BRENDA - Enzyme Database
show all sequences of 1.5.1.41

Improvement of the intracellular environment for enhancing L-arginine production of Corynebacterium glutamicum by inactivation of H2O2-forming flavin reductases and optimization of ATP supply

Man, Z.; Rao, Z.; Xu, M.; Guo, J.; Yang, T.; Zhang, X.; Xu, Z.; Metab. Eng. 38, 310-321 (2016)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene frd1, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant overexpression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
Corynebacterium crenatum
Engineering
Amino acid exchange
Commentary
Organism
additional information
improvement of the intracellular environment for enhancing L-arginine production of Corynebacterium glutamicum by inactivation of H2O2-forming flavin reductases and optimization of ATP supply. Construction of mutants of gene frd1, strain 5-5(frd1) and deletion strains 5-5DELTAfrd1 and 5-5DELTAfrd12. The extracellular H2O2 concentrations of mutants 5-5DELTAfrd1 and 5-5DELTAfrd12 are lower than that of the wild-type strain SYPA5-5, and the extracellular H2O2 concentrations of mutant 5-5(frd1) is increased compared to the wild-type. Flavin reductase activities in frd1 and frd2 overexpression and deletion strains with NADH and FAD, overview
Corynebacterium crenatum
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0044
-
NADH
with riboflavin, pH 7.5, 30°C, recombinant enzyme
Corynebacterium crenatum
0.0052
-
NADH
with FMN, pH 7.5, 30°C, recombinant enzyme
Corynebacterium crenatum
0.0056
-
NADH
with FAD, pH 7.5, 30°C, recombinant enzyme
Corynebacterium crenatum
0.0068
-
NADPH
with FMN, pH 7.5, 30°C, recombinant enzyme
Corynebacterium crenatum
0.0085
-
NADPH
with FAD, pH 7.5, 30°C, recombinant enzyme
Corynebacterium crenatum
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
FAD + NAD(P)H
Corynebacterium crenatum
-
FADH2 + NAD(P)+
-
-
r
FMN + NAD(P)H
Corynebacterium crenatum
-
FMNH2 + NAD(P)+
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Corynebacterium crenatum
-
-
-
Corynebacterium crenatum SYPA5-5
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant N-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Corynebacterium crenatum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
FAD + NAD(P)H
-
743224
Corynebacterium crenatum
FADH2 + NAD(P)+
-
-
-
r
FAD + NADPH
-
743224
Corynebacterium crenatum
FADH2 + NADP+
-
-
-
r
FMN + NAD(P)H
-
743224
Corynebacterium crenatum
FMNH2 + NAD(P)+
-
-
-
r
FMN + NADH
-
743224
Corynebacterium crenatum
FMNH2 + NAD+
-
-
-
r
FMN + NADPH
-
743224
Corynebacterium crenatum
FMNH2 + NADP+
-
-
-
r
riboflavin + NADH
preferred substrate
743224
Corynebacterium crenatum
FMNH2 + NAD+
-
-
-
r
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Corynebacterium crenatum
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.061
-
NADPH
with FAD, pH 7.5, 30°C, recombinant enzyme
Corynebacterium crenatum
0.069
-
NADPH
with FMN, pH 7.5, 30°C, recombinant enzyme
Corynebacterium crenatum
0.09
-
NADH
with FMN, pH 7.5, 30°C, recombinant enzyme
Corynebacterium crenatum
0.547
-
NADH
with riboflavin, pH 7.5, 30°C, recombinant enzyme
Corynebacterium crenatum
0.603
-
NADH
with FAD, pH 7.5, 30°C, recombinant enzyme
Corynebacterium crenatum
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Corynebacterium crenatum
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Corynebacterium crenatum
NADH
-
Corynebacterium crenatum
NADP+
-
Corynebacterium crenatum
NADPH
-
Corynebacterium crenatum
Cloned(Commentary) (protein specific)
Commentary
Organism
gene frd1, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant overexpression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
Corynebacterium crenatum
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Corynebacterium crenatum
NADH
-
Corynebacterium crenatum
NADP+
-
Corynebacterium crenatum
NADPH
-
Corynebacterium crenatum
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
improvement of the intracellular environment for enhancing L-arginine production of Corynebacterium glutamicum by inactivation of H2O2-forming flavin reductases and optimization of ATP supply. Construction of mutants of gene frd1, strain 5-5(frd1) and deletion strains 5-5DELTAfrd1 and 5-5DELTAfrd12. The extracellular H2O2 concentrations of mutants 5-5DELTAfrd1 and 5-5DELTAfrd12 are lower than that of the wild-type strain SYPA5-5, and the extracellular H2O2 concentrations of mutant 5-5(frd1) is increased compared to the wild-type. Flavin reductase activities in frd1 and frd2 overexpression and deletion strains with NADH and FAD, overview
Corynebacterium crenatum
