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2-aminobenzaldehyde + H2O + 2 oxidized benzyl viologen
2-aminobenzoate + 2 H+ + 2 reduced benzyl viologen
4-hydroxybenzaldehyde + H2O + 2 oxidized benzyl viologen
4-hydroxybenzoate + 2 H+ + 2 reduced benzyl viologen
acetaldehyde + H2O + 2 NAD+
acetate + 2 NADH + 2 H+
acetaldehyde + H2O + 2 oxidized benzyl viologen
acetate + 2 H+ + 2 reduced benzyl viologen
acetaldehyde + H2O + oxidized benzyl viologen
acetate + H+ + reduced benzyl viologen
acetaldehyde + H2O + oxidized benzyl viologen
acetate + reduced benzyl viologen
-
at 5% of the activity with crotonaldehyde
-
-
?
acetaldehyde + H2O + oxidized ferredoxin
acetate + H+ + reduced ferredoxin
acetate + H+ + reduced ferredoxin
acetaldehyde + H2O + oxidized ferredoxin
acetate + H+ + reduced methyl viologen
acetaldehyde + H2O + oxidized methyl viologen
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
benzaldehyde + H2O + 2 FAD
benzoate + 2 FADH2
-
-
-
?
benzaldehyde + H2O + 2 NAD+
benzoate + 2 NADH + 2 H+
-
-
-
?
benzaldehyde + H2O + 2 oxidized benzyl viologen
benzoate + 2 H+ + 2 reduced benzyl viologen
-
-
-
?
benzaldehyde + H2O + oxidized benzyl viologen
benzoate + H+ + reduced benzyl viologen
-
144% activity compared to phenylacetaldehyde
-
-
?
benzaldehyde + H2O + oxidized benzyl viologen
benzoate + reduced benzyl viologen
-
at 149% of the activity with crotonaldehyde
-
-
?
benzaldehyde + H2O + oxidized benzyl viologen
benzoic acid + H+ + reduced benzyl viologen
benzaldehyde + H2O + oxidized ferredoxin
benzoic acid + H+ + reduced ferredoxin
-
-
-
-
?
benzoate + Ti(III) citrate + 2 H+
benzaldehyde + Ti(I) citrate + H2O
-
-
-
?
butyraldehyde + H2O + oxidized benzyl viologen
butanoate + H+ + reduced benzyl viologen
-
-
-
?
butyraldehyde + H2O + oxidized ferredoxin
butyrate + H+ + reduced ferredoxin
cinnamaldehyde + H2O + oxidized benzyl viologen
cinnamate + reduced benzyl viologen
-
at 139% of the activity with crotonaldehyde
-
-
?
crotonaldehyde + CoA + 2 oxidized ferredoxin
crotonate + CO2 + 2 reduced ferredoxin + 2 H+
-
the ability of the 4Fe-ferredoxin to accept electrons is not absolutely dependent upon Asp14 (of ferredoxin), as this residue can be effectively replaced by Cys. However, the efficiency of electron transfer is compromised if Asp14 is replaced by Ser, or if the 4Fe-cluster is converted to the 3Fe-form, but Asp14 does not appear to offer any kinetic advantage over the expected Cys
-
-
?
crotonaldehyde + H2O + 2 NAD+
crotonate + 2 NADH + 2 H+
-
-
-
?
crotonaldehyde + H2O + 2 oxidized benzyl viologen
crotonate + 2 H+ + 2 reduced benzyl viologen
-
-
-
?
crotonaldehyde + H2O + oxidized benzyl viologen
crotonate + H+ + reduced benzyl viologen
crotonaldehyde + H2O + oxidized benzyl viologen
crotonate + reduced benzyl viologen
-
-
-
-
?
crotonaldehyde + H2O + oxidized benzyl viologen
crotonate + reduced benzyl viologen + H+
-
-
-
?
crotonaldehyde + H2O + oxidized ferredoxin
crotonate + H+ + reduced ferredoxin
crotonaldehyde + H2O + oxidized ferredoxin
crotonate + reduced ferredoxin
crotonaldehyde + H2O + oxidized methyl viologen
crotonate + H+ + reduced methyl viologen
crotonaldehyde + H2O + oxidized methyl viologen
crotonate + reduced methyl viologen + H+
-
-
-
?
formaldehyde + H2O + 2 oxidized benzyl viologen
formate + 2 H+ + 2 reduced benzyl viologen
-
-
-
?
formaldehyde + H2O + oxidized benzyl viologen
formate + H+ + reduced benzyl viologen
formaldehyde + H2O + oxidized benzyl viologen
formate + reduced benzyl viologen
-
-
-
-
?
formaldehyde + H2O + oxidized ferredoxin
formate + H+ + reduced ferredoxin
formaldehyde + H2O + oxidized methyl viologen
formate + H+ + reduced methyl viologen
-
specific activity is 17% compared to the activity with crotonaldehyde
-
-
?
glutaraldehyde + H2O + oxidized methyl viologen
glutarate + H+ + reduced methyl viologen
-
-
-
?
glutardialdehyde + H2O + 2 oxidized benzyl viologen
?
