BRENDA - Enzyme Database
show all sequences of 1.5.1.30

Structure-function relationship of Vibrio harveyi NADPH-flavin oxidoreductase FRP: essential residues Lys167 and Arg15 for NADPH binding

Chung, H.W.; Tu, S.C.; Biochemistry 51, 4880-4887 (2012)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expressed in Escherichia coli BL21(DE3)pLysS cells
Vibrio harveyi
Engineering
Protein Variants
Commentary
Organism
K167A
the mutant has apparently greatly increased Km and reduced kcat/Km for NADPH
Vibrio harveyi
N134A
the mutant shows increased Km and reduced kcat/Km for NADPH
Vibrio harveyi
R133A
the mutant shows increased Km and reduced kcat/Km for NADPH
Vibrio harveyi
R15A
the mutant has apparently greatly increased Km and reduced kcat/Km for NADPH
Vibrio harveyi
R225A
the mutant shows about wild type activity
Vibrio harveyi
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.009
-
NADPH
wild type enzyme, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
Vibrio harveyi
0.01
-
NADPH
mutant enzyme R225A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
Vibrio harveyi
0.016
-
NADPH
mutant enzyme R133A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
Vibrio harveyi
0.034
-
NADPH
mutant enzyme N134A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
Vibrio harveyi
Organism
Organism
UniProt
Commentary
Textmining
Vibrio harveyi
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
HiTrap DEAE column chromatography, Mono Q column chromatography, and Superdex 75 gel filtration
Vibrio harveyi
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
FMN + NADPH + H+
-
724343
Vibrio harveyi
FMNH2 + NADP+
-
-
-
?
Synonyms
Synonyms
Commentary
Organism
FRP
-
Vibrio harveyi
NADPH-flavin oxidoreductase
-
Vibrio harveyi
NADPH-FMN oxidoreductase
-
Vibrio harveyi
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
5.2
-
NADPH
mutant enzyme N134A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
Vibrio harveyi
9.2
-
NADPH
mutant enzyme R133A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
Vibrio harveyi
19.2
-
NADPH
mutant enzyme R225A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
Vibrio harveyi
23.8
-
NADPH
wild type enzyme, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
Vibrio harveyi
Cofactor
Cofactor
Commentary
Organism
Structure
NADPH
-
Vibrio harveyi
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli BL21(DE3)pLysS cells
Vibrio harveyi
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADPH
-
Vibrio harveyi
Engineering (protein specific)
Protein Variants
Commentary
Organism
K167A
the mutant has apparently greatly increased Km and reduced kcat/Km for NADPH
Vibrio harveyi
N134A
the mutant shows increased Km and reduced kcat/Km for NADPH
Vibrio harveyi
R133A
the mutant shows increased Km and reduced kcat/Km for NADPH
Vibrio harveyi
R15A
the mutant has apparently greatly increased Km and reduced kcat/Km for NADPH
Vibrio harveyi
R225A
the mutant shows about wild type activity
Vibrio harveyi
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.009
-
NADPH
wild type enzyme, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
Vibrio harveyi
0.01
-
NADPH
mutant enzyme R225A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
Vibrio harveyi
0.016
-
NADPH
mutant enzyme R133A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
Vibrio harveyi
0.034
-
NADPH
mutant enzyme N134A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
Vibrio harveyi
Purification (Commentary) (protein specific)
Commentary
Organism
HiTrap DEAE column chromatography, Mono Q column chromatography, and Superdex 75 gel filtration
Vibrio harveyi
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
FMN + NADPH + H+
-
724343
Vibrio harveyi
FMNH2 + NADP+
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
5.2
-
NADPH
mutant enzyme N134A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
Vibrio harveyi
9.2
-
NADPH
mutant enzyme R133A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
Vibrio harveyi
19.2
-
NADPH
mutant enzyme R225A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
Vibrio harveyi
23.8
-
NADPH
wild type enzyme, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
Vibrio harveyi
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
12
-
NADPH
mutant enzyme R15A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
Vibrio harveyi
25
-
NADPH
mutant enzyme K167A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
Vibrio harveyi
150
-
NADPH
mutant enzyme N134A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
Vibrio harveyi
570
-
NADPH
mutant enzyme R133A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
Vibrio harveyi
2000
-
NADPH
mutant enzyme R225A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
Vibrio harveyi
2670
-
NADPH
wild type enzyme, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
Vibrio harveyi
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
12
-
NADPH
mutant enzyme R15A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
Vibrio harveyi
25
-
NADPH
mutant enzyme K167A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
Vibrio harveyi
150
-
NADPH
mutant enzyme N134A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
Vibrio harveyi
570
-
NADPH
mutant enzyme R133A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
Vibrio harveyi
2000
-
NADPH
mutant enzyme R225A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
Vibrio harveyi
2670
-
NADPH
wild type enzyme, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
Vibrio harveyi
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)
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284
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2
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1
-
1
-
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2
-
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1
2
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3
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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
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1
1
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2
2
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-
7
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6
2
4
-
7
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1
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2
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26
1
2
1
1
1
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1
1
1
3
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2
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1
3
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7
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6
2
4
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1
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2
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26
1
1
1
1
-
1
1
1
-
-
1
1
-
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-
684711
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Vibrio harveyi
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1
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1
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2
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1
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1
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1
1
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Vibrio harveyi
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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
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1
1
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1
1
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2
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4
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684610
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1
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689909
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16
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1
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2
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671610
Li
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Vibrio harveyi
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454
26-31
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3
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1
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672105
Li
Thermodynamic analysis of the ...
Vibrio harveyi
Biochemistry
45
14781-14787
2006
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672184
Deller
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Bacillus subtilis
Biochemistry
45
7083-7091
2006
-
-
-
-
-
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1
3
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2
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5
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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
2
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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14
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1
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1
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2
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2
1
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657786
Gao
Altered mechanism of the alkan ...
Escherichia coli
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Purification, characterization ...
Rhodococcus erythropolis, Rhodococcus erythropolis D1
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Initial-rate kinetics of the f ...
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Purification and characetriza ...
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Flavin reductase P: structure ...
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Shalloe
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Myocardial flavin reductase an ...
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Lei
Vibrio harveyi NADPH-flavin ox ...
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Chikuba
Cloning and nucleotide sequenc ...
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Yubisui
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