BRENDA - Enzyme Database
show all sequences of 1.8.5.B1

A two-component NADPH oxidase (NOX)-like system in bacteria is involved in the electron transfer chain to the methionine sulfoxide reductase MsrP

Juillan-Binard, C.; Picciocchi, A.; Andrieu, J.P.; Dupuy, J.; Petit-Hartlein, I.; Caux-Thang, C.; Vives, C.; Niviere, V.; Fieschi, F.; J. Biol. Chem. 292, 2485-2494 (2017)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Escherichia coli
Engineering
Amino acid exchange
Commentary
Organism
H151A
mutant has aout 57% of the heme content of wild-type
Escherichia coli
H164A
mutant has aout 63% of the heme content of wild-type
Escherichia coli
H91A
almost complete loss of heme binding
Escherichia coli
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
subunit MsrQ
Escherichia coli
16020
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
P76342 and P76343
P76342 i.e. catalytic subunit MsrP, P76343 i.e. heme-binding subunit MsrQ
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
subunit MsrQ is reduced due to the free reduced FMN generated by the flavin reductase Fre activity
742907
Escherichia coli
?
-
-
-
-
[protein]-L-methionine + a quinone + H2O
-
742907
Escherichia coli
[protein]-L-methionine (R)-S-oxide + a quinol
-
-
-
r
[protein]-L-methionine + a quinone + H2O
-
742907
Escherichia coli
[protein]-L-methionine (S)-S-oxide + a quinol
-
-
-
r
Subunits
Subunits
Commentary
Organism
More
protein physically interacts with flavin reductase Fre
Escherichia coli
Cofactor
Cofactor
Commentary
Organism
Structure
heme
heme/protein ratio is 2.5. The extinction coefficient value for the oxidized subunit MsrQ form at 412 nm is 51950 per M and cm. For the reduced MsrQ form at 426 and 558 nm, the extinction coefficient values are 69015 per M and cm and 11075 per M and cm, respectively
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
heme
heme/protein ratio is 2.5. The extinction coefficient value for the oxidized subunit MsrQ form at 412 nm is 51950 per M and cm. For the reduced MsrQ form at 426 and 558 nm, the extinction coefficient values are 69015 per M and cm and 11075 per M and cm, respectively
Escherichia coli
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
H151A
mutant has aout 57% of the heme content of wild-type
Escherichia coli
H164A
mutant has aout 63% of the heme content of wild-type
Escherichia coli
H91A
almost complete loss of heme binding
Escherichia coli
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
subunit MsrQ
Escherichia coli
16020
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
subunit MsrQ is reduced due to the free reduced FMN generated by the flavin reductase Fre activity
742907
Escherichia coli
?
-
-
-
-
[protein]-L-methionine + a quinone + H2O
-
742907
Escherichia coli
[protein]-L-methionine (R)-S-oxide + a quinol
-
-
-
r
[protein]-L-methionine + a quinone + H2O
-
742907
Escherichia coli
[protein]-L-methionine (S)-S-oxide + a quinol
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
More
protein physically interacts with flavin reductase Fre
Escherichia coli
Other publictions for EC 1.8.5.B1
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)
742907
Juillan-Binard
A two-component NADPH oxidase ...
Escherichia coli
J. Biol. Chem.
292
2485-2494
2017
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743348
Gennaris
Repairing oxidized proteins i ...
Escherichia coli
Nature
528
409-412
2015
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3
1
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742828
Loschi
Structural and biochemical id ...
Escherichia coli
J. Biol. Chem.
279
50391-50400
2004
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1
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5
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1
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5
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1
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1
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1
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5
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5
5