-
-
-
?
glutardialdehyde + H2O + oxidized benzyl viologen
? + H+ + reduced benzyl viologen
-
111% activity compared to phenylacetaldehyde
-
-
?
glutaric dialdehyde + H2O + oxidized benzyl viologen
?
-
formaldehyde ferredoxin oxidoreductase
-
-
ir
glyceraldehyde + H2O + 2 oxidized benzyl viologen
glycerate + 2 H+ + 2 reduced benzyl viologen
-
-
-
?
glyceraldehyde + H2O + oxidized ferredoxin
glycerate + H+ + reduced ferredoxin
glyceraldehyde + H2O + oxidized methyl viologen
glycerate + H+ + reduced methyl viologen
glyceraldehyde 3-phosphate + H2O + oxidized ferredoxin
glycerate 3-phosphate + H+ + reduced ferredoxin
hexanal + H2O + oxidized methyl viologen
hexanoate + H+ + reduced methyl viologen
-
specific activity is 5.7% compared to the activity with crotonaldehyde
-
-
?
indoleacetaldehyde + H2O + oxidized benzyl viologen
indoleacetate + H+ + reduced benzyl viologen
isobutyraldehyde + H2O + oxidized benzyl viologen
isobutanoate + H+ + reduced benzyl viologen
-
-
-
?
isovalerylaldehyde + H2O + oxidized benzyl viologen
isovalerate + H+ + reduced benzyl viologen
phenylacetaldehyde + H2O + 2 NAD+
phenylacetate + 2 NADH + 2 H+
-
-
-
?
phenylacetaldehyde + H2O + 2 oxidized benzyl viologen
phenylacetate + 2 H+ + 2 reduced benzyl viologen
-
-
-
?
phenylacetaldehyde + H2O + oxidized benzyl viologen
phenylacetate + H+ + reduced benzyl viologen
phenylacetaldehyde + H2O + oxidized ferredoxin
phenylacetate + H+ + reduced ferredoxin
-
-
-
-
?
phenylpropionaldehyde + H2O + oxidized benzyl viologen
phenylpropanoate + H+ + reduced benzyl viologen
propionaldehyde + H2O + 2 oxidized benzyl viologen
propionate + 2 H+ + 2 reduced benzyl viologen
-
-
-
?
propionaldehyde + H2O + oxidized benzyl viologen
propanoate + H+ + reduced benzyl viologen
-
-
-
?
propionaldehyde + H2O + oxidized benzyl viologen
propionate + H+ + reduced benzyl viologen
propionaldehyde + H2O + oxidized ferredoxin
propionate + H+ + reduced ferredoxin
salicylaldehyde + H2O + oxidized benzyl viologen
salicylic acid + H+ + reduced benzyl viologen
-
-
-
-
ir
succinic semialdehyde + H2O + oxidized benzyl viologen
succinic acid + H+ + reduced benzyl viologen
additional information
?
-
2-aminobenzaldehyde + H2O + 2 oxidized benzyl viologen
2-aminobenzoate + 2 H+ + 2 reduced benzyl viologen
-
-
-
?
2-aminobenzaldehyde + H2O + 2 oxidized benzyl viologen
2-aminobenzoate + 2 H+ + 2 reduced benzyl viologen
-
-
-
?
4-hydroxybenzaldehyde + H2O + 2 oxidized benzyl viologen
4-hydroxybenzoate + 2 H+ + 2 reduced benzyl viologen
-
-
-
?
