BRENDA - Enzyme Database
show all sequences of 1.5.1.30

Purification and characterization of NfrA1, a Bacillus subtilis nitro/flavin reductase capable of interacting with the bacterial luciferase

Zenno, S.; Kobori, T.; Tanokura, M.; Saigo, K.; Biosci. Biotechnol. Biochem. 62, 1978-1987 (1998)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expressed in Escherichia coli
Bacillus subtilis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.00085
-
NADPH
nitrofurazone as electron acceptor
Bacillus subtilis
0.0035
-
NADPH
FMN as electron accceptor
Bacillus subtilis
0.0047
-
FMN
-
Bacillus subtilis
0.0163
-
nitrofurazone
-
Bacillus subtilis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
28000
-
x * 28000, SDS-PAGE
Bacillus subtilis
28320
-
calculated from sequence of cDNA
Bacillus subtilis
Organism
Organism
UniProt
Commentary
Textmining
Bacillus subtilis
-
ISW 1214.
-
Bacillus subtilis ISW 1214.
-
ISW 1214.
-
Purification (Commentary)
Purification (Commentary)
Organism
-
Bacillus subtilis
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
53
-
-
Bacillus subtilis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
FMN + NADPH
-
392302
Bacillus subtilis
FMNH2 + NADP+
-
-
-
?
FMN + NADPH
-
392302
Bacillus subtilis ISW 1214.
FMNH2 + NADP+
-
-
-
?
nitrofurazone + NADPH + 4 H+
-
392302
Bacillus subtilis
5-(hydroxyamino)furan-2-carbaldehyde semicarbazone + NADP+ + H2O
-
-
-
?
nitrofurazone + NADPH + 4 H+
-
392302
Bacillus subtilis ISW 1214.
5-(hydroxyamino)furan-2-carbaldehyde semicarbazone + NADP+ + H2O
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 28000, SDS-PAGE
Bacillus subtilis
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
23
-
enzyme assay
Bacillus subtilis
Cofactor
Cofactor
Commentary
Organism
Structure
FMN
-
Bacillus subtilis
NADPH
-
Bacillus subtilis
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli
Bacillus subtilis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FMN
-
Bacillus subtilis
NADPH
-
Bacillus subtilis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.00085
-
NADPH
nitrofurazone as electron acceptor
Bacillus subtilis
0.0035
-
NADPH
FMN as electron accceptor
Bacillus subtilis
0.0047
-
FMN
-
Bacillus subtilis
0.0163
-
nitrofurazone
-
Bacillus subtilis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
28000
-
x * 28000, SDS-PAGE
Bacillus subtilis
28320
-
calculated from sequence of cDNA
Bacillus subtilis
Purification (Commentary) (protein specific)
Commentary
Organism
-
Bacillus subtilis
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
53
-
-
Bacillus subtilis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
FMN + NADPH
-
392302
Bacillus subtilis
FMNH2 + NADP+
-
-
-
?
FMN + NADPH
-
392302
Bacillus subtilis ISW 1214.
FMNH2 + NADP+
-
-
-
?
nitrofurazone + NADPH + 4 H+
-
392302
Bacillus subtilis
5-(hydroxyamino)furan-2-carbaldehyde semicarbazone + NADP+ + H2O
-
-
-
?
nitrofurazone + NADPH + 4 H+
-
392302
Bacillus subtilis ISW 1214.
5-(hydroxyamino)furan-2-carbaldehyde semicarbazone + NADP+ + H2O
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 28000, SDS-PAGE
Bacillus subtilis
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
23
-
enzyme assay
Bacillus subtilis
Other publictions for EC 1.5.1.30
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
743224
Man
Improvement of the intracellu ...
Corynebacterium crenatum, Corynebacterium crenatum SYPA5-5
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38
310-321
2016
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1
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1
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2
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4
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7
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1
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8
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3
1
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2
1
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2
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1
2
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1
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2
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4
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1
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8
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1
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2
1
-
-
-
-
-
-
-
2
2
743307
Leitsch
Trichomonas vaginalis flavin ...