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0044
-
NADH
with riboflavin, pH 7.5, 30°C, recombinant enzyme
Corynebacterium crenatum
0.0052
-
NADH
with FMN, pH 7.5, 30°C, recombinant enzyme
Corynebacterium crenatum
0.0056
-
NADH
with FAD, pH 7.5, 30°C, recombinant enzyme
Corynebacterium crenatum
0.0068
-
NADPH
with FMN, pH 7.5, 30°C, recombinant enzyme
Corynebacterium crenatum
0.0085
-
NADPH
with FAD, pH 7.5, 30°C, recombinant enzyme
Corynebacterium crenatum
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
FAD + NAD(P)H
Corynebacterium crenatum
-
FADH2 + NAD(P)+
-
-
r
FMN + NAD(P)H
Corynebacterium crenatum
-
FMNH2 + NAD(P)+
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant N-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Corynebacterium crenatum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
FAD + NAD(P)H
-
743224
Corynebacterium crenatum
FADH2 + NAD(P)+
-
-
-
r
FAD + NADPH
-
743224
Corynebacterium crenatum
FADH2 + NADP+
-
-
-
r
FMN + NAD(P)H
-
743224
Corynebacterium crenatum
FMNH2 + NAD(P)+
-
-
-
r
FMN + NADH
-
743224
Corynebacterium crenatum
FMNH2 + NAD+
-
-
-
r
FMN + NADPH
-
743224
Corynebacterium crenatum
FMNH2 + NADP+
-
-
-
r
riboflavin + NADH
preferred substrate
743224
Corynebacterium crenatum
FMNH2 + NAD+
-
-
-
r
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Corynebacterium crenatum
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.061
-
NADPH
with FAD, pH 7.5, 30°C, recombinant enzyme
Corynebacterium crenatum
0.069
-
NADPH
with FMN, pH 7.5, 30°C, recombinant enzyme
Corynebacterium crenatum
0.09
-
NADH
with FMN, pH 7.5, 30°C, recombinant enzyme
Corynebacterium crenatum
0.547
-
NADH
with riboflavin, pH 7.5, 30°C, recombinant enzyme
Corynebacterium crenatum
0.603
-
NADH
with FAD, pH 7.5, 30°C, recombinant enzyme
Corynebacterium crenatum
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Corynebacterium crenatum
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
7.18
-
NADPH
with FAD, pH 7.5, 30°C, recombinant enzyme
Corynebacterium crenatum
10.15
-
NADPH
with FMN, pH 7.5, 30°C, recombinant enzyme
Corynebacterium crenatum
17.31
-
NADH
with FMN, pH 7.5, 30°C, recombinant enzyme
Corynebacterium crenatum
107.68
-
NADH
with FAD, pH 7.5, 30°C, recombinant enzyme
Corynebacterium crenatum
136.75
-
NADH
with riboflavin, pH 7.5, 30°C, recombinant enzyme
Corynebacterium crenatum
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
7.18
-
NADPH
with FAD, pH 7.5, 30°C, recombinant enzyme
Corynebacterium crenatum
10.15
-
NADPH
with FMN, pH 7.5, 30°C, recombinant enzyme
Corynebacterium crenatum
17.31
-
NADH
with FMN, pH 7.5, 30°C, recombinant enzyme
Corynebacterium crenatum
107.68
-
NADH
with FAD, pH 7.5, 30°C, recombinant enzyme
Corynebacterium crenatum
136.75
-
NADH
with riboflavin, pH 7.5, 30°C, recombinant enzyme
Corynebacterium crenatum
Other publictions for EC 1.5.1.41
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)
743224
Man
Improvement of the intracellu ...
Corynebacterium crenatum, Corynebacterium crenatum SYPA5-5
Metab. Eng.
38
310-321
2016
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1
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1
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5
-
-
-
2
-
6
-
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1
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-
-
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-
6
-
1
-
-
5
1
-
-
4
-
-
-
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-
1
4
-
1
-
-
-
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5
-
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2
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1
-
-
-
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6
-
1
-
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5
1
-
-
-
-
-
-
-
5
5
720976
Okai
High pressure refolding, purif ...
Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7
Protein Expr. Purif.
84
214-218
2012
-
-
1
1
-
-
-
-
-
-
-
-
-
12
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
392202
Ingelman
Crystal structure of NAD(P)H:f ...
Escherichia coli
Biochemistry
38
7040-7049
1999
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
392192
Spyrou
Characterization of the flavin ...
Escherichia coli
J. Bacteriol.
173
3673-3679
1991
-
-
1
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
392190
Fontecave
NAD(P)H:flavin oxidoreductase ...
Escherichia coli
J. Biol. Chem.
262
12325-12331
1987
-
-
-
-
-
1
3
7
-
-
1
-
-
1
-
-
1
-
-
-
1
-
5
1
1
-
-
-
1
-
1
-
-
1
-
-
-
-
-
-
-
1
-
3
-
7
-
-
1
-
-
-
-
1
-
-
1
-
5
1
1
-
-
-
1
-
1
1
-
-
-
-
-
-