4-hydroxybenzaldehyde + H2O + 2 oxidized benzyl viologen
4-hydroxybenzoate + 2 H+ + 2 reduced benzyl viologen
-
-
-
?
acetaldehyde + H2O + 2 NAD+
acetate + 2 NADH + 2 H+
-
-
-
?
acetaldehyde + H2O + 2 NAD+
acetate + 2 NADH + 2 H+
-
-
-
?
acetaldehyde + H2O + 2 oxidized benzyl viologen
acetate + 2 H+ + 2 reduced benzyl viologen
-
-
-
?
acetaldehyde + H2O + 2 oxidized benzyl viologen
acetate + 2 H+ + 2 reduced benzyl viologen
-
-
-
?
acetaldehyde + H2O + oxidized benzyl viologen
acetate + H+ + reduced benzyl viologen
-
52% activity compared to phenylacetaldehyde
-
-
?
acetaldehyde + H2O + oxidized benzyl viologen
acetate + H+ + reduced benzyl viologen
-
formaldehyde ferredoxin oxidoreductase
-
ir
acetaldehyde + H2O + oxidized benzyl viologen
acetate + H+ + reduced benzyl viologen
formaldehyde ferredoxin oxidoreductase
-
ir
acetaldehyde + H2O + oxidized benzyl viologen
acetate + H+ + reduced benzyl viologen
-
-
-
?
acetaldehyde + H2O + oxidized benzyl viologen
acetate + H+ + reduced benzyl viologen
-
formaldehyde ferredoxin oxidoreductase
-
ir
acetaldehyde + H2O + oxidized benzyl viologen
acetate + H+ + reduced benzyl viologen
-
-
-
ir
acetaldehyde + H2O + oxidized benzyl viologen
acetate + H+ + reduced benzyl viologen
-
-
-
ir
acetaldehyde + H2O + oxidized benzyl viologen
acetate + H+ + reduced benzyl viologen
-
-
-
ir
acetaldehyde + H2O + oxidized ferredoxin
acetate + H+ + reduced ferredoxin
-
-
-
-
?
acetaldehyde + H2O + oxidized ferredoxin
acetate + H+ + reduced ferredoxin
-
-
-
ir
acetaldehyde + H2O + oxidized ferredoxin
acetate + H+ + reduced ferredoxin
-
formaldehyde ferredoxin oxidoreductase
-
ir
acetaldehyde + H2O + oxidized ferredoxin
acetate + H+ + reduced ferredoxin
-
best substrate
-
ir
acetate + H+ + reduced ferredoxin
acetaldehyde + H2O + oxidized ferredoxin
-
-
-
-
?
acetate + H+ + reduced ferredoxin
acetaldehyde + H2O + oxidized ferredoxin
-
-
-
?
acetate + H+ + reduced ferredoxin
acetaldehyde + H2O + oxidized ferredoxin
-
-
-
-
?
acetate + H+ + reduced ferredoxin
acetaldehyde + H2O + oxidized ferredoxin
-
-
-
-
?
acetate + H+ + reduced methyl viologen
acetaldehyde + H2O + oxidized methyl viologen
-
very low activity
-
ir
acetate + H+ + reduced methyl viologen
acetaldehyde + H2O + oxidized methyl viologen
-
below pH 6.0
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
-
-
?
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
-
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
-
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
-
-
?
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
-
-
?
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
-
-
?
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
-
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
-
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
-
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
-
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
formaldehyde ferredoxin oxidoreductase, C1-C3 aldehydes
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
formaldehyde ferredoxin oxidoreductase, C1-C3 aldehydes
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
formaldehyde ferredoxin oxidoreductase, enzyme plays a role in peptide fermentation in hyperthermophilic archaea
-
?
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
-
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
formaldehyde ferredoxin oxidoreductase, enzyme plays a role in peptide fermentation in hyperthermophilic archaea
-
?
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
-
-
?
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
-
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
-
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
enzyme oxidizes aldehydes generated during amino acid catabolism
-
-
?
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
-
-
-
?, ir
benzaldehyde + H2O + oxidized benzyl viologen
benzoic acid + H+ + reduced benzyl viologen
-
no activity
-
-
?
benzaldehyde + H2O + oxidized benzyl viologen
benzoic acid + H+ + reduced benzyl viologen
-
-
-
-
ir
butyraldehyde + H2O + oxidized ferredoxin
butyrate + H+ + reduced ferredoxin
-
-
-
ir
butyraldehyde + H2O + oxidized ferredoxin
butyrate + H+ + reduced ferredoxin
-
low activity
-
ir
butyraldehyde + H2O + oxidized ferredoxin
butyrate + H+ + reduced ferredoxin
-
formaldehyde ferredoxin oxidoreductase
-
ir
crotonaldehyde + H2O + oxidized benzyl viologen
crotonate + H+ + reduced benzyl viologen
-
48% activity compared to phenylacetaldehyde
-
-
?