Trichomonas vaginalis, Trichomonas vaginalis G3
Mol. Microbiol.
91
198-208
2014
-
-
1
-
-
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1
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4
-
5
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1
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4
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3
1
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1
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3
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1
3
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1
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4
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1
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4
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1
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1
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-
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2
2
-
-
-
724343
Chung
Structure-function relationshi ...
Vibrio harveyi
Biochemistry
51
4880-4887
2012
-
-
1
-
5
-
-
4
-
-
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5
-
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1
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1
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3
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4
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1
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5
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1
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1
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4
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6
6
724769
Haynes
Reactions of antimalarial pero ...
Escherichia coli
ChemMedChem
6
279-291
2011
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2
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1
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1
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1
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-
725248
Kozmin
Role for CysJ flavin reductase ...
Escherichia coli
J. Bacteriol.
192
2026-2033
2010
-
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-
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-
-
-
-
-
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4
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2
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1
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1
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2
2
-
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-
698992
Campbell
Fre Is the Major Flavin Reduct ...
Escherichia coli
J. Biol. Chem.
284
8322-8328
2009
2
-
1
-
1
-
-
2
-
-
1
2
-
6
-
-
1
-
-
-
-
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4
1
3
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2
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1
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1
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2
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1
2
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1
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-
-
4
1
-
-
-
-
-
-
-
-
-
1
1
-
2
2
699057
Takahashi
Characterization of a flavin r ...
Bacillus subtilis, Bacillus subtilis WU-S2B
J. Biosci. Bioeng.
107
38-41
2009
2
-
1
-
-
-
7
-
-
6
2
4
-
11
-
-
1
-
-
-
2
-
26
1
2
1
1
1
-
1
1
1
3
-
-
-
2
-
1
3
-
-
-
-
7
-
-
-
6
2
4
-
-
-
1
-
-
2
-
26
1
1
1
1
-
1
1
1
-
-
1
1
-
-
-
684711
Jawanda
A single-residue mutation dest ...
Vibrio harveyi
Arch. Biochem. Biophys.
472
51-57
2008
-
-
1
-
1
-
-
2
-
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1
-
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4
-
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1
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1
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1
1
2
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2
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1
2
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1
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1
1
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1
1
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685230
Jawanda
Vibrio harveyi flavin reductas ...
Vibrio harveyi
Biochemistry
47
368-377
2008
-
-
1
-
-
-
-
4
-
-
1
-
-
3
-
-
1
-
-
-
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1
1
1
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2
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2
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1
2
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4
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1
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1
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-
1
1
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-
-
2
-
-
-
-
-
-
-
-
-
-
689388
Tu
Activity coupling and complex ...
Aliivibrio fischeri, Vibrio harveyi
Photochem. Photobiol. Sci.
7
183-188
2008
-
-
-
-
-
-
-
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4
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2
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2
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4
4
2
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4
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4
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4
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4
4
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-
684610
Liu
Azoreductase from Rhodobacter ...
Luteovulum sphaeroides, Luteovulum sphaeroides AS1.1737
Appl. Microbiol. Biotechnol.
76
1271-1279
2007
-
-
1
-
-
-
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2
-
-
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2
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6
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2
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1
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3
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1
3
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2
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6
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1
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689909
Vorontsov
Crystal structure of an apo fo ...
Shigella flexneri
Protein Sci.
16
2483-2490
2007
-
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1
1
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2
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2
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1
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1
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2
2
2
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2
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1
2
1
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2
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2
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1
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2
2
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671610
Li
Activity coupling of Vibrio ha ...
Vibrio harveyi
Arch. Biochem. Biophys.
454
26-31
2006
-
-
-
-
-
-
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3
-
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4
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1
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1
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1
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-
-
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-
-
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-
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672105
Li
Thermodynamic analysis of the ...
Vibrio harveyi
Biochemistry
45
14781-14787
2006
-
-
-
-
-
-
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4
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1
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672184
Deller
Characterization of a thermost ...
