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Literature summary for 1.5.1.41 extracted from

  • Caux, C.; Guigliarelli, B.; Vives, C.; Biaso, F.; Horeau, M.; Hassoune, H.; Petit-Hartlein, I.; Juillan-Binard, C.; Torelli, S.; Fieschi, F.; Niviere, V.
    Membrane-bound flavocytochrome MsrQ is a substrate of the flavin reductase Fre in Escherichia coli (2021), ACS Chem. Biol., 16, 2547-2559 .
    View publication on PubMed
Search for more literature for 1.5.1.41

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Escherichia coli 5829
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli enzyme Fre uses the FMN MsrQ cofactor as a substrate to catalyze the electron transfer from cytosolic NADH to the heme. Formation of a specific complex between MsrQ and Fre could favor this unprecedented mechanism, which most likely involves transfer of the reduced FMN cofactor from the Fre active site to MsrQ. Fre forms a specific complex with wild-type MsrQ and the MsrQ H151A mutant. The H151A mutation has no significant quantitative effects on the MsrQ/Fre interaction. Since the MsrQ H151A mutation specifically induces the loss of the FMN cofactor, these data suggest that the flavin cofactor is not involved in the formation of the MsrQ/Fre complex ?
-
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riboflavin + NADH + H+ Escherichia coli
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 reduced riboflavin + NAD+
-
 ?
riboflavin + NADPH + H+ Escherichia coli
-
 reduced riboflavin + NADP+
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AEN1
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme Fre uses the FMN MsrQ cofactor as a substrate to catalyze the electron transfer from cytosolic NADH to the heme. Formation of a specific complex between MsrQ and Fre could favor this unprecedented mechanism, which most likely involves transfer of the reduced FMN cofactor from the Fre active site to MsrQ. Fre forms a specific complex with wild-type MsrQ and the MsrQ H151A mutant. The H151A mutation has no significant quantitative effects on the MsrQ/Fre interaction. Since the MsrQ H151A mutation specifically induces the loss of the FMN cofactor, these data suggest that the flavin cofactor is not involved in the formation of the MsrQ/Fre complex Escherichia coli ?
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riboflavin + NADH + H+
-
 Escherichia coli reduced riboflavin + NAD+
-
 ?
riboflavin + NADPH + H+
-
 Escherichia coli reduced riboflavin + NADP+
-
 ?

Synonyms

Synonyms Comment Organism
flavin reductase
-
 Escherichia coli
fre
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Escherichia coli
NADPH
-
 Escherichia coli

General Information

General Information Comment Organism
physiological function the flavin reductase Fre in Escherichia coli reduces the cofactor FMN of MsrQ, that is part of MsrPQ, a distinct type of methionine sulfoxide reductase (Msr) system found in bacteria. It is specifically involved in the repair of periplasmic methionine residues that are oxidized by hypochlorous acid. MsrP is a periplasmic molybdoenzyme that carries out the Msr activity, whereas MsrQ, an integral membrane-bound hemoprotein, acts as the physiological partner of MsrP to provide electrons for catalysis. MsrQ holds a flavin mononucleotide (FMN) cofactor that occupies the site where a second heme binds in other members of the FDR superfamily on the cytosolic side of the membrane. EPR spectroscopy indicates that the FMN cofactor can accommodate a radical semiquinone species. The cytosolic flavin reductase Fre has previously been shown to reduce the MsrQ heme. Fre uses the FMN MsrQ cofactor as a substrate to catalyze the electron transfer from cytosolic NADH to the heme. Formation of a specific complex between MsrQ and Fre favors this unprecedented mechanism, which most likely involves transfer of the reduced FMN cofactor from the Fre active site to MsrQ Escherichia coli