crotonaldehyde + H2O + oxidized benzyl viologen
crotonate + H+ + reduced benzyl viologen
-
-
-
ir
crotonaldehyde + H2O + oxidized benzyl viologen
crotonate + H+ + reduced benzyl viologen
-
-
-
?
crotonaldehyde + H2O + oxidized benzyl viologen
crotonate + H+ + reduced benzyl viologen
-
low activity, formaldehyde ferredoxin oxidoreductase
-
-
ir
crotonaldehyde + H2O + oxidized benzyl viologen
crotonate + H+ + reduced benzyl viologen
-
no activity
-
-
?
crotonaldehyde + H2O + oxidized benzyl viologen
crotonate + H+ + reduced benzyl viologen
-
-
-
-
ir
crotonaldehyde + H2O + oxidized benzyl viologen
crotonate + H+ + reduced benzyl viologen
-
-
-
-
ir
crotonaldehyde + H2O + oxidized ferredoxin
crotonate + H+ + reduced ferredoxin
-
best substrate
-
-
ir
crotonaldehyde + H2O + oxidized ferredoxin
crotonate + H+ + reduced ferredoxin
-
-
-
-
r
crotonaldehyde + H2O + oxidized ferredoxin
crotonate + reduced ferredoxin
-
utilizes a 7Fe ferredoxin as the putative physiological redox partner, instead of a 4Fe ferredoxin as in Pyrococcus furiosus, 17% of the activity with benzyl viologen
-
-
?
crotonaldehyde + H2O + oxidized ferredoxin
crotonate + reduced ferredoxin
-
-
-
-
?
crotonaldehyde + H2O + oxidized methyl viologen
crotonate + H+ + reduced methyl viologen
-
-
-
-
?
crotonaldehyde + H2O + oxidized methyl viologen
crotonate + H+ + reduced methyl viologen
-
artifical electron acceptor
-
-
ir
formaldehyde + H2O + oxidized benzyl viologen
formate + H+ + reduced benzyl viologen
-
26% activity compared to phenylacetaldehyde
-
-
?
formaldehyde + H2O + oxidized benzyl viologen
formate + H+ + reduced benzyl viologen
-
formaldehyde ferredoxin oxidoreductase
-
ir
formaldehyde + H2O + oxidized benzyl viologen
formate + H+ + reduced benzyl viologen
formaldehyde ferredoxin oxidoreductase
-
ir
formaldehyde + H2O + oxidized benzyl viologen
formate + H+ + reduced benzyl viologen
-
formaldehyde ferredoxin oxidoreductase
-
ir
formaldehyde + H2O + oxidized benzyl viologen
formate + H+ + reduced benzyl viologen
-
-
-
ir
formaldehyde + H2O + oxidized benzyl viologen
formate + H+ + reduced benzyl viologen
-
-
-
ir
formaldehyde + H2O + oxidized benzyl viologen
formate + H+ + reduced benzyl viologen
-
-
-
ir
formaldehyde + H2O + oxidized ferredoxin
formate + H+ + reduced ferredoxin
-
-
-
ir
formaldehyde + H2O + oxidized ferredoxin
formate + H+ + reduced ferredoxin
-
-
-
?
formaldehyde + H2O + oxidized ferredoxin
formate + H+ + reduced ferredoxin
-
formaldehyde and aldehyde ferredoxin oxidoreductases
-
ir
glyceraldehyde + H2O + oxidized ferredoxin
glycerate + H+ + reduced ferredoxin
-
-
-
?
glyceraldehyde + H2O + oxidized ferredoxin
glycerate + H+ + reduced ferredoxin
-
-
-
?
glyceraldehyde + H2O + oxidized ferredoxin
glycerate + H+ + reduced ferredoxin
-
-
-
ir
glyceraldehyde + H2O + oxidized ferredoxin
glycerate + H+ + reduced ferredoxin
-
involved in glycolysis
-
ir
glyceraldehyde + H2O + oxidized methyl viologen
glycerate + H+ + reduced methyl viologen
-
-
-
ir
glyceraldehyde + H2O + oxidized methyl viologen
glycerate + H+ + reduced methyl viologen
-
very poor substrate
-
-
?
glyceraldehyde 3-phosphate + H2O + oxidized ferredoxin
glycerate 3-phosphate + H+ + reduced ferredoxin
-
-
-
?
