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EC Tree
IUBMB Comments The enzyme from Pyrococcus furiosus requires FAD. It reduces a number of electron carriers, including benzyl viologen, menadione and 2,6-dichloroindophenol, but rubredoxin is the most efficient. Ferredoxin is not utilized.
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
Reaction Schemes
2
reduced rubredoxin
+
=
2
oxidized rubredoxin
+
+
Synonyms
nad(p)h-dependent rubredoxin reductase,
more
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NAD(P)-rubredoxin oxidoreductase
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NAD(P)H-dependent rubredoxin reductase
NAD(P)H-rubredoxin oxidoreductase
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NADPH:rubredoxin oxidoreductase
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reductase, rubredoxin-nicotinamide adenine dinucleotide (phosphate)
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rubredoxin-nicotinamide adenine dinucleotide (phosphate) reductase
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rubredoxin-nicotinamide adenine dinucleotide phosphate reductase
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NAD(P)H-dependent rubredoxin reductase
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NAD(P)H-dependent rubredoxin reductase
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NROR
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-
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2 reduced rubredoxin + NAD(P)+ = 2 oxidized rubredoxin + NAD(P)H + H+
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rubredoxin:NAD(P)+ oxidoreductase
The enzyme from Pyrococcus furiosus requires FAD. It reduces a number of electron carriers, including benzyl viologen, menadione and 2,6-dichloroindophenol, but rubredoxin is the most efficient. Ferredoxin is not utilized.
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2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
cytochrome c from horse heart
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-
?
2 oxidized rubredoxin + NADH
2 reduced rubredoxin + NAD+ + H+
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-
-
-
?
2 oxidized rubredoxin + NADPH
2 reduced rubredoxin + NADP+ + H+
2,6-dichloroindophenol + NADH
reduced 2,6-dichloroindophenol + NAD+ + H+
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-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADH
?
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-
-
-
?
benzyl viologen + NADH
reduced benzyl viologen + NAD+
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-
-
-
?
FAD + NADH
FADH2 + NAD+
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-
-
-
?
Fe(III) citrate + NADH
Fe(II) citrate + NAD+
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-
-
-
?
FMN + NADH
FMNH2 + NAD+
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-
-
-
?
methyl viologen + NADH
reduced methyl viologen + NAD+ + H+
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-
-
-
?
oxidized benzyl viologen + NADH
reduced benzyl viologen + NAD+
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-
-
-
?
oxidized benzyl viologen + NADH
reduced benzyl viologen + NAD+ + H+
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-
-
?
oxidized benzyl viologen + NADPH
reduced benzyl viologen + NADP+
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-
-
-
?
oxidized benzyl viologen + NADPH
reduced benzyl viologen + NADP+ + H+
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-
-
?
oxidized Clostridium pasteurianum rubredoxin + NADH
reduced Clostridium pasteurianum rubredoxin + NAD+ + H+
oxidized Clostridium pasteurianum rubredoxin + NADPH
reduced Clostridium pasteurianum rubredoxin + NADP+ + H+
oxidized flavodiiron protein + NADH
reduced flavodiiron protein + NAD+ + H+
oxidized flavodiiron protein + NADPH
reduced flavodiiron protein + NADP+ + H+
oxidized Pyrococcus furiosus rubredoxin + NADH
reduced Pyrococcus furiosus rubredoxin + NAD+ + H+
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-
-
-
?
oxidized Pyrococcus furiosus rubredoxin + NADPH
reduced Pyrococcus furiosus rubredoxin + NADP+ + H+
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-
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-
?
oxidized rubredoxin + NADH
reduced rubredoxin + NAD+
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rubredoxin is the best substrate
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-
?
oxidized rubredoxin + NADPH
reduced rubredoxin + NADP+
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-
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-
?
oxidized rubredoxin + NADPH
reduced rubredoxin + NADP+ + H+
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-
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-
r
oxidized rubrerythrin + NADH
reduced rubrerythrin + NAD+ + H+
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-
-
-
?
oxidized rubrerythrin + NADPH
reduced rubrerythrin + NADP+ + H+
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-
-
-
?
additional information
?
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2 oxidized rubredoxin + NADPH
2 reduced rubredoxin + NADP+ + H+
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-
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-
?
2 oxidized rubredoxin + NADPH
2 reduced rubredoxin + NADP+ + H+
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-
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?
2 oxidized rubredoxin + NADPH
2 reduced rubredoxin + NADP+ + H+
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rubredoxin is the most efficient electron acceptor
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?
