1.5.1.41: riboflavin reductase [NAD(P)H]
This is an abbreviated version!
For detailed information about riboflavin reductase [NAD(P)H], go to the full flat file.
Word Map on EC 1.5.1.41
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1.5.1.41
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nadph:flavin
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nadph
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fad
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ribonucleotide
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iron
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hydroxyurea
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isoalloxazine
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reductases
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prosthetic
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beneckea
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tyrosyl
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harveyi
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eliasson
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fmnh2
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donor-acceptor
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reichard
- 1.5.1.41
-
nadph:flavin
- nadph
- fad
-
ribonucleotide
- iron
- hydroxyurea
- isoalloxazine
-
reductases
-
prosthetic
-
beneckea
-
tyrosyl
- harveyi
-
eliasson
- fmnh2
-
donor-acceptor
-
reichard
Reaction
Synonyms
EC 1.5.1.29, EC 1.6.8.1, flavin reductase, flavin reductase HpaCSt, frd1, Frd181, fre, NAD(P)H-dependent H2O2-forming flavin reductase, NAD(P)H:flavin oxidoreductase
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General Information
General Information on EC 1.5.1.41 - riboflavin reductase [NAD(P)H]
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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
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