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acetaldehyde + H2O + oxidized benzyl viologen
acetate + H+ + reduced benzyl viologen
-
-
-
?
acetaldehyde + H2O + oxidized benzyl viologen
acetate + reduced benzyl viologen + H+
-
-
-
?
acetaldehyde + H2O + oxidized methyl viologen
acetate + H+ + reduced methyl viologen
butyraldehyde + H2O + oxidized methyl viologen
butyrate + H+ + reduced methyl viologen
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 H+ + 2 reduced ferredoxin
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
-
-
?
formaldehyde + H2O + oxidized benzyl viologen
formate + H+ + reduced benzyl viologen
formaldehyde + H2O + oxidized benzyl viologen
formate + reduced benzyl viologen + H+
formaldehyde + H2O + oxidized ferredoxin
formate + H+ + reduced ferredoxin
formaldehyde + H2O + oxidized methyl viologen
formate + H+ + reduced methyl viologen
formaldehyde + H2O + oxidized methyl viologen
formate + reduced methyl viologen + H+
glutaric dialdehyde + H2O + oxidized benzyl viologen
? + reduced benzyl viologen + H+
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+
-
-
-
?
additional information
?
-
acetaldehyde + H2O + oxidized methyl viologen
acetate + H+ + reduced methyl viologen
-
-
-
?
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
-
-
-
?
formaldehyde + H2O + 2 oxidized ferredoxin
formate + 2 H+ + 2 reduced ferredoxin
-
-
-
?
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+
-
-
-
?
glutaric dialdehyde + H2O + oxidized benzyl viologen
? + reduced benzyl viologen + H+
best substrate, C5- or C6-type aldehydes might be physiologically relevant substrates
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
no activity with crotonaldehyde, benzaldehyde, isovalerylaldehyde or phenylacetaldehyde
-
-
?
additional information
?
-
activity with crotonaldehyde is less than 10% compared to activity with acetaldehyde: crotonaldehyde, benzaldehyde, phenylacetaldehyde
-
-
?
additional information
?
-
-
activity with crotonaldehyde is less than 10% compared to activity with acetaldehyde: crotonaldehyde, benzaldehyde, phenylacetaldehyde
-
-
?
additional information
?
-
activity with crotonaldehyde is less than 10% compared to activity with acetaldehyde: crotonaldehyde, benzaldehyde, phenylacetaldehyde
-
-
?
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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
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
contains one [4Fe-4S] cubane per 69000 Da subunit
Iron
enzyme contains an [Fe4S4]+ cluster
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
contains one tungstodipterin per 69000 Da subunit
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-containing protein
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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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.
268
13592-13600
1993
Thermococcus litoralis (Q56303), Thermococcus litoralis, Thermococcus litoralis DSM 5473 (Q56303)
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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
Thermococcus litoralis (Q56303), Thermococcus litoralis
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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 (O93738), 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 (Q8U1K3), Pyrococcus furiosus
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Roy, R.; Menon, A.L.; Adams, M.W.W.
Aldehyde oxidoreductases from Pyrococcus furiosus
Methods Enzymol.
331
132-144
2001
Pyrococcus furiosus (O93738)
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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
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Bol, E.; Bevers, L.E.; Hagedoorn, P.L.; Hagen, W.R.
Redox chemistry of tungsten and iron-sulfur prosthetic groups in Pyrococcus furiosus formaldehyde ferredoxin oxidoreductase
J. Biol. Inorg. Chem.
11
999-1006
2006
Pyrococcus furiosus, Pyrococcus furiosus (Q8U1K3)
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
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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
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Dhawan, I.K.; Roy, R.; Koehler, B.P.; Mukund, S.; Adams, M.W.; Johnson, M.K.
Spectroscopic studies of the tungsten-containing formaldehyde ferredoxin oxidoreductase from the hyperthermophilic archaeon Thermococcus litoralis
J. Biol. Inorg. Chem.
5
313-327
2000
Thermococcus litoralis (Q56303), Thermococcus litoralis, Thermococcus litoralis DSM 5473 (Q56303)
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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
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Sevcenco, A.M.; Pinkse, M.W.; Bol, E.; Krijger, G.C.; Wolterbeek, H.T.; Verhaert, P.D.; Hagedoorn, P.L.; Hagen, W.R.
The tungsten metallome of Pyrococcus furiosus
Metallomics
1
395-402
2009
Pyrococcus furiosus (Q8U1K3), Pyrococcus furiosus
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Smalley, N.E.; Taipale, S.; De Marco, P.; Doronina, N.V.; Kyrpides, N.; Shapiro, N.; Woyke, T.; Kalyuzhnaya, M.G.
Functional and genomic diversity of methylotrophic Rhodocyclaceae: description of Methyloversatilis discipulorum sp. nov
Int. J. Syst. Evol. Microbiol.
65
2227-2233
2015
Methyloversatilis discipulorum, Methyloversatilis discipulorum RZ18-153, Methyloversatilis discipulorum FAM1, Methyloversatilis discipulorum RZ94
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
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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
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Hagedoorn, P.L.
Steady-state kinetics of the tungsten containing aldehyde ferredoxin oxidoreductases from the hyperthermophilic archaeon Pyrococcus furiosus
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2019
Pyrococcus furiosus (Q8U1K3)
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