glyceraldehyde 3-phosphate + H2O + oxidized ferredoxin
glycerate 3-phosphate + H+ + reduced ferredoxin
-
-
-
?
indoleacetaldehyde + H2O + oxidized benzyl viologen
indoleacetate + H+ + reduced benzyl viologen
-
-
-
?
indoleacetaldehyde + H2O + oxidized benzyl viologen
indoleacetate + H+ + reduced benzyl viologen
-
formaldehyde ferredoxin oxidoreductase
-
-
ir
indoleacetaldehyde + H2O + oxidized benzyl viologen
indoleacetate + H+ + reduced benzyl viologen
-
-
-
-
ir
isovalerylaldehyde + H2O + oxidized benzyl viologen
isovalerate + H+ + reduced benzyl viologen
-
formaldehyde ferredoxin oxidoreductase, no activity
-
-
?
isovalerylaldehyde + H2O + oxidized benzyl viologen
isovalerate + H+ + reduced benzyl viologen
formaldehyde ferredoxin oxidoreductase, no activity
-
-
?
isovalerylaldehyde + H2O + oxidized benzyl viologen
isovalerate + H+ + reduced benzyl viologen
-
formaldehyde ferredoxin oxidoreductase, no activity
-
-
?
isovalerylaldehyde + H2O + oxidized benzyl viologen
isovalerate + H+ + reduced benzyl viologen
-
-
-
-
ir
phenylacetaldehyde + H2O + oxidized benzyl viologen
phenylacetate + H+ + reduced benzyl viologen
-
100% activity
-
-
?
phenylacetaldehyde + H2O + oxidized benzyl viologen
phenylacetate + H+ + reduced benzyl viologen
-
no activity
-
-
?
phenylacetaldehyde + H2O + oxidized benzyl viologen
phenylacetate + H+ + reduced benzyl viologen
-
-
-
-
ir
phenylpropionaldehyde + H2O + oxidized benzyl viologen
phenylpropanoate + H+ + reduced benzyl viologen
-
-
-
r
phenylpropionaldehyde + H2O + oxidized benzyl viologen
phenylpropanoate + H+ + reduced benzyl viologen
-
formaldehyde ferredoxin oxidoreductase
-
-
ir
propionaldehyde + H2O + oxidized benzyl viologen
propionate + H+ + reduced benzyl viologen
-
36% activity compared to phenylacetaldehyde
-
-
?
propionaldehyde + H2O + oxidized benzyl viologen
propionate + H+ + reduced benzyl viologen
-
formaldehyde ferredoxin oxidoreductase
-
ir
propionaldehyde + H2O + oxidized benzyl viologen
propionate + H+ + reduced benzyl viologen
formaldehyde ferredoxin oxidoreductase
-
ir
propionaldehyde + H2O + oxidized benzyl viologen
propionate + H+ + reduced benzyl viologen
-
formaldehyde ferredoxin oxidoreductase
-
ir
propionaldehyde + H2O + oxidized benzyl viologen
propionate + H+ + reduced benzyl viologen
-
-
-
ir
propionaldehyde + H2O + oxidized benzyl viologen
propionate + H+ + reduced benzyl viologen
-
-
-
ir
propionaldehyde + H2O + oxidized ferredoxin
propionate + H+ + reduced ferredoxin
-
-
-
-
?
propionaldehyde + H2O + oxidized ferredoxin
propionate + H+ + reduced ferredoxin
-
formaldehyde ferredoxin oxidoreductase
-
ir
succinic semialdehyde + H2O + oxidized benzyl viologen
succinic acid + H+ + reduced benzyl viologen
-
-
-
r
succinic semialdehyde + H2O + oxidized benzyl viologen
succinic acid + H+ + reduced benzyl viologen
-
formaldehyde ferredoxin oxidoreductase
-
-
ir
additional information
?
-
enzyme AORAa catalyzes the oxidation of a broad variety of aldehydes to the respective acids with either viologen dyes or NAD+ as electron acceptors, about twofold higher kcat values with benzyl viologen than with NAD+ as electron acceptor. Enzyme AORAa is also catalyzing the reverse reaction, reduction of benzoate to benzaldehyde, albeit at very low rates and under conditions strongly favoring acid reduction, e.g. low pH and using Ti(III) citrate as electron donor of very low redox potential. Substrate specificity, overview
-
-
-
additional information
?
