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Information on EC 1.2.7.B2 - formaldehyde ferredoxin oxidoreductase
for references in articles please use BRENDA:EC1.2.7.B2preliminary BRENDA-supplied EC number
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EC Tree
1.2.7.B2 formaldehyde ferredoxin oxidoreductaseSpecify your search results
Word Map
- 1.2.7.B2
- tungsten
-
pyrococcus
- furiosus
-
tungsten-containing
-
hyperthermophilic
- archaeon
-
tungstoenzymes
-
iron-sulfur
- pterins
-
homotetramer
- litoralis
-
thermococcus
-
two-electron
- glyceraldehyde-3-phosphate
- methyloversatilis
- wiv
- methylamine
- cubane
-
pqq-dependent
-
mxafi
-
five-member
- molybdenum
-
calvin
- nitrogenase
- universalis
-
lake
- glutarate
-
washington
-
methylotrophic
- thermotolerans
-
formic
-
monoamine
- n-methylglutamate
- rhodocyclaceae
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two-subunit
-
quinohemoprotein
-
dye-mediated
-
tungsten-dependent
-
low-potential
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
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+
2
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+
2
+
2
+
+
2
=
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2
+
2
Synonyms
formaldehyde ferredoxin oxidoreductase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
FOR
formaldehyde ferredoxin oxidoreductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
formaldehyde + H2O + 2 oxidized ferredoxin = formate + 2 reduced ferredoxin + 2 H+
-
-
-
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formaldehyde + H2O + 2 oxidized ferredoxin = formate + 2 H+ + 2 reduced ferredoxin
a mechanism is proposed in which the formaldehyde substrate binds directly to the tungsten ion. W(VI)=O then performs a nucleophilic attack on the formaldehyde carbon to form a tetrahedral intermediate. In the second step, which is calculated to be rate limiting, a proton is transferred to the second-shell Glu308 residue, coupled with a two-electron reduction of the tungsten ion
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formaldehyde + H2O + 2 oxidized ferredoxin = formate + 2 H+ + 2 reduced ferredoxin
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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
formaldehyde:ferredoxin oxidoreductase
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetaldehyde + H2O + oxidized benzyl viologen
acetate + H+ + reduced benzyl viologen
-
-
-
?
acetaldehyde + H2O + oxidized benzyl viologen
acetate + reduced benzyl viologen + H+
-
-
-
?
crotonaldehyde + H2O + oxidized methyl viologen
crotonate + reduced methyl viologen + H+
-
specific activity is 2.5% compared to the activity with formaldehyde
-
-
?
formaldehyde + H2O + 2 oxidized ferredoxin
formate + 2 reduced ferredoxin + 2 H+
formaldehyde is unlikely to be the physiologiocal substrate (Km-value: 25 mM)
-
-
?
formaldehyde + H2O + 2 oxidized methyl viologen
formate + 2 reduced methyl viologen + 2 H+
-
-
-
?
formaldehyde + H2O + oxidized benzyl viologen
formate + 2 H+ + reduced benzyl viologen
no activity with methanol or formic acid as substrate
-
-
?
hexanal + H2O + oxidized methyl viologen
hexanoate + reduced methyl viologen + H+
-
specific activity is 2% compared to the activity with formaldehyde
-
-
?
indole-3-acetaldehyde + H2O + oxidized benzyl viologen
indole-3-acetate + H+ + reduced benzyl viologen
-
-
-
?
indole-3-acetaldehyde + H2O + oxidized benzyl viologen
indole-3-acetate + reduced benzyl viologen + H+
-
-
-
?
phenylpropionaldehyde + H2O + oxidized benzyl viologen
phenylpropionate + H+ + reduced benzyl viologen
-
-
-
?
phenylpropionaldehyde + H2O + oxidized benzyl viologen
phenylpropionate + reduced benzyl viologen + H+
-
-
-
?
propionaldehyde + H2O + oxidized benzyl viologen
propionate + H+ + reduced benzyl viologen
-
-
-
?
propionaldehyde + H2O + oxidized benzyl viologen
propionate + reduced benzyl viologen + H+
-
-
-
?
