Information on EC 1.2.7.B2 - formaldehyde ferredoxin oxidoreductase

for references in articles please use BRENDA:EC1.2.7.B2
Word Map on EC 1.2.7.B2
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)


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

EC NUMBER
COMMENTARY hide
1.2.7.B2
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
formaldehyde ferredoxin oxidoreductase
-
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
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
formaldehyde:ferredoxin oxidoreductase
-
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
-
-
-
-
?
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
-
specific activity is 2.5% compared to the activity with formaldehyde
-
-
?
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)
-
-
?
formaldehyde + H2O + oxidized benzyl viologen
formate + 2 H+ + reduced benzyl viologen
show the reaction diagram
-
no activity with methanol or formic acid as substrate
-
-
?
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 ferredoxin
formate + H+ + reduced ferredoxin
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
-
specific activity is 2% compared to the activity with formaldehyde
-
-
?
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
-
-
-
?
propionaldehyde + H2O + oxidized benzyl viologen
propionate + H+ + reduced benzyl viologen
show the reaction diagram
-
-
-
-
?
propionaldehyde + H2O + oxidized benzyl viologen
propionate + reduced benzyl viologen + H+
show the reaction diagram
-
-
-
?
propionaldehyde + H2O + oxidized methyl viologen
propionate + H+ + reduced methyl viologen
show the reaction diagram
77% compared to the activity with acetyladehyde
-
-
?
succinic semialdehyde + H2O + oxidized benzyl viologen
succinate + H+ + reduced benzyl viologen
show the reaction diagram
-
-
-
-
?
succinic semialdehyde + H2O + oxidized benzyl viologen
succinate + reduced benzyl viologen + 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
formaldehyde + H2O + oxidized ferredoxin
formate + H+ + reduced ferredoxin
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
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
tungsto-bispterin cofactor
-
-
-
additional information
-
the enzyme contains a pterin cofactor
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Calcium
-
contains approximately 1 W atom, 4 Fe atoms, and 1 Ca atom per subunit
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
arsenite
-
5 mM, 50% inhibition after min
cyanide
-
5 mM, 50% inhibition after min
glycerol
-
60% v/v, 6 h, 60% loss of activity
Glyoxal
-
above 1 mM
iodoacetate
-
5 mM, 50% inhibition after min
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Sulfide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
60
acetaldehyde
-
80°C, pH 8.4
0.021 - 25
formaldehyde
0.8
glutaric dialdehyde
-
80°C, pH 8.4
25
Indole-3-acetaldehyde
-
80°C, pH 8.4
0.073
Oxidized benzyl viologen
-
pH 8.4, 80°C
0.014 - 0.1
oxidized ferredoxin
15
phenylpropionaldehyde
-
80°C, pH 8.4
62
propionaldehyde
-
80°C, pH 8.4
8
Succinic semialdehyde
-
80°C, pH 8.4
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
44000
acetaldehyde
-
80°C, pH 8.4
14 - 71000
formaldehyde
42000
glutaric dialdehyde
-
80°C, pH 8.4
2300
Indole-3-acetaldehyde
-
80°C, pH 8.4
25000
phenylpropionaldehyde
-
80°C, pH 8.4
11000
propionaldehyde
-
80°C, pH 8.4
5700
Succinic semialdehyde
-
80°C, pH 8.4
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
730
acetaldehyde
-
80°C, pH 8.4
560 - 3000
formaldehyde
60000
glutaric dialdehyde
-
80°C, pH 8.4
90
Indole-3-acetaldehyde
-
80°C, pH 8.4
1700
phenylpropionaldehyde
-
80°C, pH 8.4
170
propionaldehyde
-
80°C, pH 8.4
710
Succinic semialdehyde
-
80°C, pH 8.4
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
-
pH 8.4, 80°C
58
-
pH 8.4, 90°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
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
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
assay at
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
-
gel filtration
68700
-
4 * 68700, calculated from sequence
68941
-
4 * 68941, calculated from sequence
69072
-
tandem mass spectrometry
70000
-
4 * 70000, SDS-PAGE
275000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 69072, tandem mass spectrometry
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
-
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
-
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme from vanadium- and molybdenum-grown cells
-
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
-