Information on EC 1.2.7.B2 - formaldehyde ferredoxin oxidoreductase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.2.7.B2
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
formaldehyde ferredoxin oxidoreductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
formaldehyde + H2O + 2 oxidized ferredoxin = formate + 2 H+ + 2 reduced ferredoxin
show the reaction diagram
formaldehyde + H2O + 2 oxidized ferredoxin = formate + 2 reduced ferredoxin + 2 H+
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
formaldehyde:ferredoxin oxidoreductase
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
the enzyme plays a role in peptide fermentation
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetaldehyde + H2O + oxidized benzyl viologen
acetate + H+ + reduced benzyl viologen
show the reaction diagram
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-
-
-
?
acetaldehyde + H2O + oxidized benzyl viologen
acetate + reduced benzyl viologen + H+
show the reaction diagram
-
-
-
?
acetaldehyde + H2O + oxidized methyl viologen
acetate + H+ + reduced methyl viologen
show the reaction diagram
butyraldehyde + H2O + oxidized methyl viologen
butyrate + H+ + reduced methyl viologen
show the reaction diagram
crotonaldehyde + H2O + oxidized methyl viologen
crotonate + reduced methyl viologen + H+
show the reaction diagram
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specific activity is 2.5% compared to the activity with formaldehyde
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-
?
formaldehyde + H2O + 2 oxidized ferredoxin
formate + 2 H+ + 2 reduced ferredoxin
show the reaction diagram
formaldehyde + H2O + 2 oxidized ferredoxin
formate + 2 reduced ferredoxin + 2 H+
show the reaction diagram
formaldehyde is unlikely to be the physiologiocal substrate (Km-value: 25 mM)
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-
?
formaldehyde + H2O + oxidized benzyl viologen
formate + 2 H+ + reduced benzyl viologen
show the reaction diagram
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no activity with methanol or formic acid as substrate
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-
?
formaldehyde + H2O + oxidized benzyl viologen
formate + H+ + reduced benzyl viologen
show the reaction diagram
-
-
-
-
?
formaldehyde + H2O + oxidized benzyl viologen
formate + reduced benzyl viologen + H+
show the reaction diagram
-
-
-
?
formaldehyde + H2O + oxidized methyl viologen
formate + H+ + reduced methyl viologen
show the reaction diagram
formaldehyde + H2O + oxidized methyl viologen
formate + reduced methyl viologen + H+
show the reaction diagram
-
-
-
-
?
glutaric dialdehyde + H2O + oxidized benzyl viologen
? + reduced benzyl viologen + H+
show the reaction diagram
hexanal + H2O + oxidized methyl viologen
hexanoate + reduced methyl viologen + H+
show the reaction diagram
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specific activity is 2% compared to the activity with formaldehyde
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-
?
indole-3-acetaldehyde + H2O + oxidized benzyl viologen
indole-3-acetate + H+ + reduced benzyl viologen
show the reaction diagram
-
-
-
-
?
indole-3-acetaldehyde + H2O + oxidized benzyl viologen
indole-3-acetate + reduced benzyl viologen + H+
show the reaction diagram
-
-
-
?
phenylpropionaldehyde + H2O + oxidized benzyl viologen
phenylpropionate + H+ + reduced benzyl viologen
show the reaction diagram
-
-
-
-
?
phenylpropionaldehyde + H2O + oxidized benzyl viologen
phenylpropionate + reduced benzyl viologen + H+
show the reaction diagram
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-
-
?
propionaldehyde + H2O + oxidized benzyl viologen
propionate + H+ + reduced benzyl viologen
show the reaction diagram
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-
-
-
?
propionaldehyde + H2O + oxidized benzyl viologen
propionate + reduced benzyl viologen + H+
show the reaction diagram
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-
-
?
propionaldehyde + H2O + oxidized methyl viologen
propionate + H+ + reduced methyl viologen
show the reaction diagram
77% compared to the activity with acetyladehyde
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-
?
succinic semialdehyde + H2O + oxidized benzyl viologen
succinate + H+ + reduced benzyl viologen
show the reaction diagram
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-
-
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?
succinic semialdehyde + H2O + oxidized benzyl viologen
succinate + reduced benzyl viologen + H+
show the reaction diagram
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pterin
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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
additional information
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the enzyme contains a pterin cofactor
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Calcium
-
contains approximately 1 W atom, 4 Fe atoms, and 1 Ca atom per subunit
Tungsten
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
arsenite
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5 mM, 50% inhibition after min
cyanide
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5 mM, 50% inhibition after min
glycerol
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60% v/v, 6 h, 60% loss of activity
Glyoxal
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above 1 mM
iodoacetate
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5 mM, 50% inhibition after min
additional information
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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 hide
LITERATURE
IMAGE
Sulfide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
60
acetaldehyde
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80°C, pH 8.4
0.021 - 25
formaldehyde
0.8
glutaric dialdehyde
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80°C, pH 8.4
25
Indole-3-acetaldehyde
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80°C, pH 8.4
0.073
Oxidized benzyl viologen
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pH 8.4, 80°C
0.014 - 0.1
oxidized ferredoxin
15
phenylpropionaldehyde
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80°C, pH 8.4
62
propionaldehyde
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80°C, pH 8.4
8
Succinic semialdehyde
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80°C, pH 8.4
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
44000
acetaldehyde
Pyrococcus furiosus
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80°C, pH 8.4
14 - 71000
formaldehyde
42000
glutaric dialdehyde
Pyrococcus furiosus
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80°C, pH 8.4
2300
Indole-3-acetaldehyde
Pyrococcus furiosus
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80°C, pH 8.4
25000
phenylpropionaldehyde
Pyrococcus furiosus
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80°C, pH 8.4
11000
propionaldehyde
Pyrococcus furiosus
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80°C, pH 8.4
5700
Succinic semialdehyde
Pyrococcus furiosus
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80°C, pH 8.4
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
730
acetaldehyde
Pyrococcus furiosus
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80°C, pH 8.4
90
560 - 3000
formaldehyde
130
60000
glutaric dialdehyde
Pyrococcus furiosus
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80°C, pH 8.4
11299
90
Indole-3-acetaldehyde
Pyrococcus furiosus
-
80°C, pH 8.4
1534
1700
phenylpropionaldehyde
Pyrococcus furiosus
-
80°C, pH 8.4
9675
170
propionaldehyde
Pyrococcus furiosus
-
80°C, pH 8.4
273
710
Succinic semialdehyde
Pyrococcus furiosus
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80°C, pH 8.4
809
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
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pH 8.4, 80°C
58
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pH 8.4, 90°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
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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
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 10
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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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
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gel filtration
68700
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4 * 68700, calculated from sequence
68941
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4 * 68941, calculated from sequence
70000
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4 * 70000, SDS-PAGE
275000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
tetramer
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 hide
LITERATURE
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
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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
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644682
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme from vanadium- and molybdenum-grown cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
approximately invariant expression levels in normal growth versus cold-shock conditions
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