propionaldehyde + H2O + oxidized methyl viologen
propionate + H+ + reduced methyl viologen
77% compared to the activity with acetyladehyde
-
-
?
succinic semialdehyde + H2O + oxidized benzyl viologen
succinate + H+ + reduced benzyl viologen
-
-
-
?
succinic semialdehyde + H2O + oxidized benzyl viologen
succinate + reduced benzyl viologen + H+
-
-
-
?
acetaldehyde + H2O + oxidized methyl viologen
acetate + H+ + reduced methyl viologen
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-
-
?
acetaldehyde + H2O + oxidized methyl viologen
acetate + H+ + reduced methyl viologen
-
-
-
?
butyraldehyde + H2O + oxidized methyl viologen
butyrate + H+ + reduced methyl viologen
10% compared to the activity with acetyladehyde
-
-
?
butyraldehyde + H2O + oxidized methyl viologen
butyrate + H+ + reduced methyl viologen
10% compared to the activity with acetyladehyde
-
-
?
formaldehyde + H2O + 2 oxidized ferredoxin
formate + 2 H+ + 2 reduced ferredoxin
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-
-
?
formaldehyde + H2O + 2 oxidized ferredoxin
formate + 2 H+ + 2 reduced ferredoxin
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-
-
?
formaldehyde + H2O + 2 oxidized ferredoxin
formate + 2 H+ + 2 reduced ferredoxin
-
-
-
?
formaldehyde + H2O + 2 oxidized ferredoxin
formate + 2 H+ + 2 reduced ferredoxin
-
-
-
?
formaldehyde + H2O + oxidized benzyl viologen
formate + H+ + reduced benzyl viologen
-
-
-
?
formaldehyde + H2O + oxidized benzyl viologen
formate + H+ + reduced benzyl viologen
-
-
-
-
?
formaldehyde + H2O + oxidized benzyl viologen
formate + H+ + reduced benzyl viologen
-
-
-
?
formaldehyde + H2O + oxidized benzyl viologen
formate + reduced benzyl viologen + H+
-
-
-
?
formaldehyde + H2O + oxidized benzyl viologen
formate + reduced benzyl viologen + H+
-
-
-
?
formaldehyde + H2O + oxidized ferredoxin
formate + H+ + reduced ferredoxin
-
-
-
-
?
formaldehyde + H2O + oxidized ferredoxin
formate + H+ + reduced ferredoxin
-
-
-
-
?
formaldehyde + H2O + oxidized ferredoxin
formate + H+ + reduced ferredoxin
-
-
-
-
?
formaldehyde + H2O + oxidized ferredoxin
formate + H+ + reduced ferredoxin
-
-
-
-
?
formaldehyde + H2O + oxidized methyl viologen
formate + H+ + reduced methyl viologen
63% compared to the activity with acetyladehyde
-
-
?
formaldehyde + H2O + oxidized methyl viologen
formate + H+ + reduced methyl viologen
63% compared to the activity with acetyladehyde
-
-
?
formaldehyde + H2O + oxidized methyl viologen
formate + reduced methyl viologen + H+
-
-
-
-
?
formaldehyde + H2O + oxidized methyl viologen
formate + reduced methyl viologen + H+
-
-
-
?
glutaric dialdehyde + H2O + oxidized benzyl viologen
? + reduced benzyl viologen + H+
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-
-
?
glutaric dialdehyde + H2O + oxidized benzyl viologen
? + reduced benzyl viologen + H+
best substrate, C5- or C6-type aldehydes might be physiologically relevant substrates
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-
?
additional information
?
-
low activity with butyraldehyde, crotonaldehyde, no activity with: isovaleraldehyde, benzaldehyde, salicaldehyde, 2-furfuraldehyde. It does not oxidize lactate, 2-hydroxybutyrate, 2-hydroxyvalerate, 2-hydroxycaproate, or 1-ethyl-2-hydroxycaproate and it does not reduce pyruvate, 2-oxobutyrate, 2-oxovalerate, 1-ethyl-3-oxovalerate, 1-ethyl-4-oxovalerate, or 2-oxocaproate
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-
?
additional information
?
