BRENDA - Enzyme Database
show all sequences of 1.5.1.41

Characterization of the flavin reductase gene (fre) of Escherichia coli and construction of a plasmid for overproduction of the enzyme

Spyrou, G.; Haggard-Ljungquist, E.; Krook, M.; Joernvall, H.; Nilsson, E.; Reichard, P.; J. Bacteriol. 173, 3673-3679 (1991)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
construction of a bacterial strain that overproduces the enzyme approximately 100fold
Escherichia coli
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
26212
-
x * 26212, calculated from sequence
Escherichia coli
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
P0AEN1
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
riboflavin + NADPH + H+
-
392192
Escherichia coli
reduced riboflavin + NADP+
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 26212, calculated from sequence
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
construction of a bacterial strain that overproduces the enzyme approximately 100fold
Escherichia coli
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
26212
-
x * 26212, calculated from sequence
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
riboflavin + NADPH + H+
-
392192
Escherichia coli
reduced riboflavin + NADP+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 26212, calculated from sequence
Escherichia coli
General Information
General Information
Commentary
Organism
physiological function
in Escherichia coli NAD(P)H:flavin oxidoreductase is part of a multienzyme system that reduces the Fe(III) center of ribonucleotide reductase to Fe(II) and thereby sets the stage for the generation by dioxygen of a free tyrosyl radical required for enzyme activity
Escherichia coli
General Information (protein specific)
General Information
Commentary
Organism
physiological function
in Escherichia coli NAD(P)H:flavin oxidoreductase is part of a multienzyme system that reduces the Fe(III) center of ribonucleotide reductase to Fe(II) and thereby sets the stage for the generation by dioxygen of a free tyrosyl radical required for enzyme activity
Escherichia coli
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
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2
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6
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1
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6
-
1
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5
1
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4
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1
4
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1
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5
-
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2
-
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1
-
-
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-
6
-
1
-
-
5
1
-
-
-
-
-
-
-
5
5
720976
Okai
High pressure refolding, purif ...
Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7
Protein Expr. Purif.
84
214-218
2012
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-
1
1
-
-
-
-
-
-
-
-
-
12
-
-
1
-
-
-
-
-
2
-
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1
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1
1
1
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1
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2
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-
392202
Ingelman
Crystal structure of NAD(P)H:f ...
Escherichia coli
Biochemistry
38
7040-7049
1999
-
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1
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1
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1
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1
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1
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1
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1
-
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-
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-
-
-
-
-
-
-
-
-
-
-
392192
Spyrou
Characterization of the flavin ...
Escherichia coli
J. Bacteriol.
173
3673-3679
1991
-
-
1
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
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1
1
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1
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1
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-
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1
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
392190
Fontecave
NAD(P)H:flavin oxidoreductase ...
Escherichia coli
J. Biol. Chem.
262
12325-12331
1987
-
-
-
-
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1
3
7
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1
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1
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1
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1
-
5
1
1
-
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1
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1
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1
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-
-
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1
-
3
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7
-
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1
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1
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1
-
5
1
1
-
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1
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1
1
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