BRENDA - Enzyme Database

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)
EC Number
Commentary
Organism
1.8.5.B1
expression in Escherichia coli
Escherichia coli
Engineering
EC Number
Amino acid exchange
Commentary
Organism
1.8.5.B1
H151A
mutant has aout 57% of the heme content of wild-type
Escherichia coli
1.8.5.B1
H164A
mutant has aout 63% of the heme content of wild-type
Escherichia coli
1.8.5.B1
H91A
almost complete loss of heme binding
Escherichia coli
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
1.8.5.B1
membrane
subunit MsrQ
Escherichia coli
16020
-
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.8.5.B1
Escherichia coli
P76342 and P76343
P76342 i.e. catalytic subunit MsrP, P76343 i.e. heme-binding subunit MsrQ
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.8.5.B1
additional information
subunit MsrQ is reduced due to the free reduced FMN generated by the flavin reductase Fre activity
742907
Escherichia coli
?
-
-
-
-
1.8.5.B1
[protein]-L-methionine + a quinone + H2O
-
742907
Escherichia coli
[protein]-L-methionine (R)-S-oxide + a quinol
-
-
-
r
1.8.5.B1
[protein]-L-methionine + a quinone + H2O
-
742907
Escherichia coli
[protein]-L-methionine (S)-S-oxide + a quinol
-
-
-
r
Subunits
EC Number
Subunits
Commentary
Organism
1.8.5.B1
More
protein physically interacts with flavin reductase Fre
Escherichia coli
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.8.5.B1
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)
EC Number
Commentary
Organism
1.8.5.B1
expression in Escherichia coli
Escherichia coli
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.8.5.B1
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)
EC Number
Amino acid exchange
Commentary
Organism
1.8.5.B1
H151A
mutant has aout 57% of the heme content of wild-type
Escherichia coli
1.8.5.B1
H164A
mutant has aout 63% of the heme content of wild-type
Escherichia coli
1.8.5.B1
H91A
almost complete loss of heme binding
Escherichia coli
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
1.8.5.B1
membrane
subunit MsrQ
Escherichia coli
16020
-
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.8.5.B1
additional information
subunit MsrQ is reduced due to the free reduced FMN generated by the flavin reductase Fre activity
742907
Escherichia coli
?
-
-
-
-
1.8.5.B1
[protein]-L-methionine + a quinone + H2O
-
742907
Escherichia coli
[protein]-L-methionine (R)-S-oxide + a quinol
-
-
-
r
1.8.5.B1
[protein]-L-methionine + a quinone + H2O
-
742907
Escherichia coli
[protein]-L-methionine (S)-S-oxide + a quinol
-
-
-
r
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.8.5.B1
More
protein physically interacts with flavin reductase Fre
Escherichia coli