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-
low activity with butyraldehyde, crotonaldehyde, no activity with: isovaleraldehyde, benzaldehyde, salicaldehyde, 2-furfuraldehyde. It does not oxidize lactate, 2-hydroxybutyrate, 2-hydroxyvalerate, 2-hydroxycaproate, or 1-ethyl-2-hydroxycaproate and it does not reduce pyruvate, 2-oxobutyrate, 2-oxovalerate, 1-ethyl-3-oxovalerate, 1-ethyl-4-oxovalerate, or 2-oxocaproate
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-
?
additional information
?
-
no activity with crotonaldehyde, benzaldehyde, isovalerylaldehyde or phenylacetaldehyde
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-
?
additional information
?
-
activity with crotonaldehyde is less than 10% compared to activity with acetaldehyde: crotonaldehyde, benzaldehyde, phenylacetaldehyde
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-
?
additional information
?
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activity with crotonaldehyde is less than 10% compared to activity with acetaldehyde: crotonaldehyde, benzaldehyde, phenylacetaldehyde
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-
?
additional information
?
-
activity with crotonaldehyde is less than 10% compared to activity with acetaldehyde: crotonaldehyde, benzaldehyde, phenylacetaldehyde
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
formaldehyde + H2O + oxidized ferredoxin
formate + H+ + reduced ferredoxin
-
-
-
-
?
formaldehyde + H2O + oxidized ferredoxin
formate + H+ + reduced ferredoxin
-
-
-
-
?
formaldehyde + H2O + oxidized ferredoxin
formate + H+ + reduced ferredoxin
-
-
-
-
?
formaldehyde + H2O + oxidized ferredoxin
formate + H+ + reduced ferredoxin
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pterin
an electron transfer pathway is proposed that begins at the tungsten center, leads to the (4Fe-4S) cluster of formaldehyde ferredoxin oxidoreductase via one of the two pterins that coordinate the tungsten, and ends at the (4Fe-4S) cluster of ferredoxin. This pathway includes two residues that coordinate the (4Fe4S) clusters, Cys287 of FOR and Asp14 of ferredoxin
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Calcium
contains approximately 1 W atom, 4 Fe atoms, and 1 Ca atom per subunit
Iron
Mo5+
molybdenum can be incorporated, Mo(V) signal is observed in electron paramagnetic resonance. Aldehyde oxidation activity correlates only with the residual tungsten content. This suggests that the Mo-containing enzymes are most likely inactive. An intracellular selection mechanism for tungstate and molybdate processing has to be present, since tungsten is found to be preferentially incorporated even under conditions with comparable intracellular concentrations of tungstate and molybdate
Tungsten
Iron
an electron transfer pathway is proposed that begins at the tungsten center, leads to the (4Fe-4S) cluster of formaldehyde ferredoxin oxidoreductase via one of the two pterins that coordinate the tungsten, and ends at the (4Fe-4S) cluster of ferredoxin. This pathway includes two residues that coordinate the (4Fe-4S) clusters, Cys287 of FOR and Asp14 of ferredoxin
Iron
contains approximately 1 W atom, 4 Fe atoms, and 1 Ca atom per subunit
Iron
the enzyme contains 16.0 gatom of iron per 280000 Da g of enzyme. Each subunit of dithionite reduced enzyme contains a magnetically isolated [4Fe-4S]1+ cluster that exists in both the S = 3/2 and S = 1/2 states
Tungsten
an electron transfer pathway is proposed that begins at the tungsten center, leads to the (4Fe-4S) cluster of formaldehyde ferredoxin oxidoreductase via one of the two pterins that coordinate the tungsten, and ends at the (4Fe-4S) cluster of ferredoxin. This pathway includes two residues that coordinate the (4Fe-4S) clusters, Cys287 of FOR and Asp14 of ferredoxin
Tungsten
-
the enzyme from Pyrococcus furiosus uses exclusively tungsten to synthesize the catalytically active forms of formaldehyde ferredoxin oxidoreductase and active molybdenum- or vanadium-containing isoenzymes are not expressed when the cells are grown in the presence of these other metals
Tungsten
the tungsten in the active enzyme is a two-electron acceptor, W(VI/IV)
Tungsten
tungsten-containing enzyme. The enzyme contains approximately 1 W atom, 4 Fe atoms, and 1 Ca atom per subunit
Tungsten
-
tungsten-dependent enzyme, no activity when tungsten is replaced by molybdenum
Tungsten
-
