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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

Reaction

reduced riboflavin
+
NAD(P)+
=
riboflavin
+
NAD(P)H
+
H+

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

ECTree

     1 Oxidoreductases
         1.5 Acting on the CH-NH group of donors
             1.5.1 With NAD+ or NADP+ as acceptor
                1.5.1.41 riboflavin reductase [NAD(P)H]

Natural Substrates Products

Natural Substrates Products on EC 1.5.1.41 - riboflavin reductase [NAD(P)H]

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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
FAD + NAD(P)H
FADH2 + NAD(P)+
show the reaction diagram
-
-
-
-
r
FMN + NAD(P)H
FMNH2 + NAD(P)+
show the reaction diagram
-
-
-
-
r
riboflavin + NADH + H+
reduced riboflavin + NAD+
show the reaction diagram
-
-
-
?
riboflavin + NADPH + H+
reduced riboflavin + NADP+
show the reaction diagram
-
-
-
?
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
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-
-