Information on EC 1.2.1.43 - formate dehydrogenase (NADP+)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.2.1.43
-
RECOMMENDED NAME
GeneOntology No.
formate dehydrogenase (NADP+)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
formate + NADP+ = CO2 + NADPH
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Carbon fixation pathways in prokaryotes
-
-
carbon tetrachloride degradation II
-
-
Metabolic pathways
-
-
Methane metabolism
-
-
Microbial metabolism in diverse environments
-
-
reductive acetyl coenzyme A pathway I (homoacetogenic bacteria)
-
-
reductive acetyl coenzyme A pathway
-
-
SYSTEMATIC NAME
IUBMB Comments
formate:NADP+ oxidoreductase
A tungsten-selenium-iron protein.
CAS REGISTRY NUMBER
COMMENTARY hide
51377-43-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CO2 + NADPH
formate + NADP+
show the reaction diagram
formate + NAD+
CO2 + NADH + H+
show the reaction diagram
formate + NADP+
CO2 + NADPH + H+
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
CO2 + NADPH
formate + NADP+
show the reaction diagram
-
first enzyme in pathway of reduction of CO2 to acetate: CO2 serves as electron acceptor generated during fermentation
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Molybdenum
selenium
Tungsten
additional information
-
activity of enzyme in growing cells is enhanced when selenite and molybdate are added together to the growth medium, tungstate replaces and is better than molybdate, 75Se-selenite is incorporated into protein fraction
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-Butanedione
5,5'-dithio-bis(2-nitrobenzoic acid)
complete inhibition at 1 mM
AgNO3
complete inhibition at 1 mM
azide
-
competitive inhibitor
CdCl2
slight inhibition at 1 mM
CoCl2
slight inhibition at 1 mM
CuSO4
slight inhibition at 1 mM
cyanide
FeCl2
complete inhibition at 1 mM
FeSO4
HgCl2
complete inhibition at 1 mM
hydroxylamine
slight inhibition at 10 mM
Hypophosphite
mercaptoethanol
-
-
NADP+
-
substrate inhibition at 5 mM or higher concentration
NaNO3
slight inhibition at 1 mM
Sodium azide
complete inhibition at 1 mM
Sodium selenite
-
0.01 M
sulfite
-
inhibition of activity with NADP+ but not with methyl viologen
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
sulfhydryl compounds
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.083 - 55.5
formate
2.35
methyl viologen
-
-
0.06 - 1.43
NAD+
0.11 - 0.83
NADP+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.25 - 1.66
NAD+
0.13 - 4.75
NADP+
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.16 - 20
NAD+
7
0.16 - 30
NADP+
10
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.4
crude enzyme, in 1 M potassium phosphate buffer (pH 7.0), at 30°C
5.3
after 3.8fold purification, in 1 M potassium phosphate buffer (pH 7.0), at 30°C
113
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methyl viologen as electron acceptor
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9.5
7
-
broad, CO2 reduction
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
-
formate + NADP+
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
low activity below
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
8 * 42000, SDS-PAGE
76000
-
alpha2 beta2, 2 * 96000 + 2 * 76000 SDS-PAGE
96000
-
alpha2 beta2, 2 * 96000 + 2 * 76000 SDS-PAGE
270000 - 300000
340000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homooctamer
tetramer
-
alpha2 beta2, 2 * 96000 + 2 * 76000 SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 12
more than 94% of the initial activity is retained at pH 5.0-12.0 after incubation for 30 min at 30°C
711869
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
mutant FDH, 1 year, no loss of activity
25
-
mutant FDH, 7 days, no decrease of activity
55 - 60
no loss of activity is observed at 55°C for 10 h, but about half of the enzyme activity is lost after incubation for 36 h. The enzyme can maintain a 50% activity for at least 5 h when it is incubated at 60°C
73
-
10 min, 60% loss of activity
76
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10 min, 90% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
azide stabilizes during purification
-
dithionite stabilizes during purification
-
glycerol stabilizes during purification
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
extremely oxygen-sensitive
-
288219, 288220, 288221, 288223, 288224
rapid inactivation by air, thiol-iron complexes and formate stabilize
-
288217, 288223
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, anaerobic conditions, glycerol, ammonium sulfate, 45 days, 35% loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE-Toyopearl column chromatography and butyl-Toyopearl 650M column chromatography
large scale production in Escherichia coli; recombinant protein, expressed in Escherichia coli
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recombinant protein, expressed in Escherichia coli
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis