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Results 1 - 5 of 5

EC Number	Natural Substrates	Commentary (Nat. Sub.)
1.5.1.41	FAD + NAD(P)H	-
1.5.1.41	FMN + NAD(P)H	-
1.5.1.41	more	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
1.5.1.41	riboflavin + NADH + H+	-
1.5.1.41	riboflavin + NADPH + H+	-

Results 1 - 5 of 5

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Release 2023.1 (January 2023)