BRENDA - Enzyme Database show
show all sequences of 1.5.1.38

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)
Commentary
Organism
expressed in Escherichia coli BL21(DE3)pLysS cells
Vibrio harveyi
Engineering
Amino acid exchange
Commentary
Organism
K167A
the mutant has apparently greatly increased Km and severely reduced kcat/Km values for NADPH and leads to a slight increase in kcat/Km for NADH
Vibrio harveyi
N134A
the mutant shows strongly decreased kcat/Km for NADPH
Vibrio harveyi
R133A
the mutant shows strongly decreased kcat/Km for NADPH
Vibrio harveyi
R15A
the mutant has apparently greatly increased Km and severely reduced kcat/Km values for NADPH
Vibrio harveyi
R225A
the mutant shows decreased kcat/Km for NADPH
Vibrio harveyi
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.009
-
NADPH
wild type enzyme, in 50 mM phosphate buffer, pH 7.0, at 22C
Vibrio harveyi
0.01
-
NADPH
mutant enzyme R225A, in 50 mM phosphate buffer, pH 7.0, at 22C
Vibrio harveyi
0.016
-
NADPH
mutant enzyme R133A, in 50 mM phosphate buffer, pH 7.0, at 22C
Vibrio harveyi
0.034
-
NADPH
mutant enzyme N134A, in 50 mM phosphate buffer, pH 7.0, at 22C
Vibrio harveyi
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
FMN + NADPH + H+
Vibrio harveyi
-
FMNH2 + NADP+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Vibrio harveyi
-
-
-
Purification (Commentary)
Commentary
Organism
DEAE-Sepharose 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
FMN + NADPH + H+
-
724343
Vibrio harveyi
FMNH2 + NADP+
-
-
-
?
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 50 mM phosphate buffer, pH 7.0, at 22C
Vibrio harveyi
9.2
-
NADPH
mutant enzyme R133A, in 50 mM phosphate buffer, pH 7.0, at 22C
Vibrio harveyi
19.2
-
NADPH
mutant enzyme R225A, in 50 mM phosphate buffer, pH 7.0, at 22C
Vibrio harveyi
23.8
-
NADPH
wild type enzyme, in 50 mM phosphate buffer, pH 7.0, at 22C
Vibrio harveyi
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli BL21(DE3)pLysS cells
Vibrio harveyi
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
K167A
the mutant has apparently greatly increased Km and severely reduced kcat/Km values for NADPH and leads to a slight increase in kcat/Km for NADH
Vibrio harveyi
N134A
the mutant shows strongly decreased kcat/Km for NADPH
Vibrio harveyi
R133A
the mutant shows strongly decreased kcat/Km for NADPH
Vibrio harveyi
R15A
the mutant has apparently greatly increased Km and severely reduced kcat/Km values for NADPH
Vibrio harveyi
R225A
the mutant shows decreased kcat/Km for NADPH
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 50 mM phosphate buffer, pH 7.0, at 22C
Vibrio harveyi
0.01
-
NADPH
mutant enzyme R225A, in 50 mM phosphate buffer, pH 7.0, at 22C
Vibrio harveyi
0.016
-
NADPH
mutant enzyme R133A, in 50 mM phosphate buffer, pH 7.0, at 22C
Vibrio harveyi
0.034
-
NADPH
mutant enzyme N134A, in 50 mM phosphate buffer, pH 7.0, at 22C
Vibrio harveyi
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
FMN + NADPH + H+
Vibrio harveyi
-
FMNH2 + NADP+
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
DEAE-Sepharose 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
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 50 mM phosphate buffer, pH 7.0, at 22C
Vibrio harveyi
9.2
-
NADPH
mutant enzyme R133A, in 50 mM phosphate buffer, pH 7.0, at 22C
Vibrio harveyi
19.2
-
NADPH
mutant enzyme R225A, in 50 mM phosphate buffer, pH 7.0, at 22C
Vibrio harveyi
23.8
-
NADPH
wild type enzyme, in 50 mM phosphate buffer, pH 7.0, at 22C
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 50 mM phosphate buffer, pH 7.0, at 22C
Vibrio harveyi
25
-
NADPH
mutant enzyme K167A, in 50 mM phosphate buffer, pH 7.0, at 22C
Vibrio harveyi
150
-
NADPH
mutant enzyme N134A, in 50 mM phosphate buffer, pH 7.0, at 22C
Vibrio harveyi
570
-
NADPH
mutant enzyme R133A, in 50 mM phosphate buffer, pH 7.0, at 22C
Vibrio harveyi
2000
-
NADPH
mutant enzyme R225A, in 50 mM phosphate buffer, pH 7.0, at 22C
Vibrio harveyi
2670
-
NADPH
wild type enzyme, in 50 mM phosphate buffer, pH 7.0, at 22C
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 50 mM phosphate buffer, pH 7.0, at 22C
Vibrio harveyi
25
-
NADPH
mutant enzyme K167A, in 50 mM phosphate buffer, pH 7.0, at 22C
Vibrio harveyi
150
-
NADPH
mutant enzyme N134A, in 50 mM phosphate buffer, pH 7.0, at 22C
Vibrio harveyi
570
-
NADPH
mutant enzyme R133A, in 50 mM phosphate buffer, pH 7.0, at 22C
Vibrio harveyi
2000
-
NADPH
mutant enzyme R225A, in 50 mM phosphate buffer, pH 7.0, at 22C
Vibrio harveyi
2670
-
NADPH
wild type enzyme, in 50 mM phosphate buffer, pH 7.0, at 22C
Vibrio harveyi
Other publictions for EC 1.5.1.38
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
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)
741937
Musila
Transformation of a flavin-fr ...
Escherichia coli
Biochemistry
55
6389-6394
2016
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2
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741865
Gwenin
Identification of novel nitro ...
Bacillus cereus, Bacillus cereus ATCC 14579
Biochem. Pharmacol.
98
392-402
2015
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1