-
enzyme AORAa catalyzes the oxidation of a broad variety of aldehydes to the respective acids with either viologen dyes or NAD+ as electron acceptors, about twofold higher kcat values with benzyl viologen than with NAD+ as electron acceptor. Enzyme AORAa is also catalyzing the reverse reaction, reduction of benzoate to benzaldehyde, albeit at very low rates and under conditions strongly favoring acid reduction, e.g. low pH and using Ti(III) citrate as electron donor of very low redox potential. Substrate specificity, overview
-
-
-
additional information
?
-
-
no activity towards xanthine, allopurinol, and isoquinoline, inactive towards N-heterolytic compounds
-
-
?
additional information
?
-
-
no activity towards xanthine, allopurinol, and isoquinoline, inactive towards N-heterolytic compounds
-
-
?
additional information
?
-
-
the enzyme is expressed under microaerobic conditions. The non-magnetic mutant, NMA21 is defective in aldehyde ferredoxin oxidoreductase gene. The enzyme may contribute to ferric iron reduction during synthesis of bacterial magnetic particles under microaerobic respiration
-
-
?
additional information
?
-
-
the enzyme is expressed under microaerobic conditions. The non-magnetic mutant, NMA21 is defective in aldehyde ferredoxin oxidoreductase gene. The enzyme may contribute to ferric iron reduction during synthesis of bacterial magnetic particles under microaerobic respiration
-
-
?
additional information
?
-
-
enzyme shows an active and an inactive form
-
-
?
additional information
?
-
-
enzyme shows an active and an inactive form
-
-
?
additional information
?
-
-
no oxidizing activity with glyceraldehyde-3-phosphate, glyoxylate, glucose, glucose 6-phosphate, CO, H2, formate, pyruvate, 2-oxoglutarate
-
-
?
additional information
?
-
-
NAD(P) is no electron acceptor
-
-
?
additional information
?
-
-
no H2 evolution from reduced methyl viologen
-
-
?
additional information
?
-
-
no activity with CoA
-
-
?
additional information
?
-
-
the enzyme is most active on aldehydes derived from amino acids
-
-
?
additional information
?
-
-
acid reduction is strongly dependent on the overall reduction potential, therfore reverse reaction is only possible with reduced methyl viologen at a low rate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Heider, J.; Ma, K.; Adams, M.W.W.
Purification, characterization, and metabolic function of tungsten-containing aldehyde ferredoxin oxidoreductase from the hyperthermophilic and proteolytic archaeon Thermococcus strain ES-1
J. Bacteriol.
177
4757-4764
1995
Thermococcus sp., Thermococcus sp. ES1
brenda
Mukund, S.; Adams, M.W.W.
The novel tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase. Evidence for its participation in a unique glycolytic pathway
J. Biol. Chem.
266
14208-14216
1991
Pyrococcus furiosus
brenda
Kletzin, A.; Mukund, S.; Kelley-Crouse, T.L.; Chan, M.K.; Rees, D.C.; Adams, M.W.
Molecular characterization of the genes encoding the tungsten-containing aldehyde ferredoxin oxidoreductase from Pyrococcus furiosus and formaldehyde ferredoxin oxidoreductase from Thermococcus litoralis
J. Bacteriol.
177
4817-4819
1995
Pyrococcus furiosus (Q51739), Pyrococcus furiosus
brenda
Chan, M.K.; Mukund, S.; Kletzin, A.; Adams, M.W.; Rees, D.C.
Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase
Science
267
1463-1469
1995
Pyrococcus furiosus
brenda
Koehler, B.P.; Mukund, S.; Conover, R.C.; Dhawan, I.K.; Roy, R.; Adams, M.W.W.; Johnson, M.K.
Spectroscopic characterization of the tungsten and iron centers in aldehyde ferredoxin oxidoreductases from two hyperthermophilic archaea
J. Am. Chem. Soc.
118
12391-12405
1996
Pyrococcus furiosus, Pyrococcus endeavori
-
brenda
Das, S.K.; Biswas, D.; Maiti, R.; Sarkar, S.
Modeling the tungsten sites of inactive and active forms of hyperthermophilic Pyrococcus furiosus aldehyde ferredoxin oxidoreductase
J. Am. Chem. Soc.
118
1387-1397
1996
Pyrococcus furiosus
-
brenda
Roy, R.; Mukund, S.; Schut, G.J.; Dunn, D.M.; Weiss, R.; Adams, M.W.
Purification and molecular characterization of the tungsten-containing formaldehyde ferredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus: the third of a putative five-member tungstoenzyme family
J. Bacteriol.
181
1171-1180
1999
Pyrococcus furiosus
brenda
Hu, Y.; Faham, S.; Roy, R.; Adams, M.W.; Rees, D.C.
