 weeks, 29% loss of activity
-
4C, native enzyme in 150 mM NaCl in 20 mM bis-Tris-propane pH 7.4, 4 months, 86% loss of activity
-
4C, stable for several weeks
-
-20C, potassium phosphate buffer, pH 7.0, 45% v/v glycerol, 1.0 mM dithiothreitol, stable for 2 months
Candida methanolica
-
4C, 0.01 M buffer, 10 days, 50% loss of activity
Candida methanolica
-
4C, enzyme dissolved in glycerol, retains activity for a few months
-
4C, pH 7.6, in presence of cofactor, EDTA, 2-mercaptoethanol and glycerol, 50% loss of activity after 72 h. NADH decrease the inactivation constant 2.5fold, formate decreases the inactivation constant 5fold, 2-mercaptoethanol decreases the inactivation constant 8fold
-
activity is retained in presence of dithiothreitol for 6 months, but lost within weeks in absence of SH compounds
-
5C, in the dark, in 0.05 M potassium phosphate buffer, pH 7, 1 mM EDTA, 5 mM 2-mercaptoethanol, 10% ammonium sulfate, stable for at least 3 weeks
-
-20C, stable for several weeks
-
-15C, 50% loss of activity after 1 month
-
0C, under anaerobic conditions, stable for some weeks
-
4C, 50 mM phosphate buffer, pH 7.5, 1 mM EDTA, 2 mM 2-mercaptoethanol, 9 months, enzyme retains 90 to 98% of its activity
-
-70C, without stabilizer, 85% loss of activity, 7% loss of activity in 33% glycerol solution
-
0C, 50% loss of activity after 1 month
-
-20C, 50% loss of activity ater 1 month
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Ni-NTA resin column chromatography
-, D6CJK0
AMP-Sepharose column chromatography and Superdex 200 gel filtration
-
Cibacron Blue 3GA-Sepharose affinity column chromatography; Cibacron Blue 3GA-Sepharose affinity column chromatography
-
partial purification, Q-Sepharose column chromatography
O13437
precipitation with polyethyleneimine at 0.04 mg/ml and Sepharose-Procion Blue HERB column chromatography
-
-
Candida methanolica
-
mutant enzyme D195S
-
Ni-NTA column chromatography
-
Ni-NTA resin column chromatography
-
two-step procedure and single-step procedure
-
Ni2+ column chromatography; Ni2+ column chromatography
A9ZNT8, A9ZNT9, -
His GraviTrap column chromatography
-, E2IQB0
essential conditions of purification are exclusion of light and oxygen
-
DEAE-cellulose column chromatography, Q-Sepharose column chromatography, hydroxyapatite column chromatography, and Superdex 200 gel filtration
-
ammonium sulfate precipitation, phenyl Sepharose column chromatography, and Sephadex G-25 gel filtration
-
-
Kloeckera sp.
-
Cibacron blue 3GA-Sepharose column chromatography
B6VPZ9, -
-
methylotrophic bacterium
-
phenyl Sepharose column chromatography and Sephacryl S-200 gel filtration
O08375
HisTrap column chromatography
-
nickel chelating Sepharose column chromatography
E7RAN7
recombinant enzyme
-
-
Pseudomonas methylica
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
high expression in Escherichia coli using the expression plasmid pFA002
-, Q845T0
production of transgenic Arabidopsis and tobacco plants that overexpress Arabidopsis formate dehydrogenase. The formate dehydrogenase specific activity in the leaf tissue of the transgenic plants increases an average of 4.5-fold for Arabidopsis and 31.5fold for tobacco
-
expressed in Escherichia coli BL21(DE3) cells
-, D6CJK0
expressed in Enterobacter aerogenes strain IAM118
-
expressed in Enterobacter aerogenes strain IAM1183
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli JM109 cells
O13437
expressed in Escherichia coli Rosetta(DE3)-pLysS cells
-
expressed in Escherichia coli; expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells
-
overexpression in Escherichia coli
-
expressed in Escherichia coli
-
expressed in Escherichia coli JM105 cells
-
expressed in Escherichia JM105 cells
Q00498
expressed in Escherichia coli BL21 (DE3) cells; expressed in Escherichia coli BL21 (DE3) cells
A9ZNT8, A9ZNT9, -
expressed in Escherichia coli BL21(DE3) cells
-, E2IQB0
expressed in Escherichia coli BL21(DE3)CodonPlus/pLysS cells
-
expressed in Escherichia coli BL21(DE3) cells
B6VPZ9, -
expressed in Escherichia coli TG1 cells
O08375
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
E7RAN7
highly expressed in Escherichia coli cells using an expression plasmid with the pUC ori and tac promoter
-
wild-type enzyme and mutant enzymes C255S and C255M, expression in Escherichia coli
-
expressed in Saccharomyces cerevisiae strain CEN.PK1001-71C
-
high expression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
D195A
-
increased activity with NADP+, decreased activity with NAD+ compared to the wild type enzyme; 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; reduced activity
D195N
-
increased activity with NADP+, decreased activity with NAD+ compared to the wild type enzyme; 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; reduced activity
D195Q
-
increased activity with NADP+, decreased activity with NAD+ compared to the wild type enzyme; 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; reduced activity
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; 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+); 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/Y196P
-
the double mutant shows an improvement in overall catalytic efficiency with NADP+ and a decrease in the efficiency with NAD+ as cofactors; the double mutant shows increased activity with NADP+, decreased activity with 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; the double mutant shows decreased activity with NADP+ and NAD+ compared to the wild type enzyme
D195S
-
increased activity with NADP+, decreased activity with NAD+ compared to the wild type enzyme; 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; reduced activity
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
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
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+
D195S
-
mutant enzyme also can use NADP+ as coenzyme; 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
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
Q00498
inactive
N300E/N147R
Q00498
inactive
Q105R
Q00498
the mutant shows wild type catalytic efficiency
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
Y302E
Q00498