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1
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4
1
1
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1
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1
1
741896
Driggers
Crystal structure of Escheric ...
Escherichia coli
Biochemistry
53
3509-3519
2014
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1
1
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1
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2
2
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3
3
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724343
Chung
Structure-function relationshi ...
Vibrio harveyi
Biochemistry
51
4880-4887
2012
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1
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5
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4
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1
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1
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1
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4
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1
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5
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1
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4
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6
6
672426
Gao
Mechanism of flavin reduction ...
Escherichia coli
Biochim. Biophys. Acta
1774
359-367
2007
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1
1
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674310
Abdurachim
Detection of protein-protein i ...
Escherichia coli
J. Bacteriol.
188
8153-8159
2006
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713622
Gao
Crystallization and preliminar ...
Escherichia coli
Acta Crystallogr. Sect. F
61
837-840
2005
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1
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1
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438770
Eichhorn
Characterization of a two-comp ...
Escherichia coli
J. Biol. Chem.
274
26639-26646
1999
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1
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1
4
-
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3
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1
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1
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4
1
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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3
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1
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4
1
1
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1
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1
1
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4
4
392200
Lei
Mechanism of reduced flavin tr ...
Vibrio harveyi
Biochemistry
37
14623-14629
1998
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1
3
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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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6
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1
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1
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1
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1
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6
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1
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1
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5
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1
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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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1
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1
1
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392297
Lei
Vibrio harveyi NADPH-flavin ox ...
Vibrio harveyi
J. Bacteriol.
176
3552-3558
1994
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1
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2
2
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1
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392180
Jablonski
Purification and properties of ...
Vibrio harveyi, Vibrio harveyi No. 392
Biochemistry
16
2932-2936
1977
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7
4
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1
2
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4
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1
1
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8
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1
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1
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1
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7
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1
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1
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392179
Gerlo
Identification of NADH-specifi ...
Vibrio harveyi
Eur. J. Biochem.
57
461-467
1975
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