2 oxidized rubredoxin + NADPH
2 reduced rubredoxin + NADP+ + H+
superoxide reductase mediates reduction of superoxide to hydrogen peroxide in an NADPH-dependent manner via a coupled reaction between NAD(P)H:rubredoxin oxidoreductase, rubredoxin, and superoxide reductase
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-
?
oxidized Clostridium pasteurianum rubredoxin + NADH
reduced Clostridium pasteurianum rubredoxin + NAD+ + H+
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-
?
oxidized Clostridium pasteurianum rubredoxin + NADH
reduced Clostridium pasteurianum rubredoxin + NAD+ + H+
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?
oxidized Clostridium pasteurianum rubredoxin + NADPH
reduced Clostridium pasteurianum rubredoxin + NADP+ + H+
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?
oxidized Clostridium pasteurianum rubredoxin + NADPH
reduced Clostridium pasteurianum rubredoxin + NADP+ + H+
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-
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?
oxidized flavodiiron protein + NADH
reduced flavodiiron protein + NAD+ + H+
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-
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?
oxidized flavodiiron protein + NADH
reduced flavodiiron protein + NAD+ + H+
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?
oxidized flavodiiron protein + NADPH
reduced flavodiiron protein + NADP+ + H+
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?
oxidized flavodiiron protein + NADPH
reduced flavodiiron protein + NADP+ + H+
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?
additional information
?
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the enzyme has no activity with ferredoxins, flavodoxins, and thioredoxins
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?
additional information
?
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the enzyme has no activity with ferredoxins, flavodoxins, and thioredoxins
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additional information
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the enzyme does not reduce Pyrococcus furiosus ferredoxin
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?
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2 oxidized rubredoxin + NADH
2 reduced rubredoxin + NAD+ + H+
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?
2 oxidized rubredoxin + NADPH
2 reduced rubredoxin + NADP+ + H+
oxidized rubredoxin + NADPH
reduced rubredoxin + NADP+
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?
2 oxidized rubredoxin + NADPH
2 reduced rubredoxin + NADP+ + H+
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rubredoxin is the most efficient electron acceptor
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?
2 oxidized rubredoxin + NADPH
2 reduced rubredoxin + NADP+ + H+
superoxide reductase mediates reduction of superoxide to hydrogen peroxide in an NADPH-dependent manner via a coupled reaction between NAD(P)H:rubredoxin oxidoreductase, rubredoxin, and superoxide reductase
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?
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FAD
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FAD
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enzyme contains FAD
FAD
essential for activity, can not be replaced by FMN
NADH
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NADH
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the catalytic efficiency exhibited by this enzyme for NADH is higher than for NADPH
NADPH
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preferred physiological electron donor
NADPH
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the catalytic efficiency exhibited by this enzyme for NADH is higher than for NADPH
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additional information
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no metals can be detected
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additional information
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no substrate inhibition at high NAD(P)H (up to 0.3 mM)
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FAD
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the enzyme contains one flavin adenine dinucleotide (FAD) molecule per mol
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5.5
Oxidized benzyl viologen
pH 8, 80°C, cosubstrate: NADH
0.0028 - 0.0043
oxidized Clostridium pasteurianum rubredoxin
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0.0032 - 0.0052
oxidized Pyrococcus furiosus rubredoxin
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0.0016 - 0.05
oxidized rubredoxin
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0.034
NADH
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0.034
NADH
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pH 8.0, 80°C, cosubstrate benzyl viologen
0.18
NADH
pH 8, 80°C, cosubstrate: benzyl viologen
0.005
NADPH
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0.005
NADPH
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pH 8.0, 80°C, cosubstrate benzyl viologen
0.048
NADPH
pH 8, 80°C, cosubstrate: benzyl viologen
0.0028
oxidized Clostridium pasteurianum rubredoxin
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with NADPH as cosubstrate, at pH 7.0 and 30°C
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0.0043
oxidized Clostridium pasteurianum rubredoxin
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with NADH as cosubstrate, at pH 7.0 and 30°C
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0.0032
oxidized Pyrococcus furiosus rubredoxin
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with NADPH as cosubstrate, at pH 7.0 and 30°C
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0.0052
oxidized Pyrococcus furiosus rubredoxin
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with NADH as cosubstrate, at pH 7.0 and 30°C
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0.0016
oxidized rubredoxin
pH 8, 23°C, cosubstrate: NADPH
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0.0095
oxidized rubredoxin
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25°C
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0.01
oxidized rubredoxin
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pH 8.0, 80°C, cosubstrate NADPH
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0.037
oxidized rubredoxin
pH 8, 80°C, cosubstrate: NADPH
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0.05
oxidized rubredoxin
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80°C
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0.05
oxidized rubredoxin
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pH 8.0, 80°C, cosubstrate: NADPH
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1236
Oxidized benzyl viologen
pH 8, 80°C, cosubstrate: NADH
3 - 13.9
oxidized Clostridium pasteurianum rubredoxin
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9.6 - 69.4
oxidized Pyrococcus furiosus rubredoxin
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221 - 15000
oxidized rubredoxin
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354
NADH
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pH 8.0, 80°C, cosubstrate: benzyl viologen
498
NADH
pH 8, 80°C, cosubstrate: benzyl viologen
258
NADPH
pH 8, 80°C, cosubstrate: benzyl viologen
341
NADPH