tungsten-dependent enzyme. A mechanism is proposed in which the formaldehyde substrate binds directly to the tungsten ion. W(VI)=O then performs a nucleophilic attack on the formaldehyde carbon to form a tetrahedral intermediate. In the second step, which is calculated to be rate limiting, a proton is transferred to the second-shell Glu308 residue, coupled with a two-electron reduction of the tungsten ion
Tungsten
a W(VI) species with terminal sulfido or thiol ligands is proposed to be responsible for the catalytic activity in sulfide-activated samples of formaldehyde ferredoxin oxidoreductase
Tungsten
tungsten-containing enzyme. The enzyme contains 3.3 gatom of tungsten per 280000 Da g of enzyme
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
the enzyme is not inhibited when it is incubated for up to 24 h with iodoacetate, arsenite, or cyanide (each at a concentration of 5 mM) prior to being assayed under standard conditions in the absence of these reagents
-
additional information
-
the enzyme is not inhibited when it is incubated for up to 24 h with iodoacetate, arsenite, or cyanide (each at a concentration of 5 mM) prior to being assayed under standard conditions in the absence of these reagents
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Sulfide
activated up to fivefold by treatment with sulfide under reducing conditions
Sulfide
incubation of the enzyme (14 mg/ml) in 100 mM Tris/HCl (pH 8.0) buffer with excess sodium sulfide (20 mM) under anaerobic conditions leads to an enhancement of the specific activity by 40%
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.021
formaldehyde
pH 8.4, 80°C, with ferredoxin as electron acceptor
0.071
formaldehyde
pH 8.4, 80°C, with benzyl viologen as electron acceptor
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
the activity of the pure enzyme with benzyl viologen as the electron acceptor increases linearly with pH over the pH range 5.5 (1.5 U/mg) to 10.0 (55 U/mg) at 80°C
8.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 10
the activity of the pure enzyme with benzyl viologen as the electron acceptor increases linearly with pH over the pH range 5.5 (1.5 U/mg) to 10.0 (55 U/mg) at 80°C
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
enzyme exhibits a significant primary kinetic isotope effect of the apparent Vmax for the deuterated substrate, formaldehyde-d2, which shows that the rate-determining step involves a C-H bond break from the aldehyde
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). FOR_THELN
Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)
621
0
68941
Swiss-Prot
-
Q8U1K3_PYRFU
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
627
0
69679
TrEMBL
other Location (Reliability: 5)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
tetramer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the enzyme is crystallized at room temperature under an argon atmosphere using a modification of the melting-point capillary method in the native state and as a complex with the inhibitor glutarate at 1.85 A and 2.4 A resolution. The binding site on formaldehyde ferredoxin oxidoreductase for the physiological electron acceptor, Pyrococcus furiosus ferredoxin is established from an formaldehyde ferredoxin oxidoreductase/ferredoxin cocrystal structure
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme as purified under standard conditions is oxygen sensitive, with the t50% being about 12 h when the enzyme is exposed to air. No activity is lost under anaerobic conditions
644689
the sensitivity to inactivation by O2, of formaldehyde ferredoxin oxidoreductase in the purified state is similar to that of the cell-free extract. That is, when the enzyme (5.0 mg/ml) as isolated under reducing conditions is briefly shaken in air to oxidize the sodium dithionite and then left exposed at 23°C, 50% of the original activity is lost after 5 h
644682
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
activity decreases significantly when the organism is grown on maltose plus S(0)
approximately invariant expression levels in normal growth versus cold-shock conditions
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mukund, S.; Adams, M.W.
Characterization of a novel tungsten-containing formaldehyde ferredoxin oxidoreductase from the hyperthermophilic archaeon, Thermococcus litoralis. A role for tungsten in peptide catabolism
J. Biol. Chem.