inactive
Y302R
Q00498
the mutant shows decreased 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 4.3C. The catalytic efficiency for NAD+ is about 2fold higher 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 2.9C. The catalytic efficiency for NAD+ is about 2fold higher 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 7.8C. The catalytic efficiency for NAD+ is slightly decreased 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 54C, 60C, 62C and 65C is decreased compared to wild-type enzyme
E61P
-
rate constant of thermal inactivation at 54C, 60C, 62C and 65C is decreased compared to wild-type enzyme
E61Q
-
rate constant of thermal inactivation at 54C, 60C, 62C and 65C is decreased compared to wild-type enzyme
A198G/D221Q
Mycobacterium vaccae N10
-
the mutant has the highest catalytic efficiency (kcat/Km) with NADP+
-
C145S/A198G/D221Q/C255V
Mycobacterium vaccae N10
-
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
Mycobacterium vaccae N10
-
the mutant shows the highest specific activity for a NADP+-accepting enzyme
-
D221A
Mycobacterium vaccae N10
-
the mutant shows catalytic efficiency with NADP+ as compared to the wild type enzyme
-
D221Q
Mycobacterium vaccae N10
-
the mutant shows catalytic efficiency with NADP+ compared to the wild type enzyme
-
E61K
Mycobacterium vaccae N10
-
rate constant of thermal inactivation at 54C, 60C, 62C and 65C is decreased compared to wild-type enzyme
-
E61P
Mycobacterium vaccae N10
-
rate constant of thermal inactivation at 54C, 60C, 62C and 65C is decreased compared to wild-type enzyme
-
E61Q
Mycobacterium vaccae N10
-
rate constant of thermal inactivation at 54C, 60C, 62C and 65C 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 25C, decrease of thermostability above 45C. 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 25C, decrease of thermostability above 45C. Native enzyme preserves more than 80% of initial activity after 2 h in 7 M urea. The mutant enzyme is completely inactive
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 54C and at 60C is slightly decreased, at 62C, and 65C 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
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; 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; Km-value for formate and Ki-value for azide decreases, KM-value for NAD+ is not affected
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
A191G
-
non-optimal residue located by Ramachandran-plot, mutation has no significant effect on enzyme stability. No significant change in enzyme kinetic properties
-
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
-
K61R
-
rate constant of thermal inactivation at 54C and at 60C is slightly decreased, at 62C, and 65C 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
-
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; 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; Km-value for formate and Ki-value for azide decreases, KM-value for NAD+ is not affected
-
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
-
D196A/Y197R
Q08911
coenzyme preference is shifted from NAD+ to NADP+, decreased thermal stability at 42C
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
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
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
heating converts the native enzyme to the molten globule state and cooling results in formation of a nonnative structure with altered kinetic properties
-
in 4 M guanidine hydrochloride and 20 mM dithiothreitol, 20 mM Tris pH 8, at 25C, for 2 h
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
-
production of NADH from NAD+
synthesis
Arthrobacter sp. KM 62
-
production of NADH from NAD+
-
biotechnology
-
overexpression of the NAD+-dependent formate dehydrogenase in Escherichia coli doubles maximum yield of NADH from 2 to 4 mol NADH/mol glucose consumed
biotechnology
-
study on stability of recombinant enzyme in homogeneous aequeous solution, at gas-liquid interfaces in a bubble column, and under shear stress. Level of enzyme stability in solution also depends on the enzyme variant employed. Mutants C23S and C23S/C262A perform much better than wild-type in quiescent solution and reactors with little mechanical stress. Mutant C23S/C262A is less stable than wild-type at high stress levels in the Couette viscometer or the bubble column
biotechnology
-
FDH from Candida boidinii is an important biocatalyst for the regeneration of the cofactor NADH in industrial enzyme-catalyzed reductions
medicine
-
enzyme-loaded erythrocytes along with equimolar solution of sodium carbonate and hydrogencarbonate facilitate removal of formate in methanol poisoning of folate-deficient rats
medicine
-
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. Coupled enzyme has a longer half-life and lower immunogenicity than native enzyme and a better in vivo efficacy in eliminating formate
analysis
-
enzyme may be used for direct spectrophotometric assay of formate
analysis
Cupriavidus oxalaticus OX
-
enzyme may be used for direct spectrophotometric assay of formate
-
biotechnology
-
use of enzyme for regeneration of NADH. Coexpression of alpha-haloketone resistant enzyme mutants and a carbonyl reductase from Kluyveromyces aestuarii for production of ethyl-(S)-4-chloro-3-hydroxybutanoate with optical purity of product of 99% enantiomeric excess, from ethyl-4-chloroacetoacetate
biotechnology
-
immobilization of enzyme on highly activated glyoxyl agarose, optimization protocol. Optimized enzyme retains 50% of the offered activity and becomes 50times more stable at high temperature and neutral pH. Optimal temperature increases by 10C at pH 4.5. Immobilized enzyme accepts dextran-NAD+ as a substrate, use on ultra-filtration reactors to catalyze the recycling of NAD+
biotechnology
-
immobilization of enzyme on highly activated glyoxyl agarose, optimization protocol. Optimized enzyme retains 50% of the offered activity and becomes 50times more stable at high temperature and neutral pH. Optimal temperature increases by 10C at pH 4.5. Immobilized enzyme accepts dextran-NAD+ as a substrate, use on ultra-filtration reactors to catalyze the recycling of NAD+
-