Formaldehyde ferredoxin oxidoreductase from Pyrococcus furiosus: the 1.85 A resolution crystal structure and its mechanistic implications
J. Mol. Biol.
286
899-914
1999
Pyrococcus furiosus
brenda
Roy, R.; Menon, A.L.; Adams, M.W.W.
Aldehyde oxidoreductases from Pyrococcus furiosus
Methods Enzymol.
331
132-144
2001
Pyrococcus endeavori, Pyrococcus furiosus, Pyrococcus furiosus (Q51739), Thermococcus litoralis, Thermococcus sp., Thermococcus sp. ES1
brenda
Wahyudi, A.T.; Takeyama, H.; Okamura, Y.; Fukuda, Y.; Matsunaga, T.
Characterization of aldehyde ferredoxin oxidoreductase gene defective mutant in Magnetospirillum magneticum AMB-1
Biochem. Biophys. Res. Commun.
303
223-229
2003
Magnetospirillum magneticum, Magnetospirillum magneticum AMB-1
brenda
Hagedoorn, P.L.; Chen, T.; Schroder, I.; Piersma, S.R.; Vries, S.D.; Hagen, W.R.
Purification and characterization of the tungsten enzyme aldehyde:ferredoxin oxidoreductase from the hyperthermophilic denitrifier Pyrobaculum aerophilum
J. Biol. Inorg. Chem.
10
259-269
2005
Pyrobaculum aerophilum
brenda
Bevers, L.E.; Bol, E.; Hagedoorn, P.L.; Hagen, W.R.
WOR5, a novel tungsten-containing aldehyde oxidoreductase from Pyrococcus furiosus with a broad substrate specificity
J. Bacteriol.
187
7056-7061
2005
Pyrococcus furiosus
brenda
Thapper, A.; Rivas, M.G.; Brondino, C.D.; Ollivier, B.; Fauque, G.; Moura, I.; Moura, J.J.
Biochemical and spectroscopic characterization of an aldehyde oxidoreductase isolated from Desulfovibrio aminophilus
J. Inorg. Biochem.
100
44-50
2006
Desulfovibrio aminophilus, Desulfovibrio aminophilus DSM 12254
brenda
Sugimoto, H.; Tano, H.; Tajima, R.; Miyake, H.; Tsukube, H.; Ohi, H.; Itoh, S.
In situ generation of oxo-sulfidobis(dithiolene)tungsten(VI) complexes: active-site models for the aldehyde ferredoxin oxidoreductase family of tungsten enzymes
Inorg. Chem.
46
8460-8462
2007
synthetic construct
brenda
Zhou, Z.H.; Adams, M.W.
Site-directed mutations of the 4Fe-ferredoxin from the hyperthermophilic archaeon Pyrococcus furiosus: role of the cluster-coordinating aspartate in physiological electron transfer reactions
Biochemistry
36
10892-10900
1997
Pyrococcus furiosus
brenda
Arendsen, A.F.; de Vocht, M.; Bulsink, Y.B.M.; Hagen, W.R.
Redox chemistry of biological tungsten: an EPR study of the aldehyde oxidoreductase from Pyrococcus furiosus
Chemistry
1
292-296
1996
Pyrococcus furiosus
-
brenda
George, G.N.; Prince, R.C.; Mukund, S.; Adams, M.W.W.
Aldehyde ferredoxin oxidoreductase from the hyperthermophilic archaebacterium Pyrococcus furiosus contains a tungsten oxo-thiolate cente
J. Am. Chem. Soc.
114
3521-3523
1992
Pyrococcus furiosus
-
brenda
Mukund, S.; Adams, M.W.
Molybdenum and vanadium do not replace tungsten in the catalytically active forms of the three tungstoenzymes in the hyperthermophilic archaeon Pyrococcus furiosus
J. Bacteriol.
178
163-167
1996
Pyrococcus furiosus (Q51739), Pyrococcus furiosus
brenda
Liao, R.Z.
Why is the molybdenum-substituted tungsten-dependent formaldehyde ferredoxin oxidoreductase not active? A quantum chemical study
J. Biol. Inorg. Chem.
18
175-181
2013
Pyrococcus furiosus (Q8U1K3)
brenda
Liao, R.Z.; Yu, J.G.; Himo, F.