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pH 8.0, 80°C, cosubstrate: benzyl viologen
3 - 6
oxidized Clostridium pasteurianum rubredoxin
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with NADH as cosubstrate, at pH 7.0 and 30°C
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13.9
oxidized Clostridium pasteurianum rubredoxin
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with NADPH as cosubstrate, at pH 7.0 and 30°C
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9.6
oxidized Pyrococcus furiosus rubredoxin
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with NADPH as cosubstrate, at pH 7.0 and 30°C
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69.4
oxidized Pyrococcus furiosus rubredoxin
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with NADH as cosubstrate, at pH 7.0 and 30°C
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221
oxidized rubredoxin
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pH 8.0, 25°C, cosubstrate NADPH
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350
oxidized rubredoxin
pH 8, 23°C, cosubstrate: NADPH
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8980
oxidized rubredoxin
pH 8, 80°C, cosubstrate: NADPH
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15000
oxidized rubredoxin
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pH 8.0, 80°C, cosubstrate NADPH
-
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225
Oxidized benzyl viologen
pH 8, 80°C, cosubstrate: NADH
5000 - 8400
oxidized Clostridium pasteurianum rubredoxin
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3000 - 13000
oxidized Pyrococcus furiosus rubredoxin
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22050 - 300000
oxidized rubredoxin
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2770
NADH
pH 8, 80°C, cosubstrate: benzyl viologen
10400
NADH
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pH 8.0, 80°C, cosubstrate benzyl viologen
5375
NADPH
pH 8, 80°C, cosubstrate: benzyl viologen
68300
NADPH
-
pH 8.0, 80°C, cosubstrate benzyl viologen
5000
oxidized Clostridium pasteurianum rubredoxin
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with NADPH as cosubstrate, at pH 7.0 and 30°C
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8400
oxidized Clostridium pasteurianum rubredoxin
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with NADH as cosubstrate, at pH 7.0 and 30°C
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3000
oxidized Pyrococcus furiosus rubredoxin
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with NADPH as cosubstrate, at pH 7.0 and 30°C
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13000
oxidized Pyrococcus furiosus rubredoxin
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with NADH as cosubstrate, at pH 7.0 and 30°C
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22050
oxidized rubredoxin
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pH 8.0, 80°C, cosubstrate NADPH
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218900
oxidized rubredoxin
pH 8, 23°C, cosubstrate: NADPH
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242700
oxidized rubredoxin
pH 8, 80°C, cosubstrate: NADPH
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300000
oxidized rubredoxin
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pH 8.0, 80°C, cosubstrate NADPH
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8
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assay at
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80
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assay at
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25 - 80
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about 70fold increase in kcat/Km for oxidized rebredoxin increases from 25°C to 80°C
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8.2
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calculated from amino acid sequence
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brenda
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brenda
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SwissProt
brenda
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brenda
DSM 3638
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brenda
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brenda
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brenda
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brenda
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physiological function
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the enzyme is possibly a part of a defense mechanism against oxygen toxicity
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NROR_PYRFU
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
359
0
39941
Swiss-Prot
-
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39900
x * 39900, calculated from sequence
40000
x * 40000, SDS-PAGE
45000
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gel filtration
45000
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1 * 45000, SDS-PAGE
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?
x * 40000, SDS-PAGE
?
x * 39900, calculated from sequence
monomer
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1 * 50000, SDS-PAGE
monomer
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1 * 49700, calculated from amino acid sequence
monomer
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1 * 50000, SDS-PAGE
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monomer
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1 * 49700, calculated from amino acid sequence
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monomer
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1 * 45000, SDS-PAGE
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80
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12 h, 50% loss of activity
95
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2 h, 50% loss of activity
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HiTrap IMAC-Ni2+ column chromatography
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expressed in Escherichia coli BL21(DE3) cells
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expression in Escherichia coli
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when the organism is grown on maltose plus S(0) the specific activity of the enzyme is highest under this growth condition, slightly lower on the maltose-only medium, and lower still in the three peptide-based media
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Ma, K.; Adams, M.W.W.
NAD(P)H:rubredoxin oxidoreductase from Pyrococcus furiosus
Methods Enzymol.
334
55-62
2001
Pyrococcus furiosus
brenda
Grunden, A.M.; Jenney, F.E.; Ma, K.; Ji, M.; Weinberg, M.V.; Adams, M.W.
In vitro reconstitution of an NADPH-dependent superoxide reduction pathway from Pyrococcus furiosus
Appl. Environ. Microbiol.
71
1522-1530
2005
Pyrococcus furiosus (Q8U1K9)
brenda
Ma, K.; Adams, M.W.
A hyperactive NAD(P)H:rubredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus
J. Bacteriol.
181
5530-5533
1999
Pyrococcus furiosus
brenda
Cabeza, M.; Guerrero, S.; Iglesias, A.; Arias, D.
New enzymatic pathways for the reduction of reactive oxygen species in Entamoeba histolytica
Biochim. Biophys. Acta
1850
1233-1244
2015
Entamoeba histolytica, Entamoeba histolytica HM1-IMSS
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
brenda
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