Bacillus subtilis
Biochemistry
45
7083-7091
2006
-
-
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1
3
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2
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7
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1
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3
1
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1
3
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3
2
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3
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1
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3
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3
1
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1
3
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678187
Okai
Crystal structures of the shor ...
Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7
Biochemistry
45
5103-5110
2006
-
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1
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16
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1
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1
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1
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657786
Gao
Altered mechanism of the alkan ...
Escherichia coli
Biochem. Biophys. Res. Commun.
331
1137-1145
2005
-
-
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2
3
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2
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1
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1
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2
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2
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3
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3
3
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1
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2
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658108
Lei
Redox potential and equilibria ...
Aliivibrio fischeri, Vibrio harveyi
Biochemistry
44
261-267
2005
-
-
2
-
1
-
-
2
-
-
-
-
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7
-
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2
-
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2
2
5
-
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2
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4
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2
4
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1
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2
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2
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2
2
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2
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671139
Gao
Crystallization and preliminar ...
Escherichia coli
Acta Crystallogr. Sect. F
F61
837-840
2005
-
-
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1
1
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4
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1
1
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659261
Kwasnicka
Coordinate expression of NADPH ...
Caenorhabditis elegans, Homo sapiens
J. Biol. Chem.
278
39051-39058
2003
2
-
2
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2
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6
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3
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3
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660061
Low
Energy transfer evidence for i ...
Vibrio harveyi
Photochem. Photobiol.
77
446-452
2003
-
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1
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2
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1
2
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4
-
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1
1
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4
1
3
1
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1
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1
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1
1
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2
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1
2
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1
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4
1
1
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Flavin specificity and subunit ...
Aliivibrio fischeri
Arch. Biochem. Biophys.
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110-116
2001
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Matsubara
Purification, characterization ...
Rhodococcus erythropolis, Rhodococcus erythropolis D1
Appl. Environ. Microbiol.
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4
1
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1
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1
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1
1
1
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1
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1
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6
1
2
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2
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1
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2
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4
1
1
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1
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392303
Wang
Vibrio harveyi NADPH-FMN oxido ...
Vibrio harveyi
Biochemistry
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2000
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4
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1
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4
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1
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2
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714077
Cunningham
Initial-rate kinetics of the f ...
Homo sapiens
Biochem. J.
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393-399
2000
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2
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Zenno
Purification and characterizat ...
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1
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4
1
1
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742109
Zenno
Purification and characetriza ...
Bacillus subtilis, Bacillus subtilis ISW 1214
Biosci. Biotechnol. Biochem.
62
1978-1987
1998
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1
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10
1
6
1
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1
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3
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1
3
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3
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1
8
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1
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1
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10
1
1
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1
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392300
Liu
Vibrio harveyi NADPH:FMN oxido ...
Vibrio harveyi
Arch. Biochem. Biophys.
337
89-95
1997
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2
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3
1
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392301
Parry
An NADPH:FAD oxidoreductase fr ...
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1997
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1
1
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3
1
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2
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1
1
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392299
Tanner
Flavin reductase P: structure ...
Vibrio harveyi
Biochemistry
35
13531-13539
1996
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1
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714076
Shalloe
Evidence that biliverdin-IX be ...
Bos taurus
Biochem. J.
316
385-387
1996
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1
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1
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1
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1
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392298
Mack
Myocardial flavin reductase an ...
Oryctolagus cuniculus
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212
35-40
1995
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6
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392297
Lei
Vibrio harveyi NADPH-flavin ox ...
Vibrio harveyi, Vibrio harveyi MAV / ATCC 33843
J. Bacteriol.
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3552-3558
1994
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Chikuba
Cloning and nucleotide sequenc ...
Homo sapiens
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198
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1994
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Yubisui
Characterization of a second f ...
Homo sapiens
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1-8
1987
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392296
Lo
Purification and properties of ...
Entamoeba histolytica, Entamoeba histolytica NIH:200
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23-30
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Yubisui
Characterization of the purifi ...
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11
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1
1
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