Tungsten-dependent formaldehyde ferredoxin oxidoreductase: reaction mechanism from quantum chemical calculations
J. Inorg. Biochem.
105
927-936
2011
Pyrococcus furiosus (Q8U1K3)
brenda
Basen, M.; Schut, G.J.; Nguyen, D.M.; Lipscomb, G.L.; Benn, R.A.; Prybol, C.J.; Vaccaro, B.J.; Poole, F.L.; Kelly, R.M.; Adams, M.W.
Single gene insertion drives bioalcohol production by a thermophilic archaeon
Proc. Natl. Acad. Sci. USA
111
17618-17623
2014
Pyrococcus furiosus (Q51739), Pyrococcus furiosus
brenda
Ammam, F.; Tremblay, P.; Lizak, D.; Zhang, T.
Effect of tungstate on acetate and ethanol production by the electrosynthetic bacterium Sporomusa ovata
Biotechnol. Biofuels
9
163
2016
Sporomusa ovata, Sporomusa ovata DSM-2662
brenda
Debnar-Daumler, C.; Seubert, A.; Schmitt, G.; Heider, J.
Simultaneous involvement of a tungsten-containing aldehyde:ferredoxin oxidoreductase and a phenylacetaldehyde dehydrogenase in anaerobic phenylalanine metabolism
J. Bacteriol.
196
483-492
2014
Aromatoleum aromaticum
brenda
Liew, F.; Henstra, A.M.; Koepke, M.; Winzer, K.; Simpson, S.D.; Minton, N.P.
Metabolic engineering of Clostridium autoethanogenum for selective alcohol production
Metab. Eng.
40
104-114
2017
Clostridium autoethanogenum
brenda
Adams, M.; Holden, J.; Menon, A.; Schut, G.; Grunden, A.; Hou, C.; Hutchins, A.; Jenney F.E., J.; Kim, C.; Ma, K.; Pan, G.; Roy, R.; Sapra, R.; Story, S.; Verhagen, M.
Key role for sulfur in peptide metabolism and in regulation of three hydrogenases in the hyperthermophilic archaeon Pyrococcus furiosus
J. Bacteriol.
183
716-724
2001
Pyrococcus furiosus (Q51739)
brenda
Sevcenco, A.; Bevers, L.; Pinkse, M.; Krijger, G.; Wolterbeek, H.; Verhaert, P.; Hagen, W.; Hagedoorn, P.
Molybdenum incorporation in tungsten aldehyde oxidoreductase enzymes from Pyrococcus furiosus
J. Bacteriol.
192
4143-4152
2010
Pyrococcus furiosus (Q51739)
brenda
Liu, Z.; Jia, D.; Zhang, K.; Zhu, H.; Zhang, Q.; Jiang, W.; Gu, Y.; Li, F.
Ethanol metabolism dynamics in Clostridium ljungdahlii grown on carbon monoxide
Appl. Environ. Microbiol.
86
e00730
2020
Clostridium ljungdahlii, Clostridium ljungdahlii DSM 13528
brenda
Hitschler, L.; Kuntz, M.; Langschied, F.; Basen, M.
Thermoanaerobacter species differ in their potential to reduce organic acids to their corresponding alcohols
Appl. Microbiol. Biotechnol.
102
8465-8476
2018
Thermoanaerobacter sp. X514 (B0K0E5)
brenda
Arndt, F.; Schmitt, G.; Winiarska, A.; Saft, M.; Seubert, A.; Kahnt, J.; Heider, J.
Characterization of an aldehyde oxidoreductase from the mesophilic bacterium Aromatoleum aromaticum EbN1, a member of a new subfamily of tungsten-containing enzymes
Front. Microbiol.
10
71
2019
Aromatoleum aromaticum (Q5P0J8), Aromatoleum aromaticum EbN1 (Q5P0J8)
brenda
Scott, I.M.; Rubinstein, G.M.; Poole, F.L.; Lipscomb, G.L.; Schut, G.J.; Williams-Rhaesa, A.M.; Stevenson, D.M.; Amador-Noguez, D.; Kelly, R.M.; Adams, M.W.W.
The thermophilic biomass-degrading bacterium Caldicellulosiruptor bescii utilizes two enzymes to oxidize glyceraldehyde 3-phosphate during glycolysis
J. Biol. Chem.
294
9995-10005
2019
Caldicellulosiruptor bescii (B9MQI2 and B9MQI1), Caldicellulosiruptor bescii, Caldicellulosiruptor bescii DSM 6725 (B9MQI2 and B9MQI1)
brenda