1.5.1.41	FAD + NAD(P)H	-	Corynebacterium crenatum	FADH2 + NAD(P)+	-	r	375123	
1.5.1.41	FAD + NADH + H+	no activity with FAD + NADPH	Escherichia coli	FADH2 + NAD+	-	?	398873	
1.5.1.41	FAD + NADPH	-	Corynebacterium crenatum	FADH2 + NADP+	-	r	259299	
1.5.1.41	FMN + NAD(P)H	-	Corynebacterium crenatum	FMNH2 + NAD(P)+	-	r	375129	
1.5.1.41	FMN + NADH	-	Corynebacterium crenatum	FMNH2 + NAD+	-	r	287738	
1.5.1.41	FMN + NADH + H+	-	Escherichia coli	FMNH2 + NAD+	-	?	397183	
1.5.1.41	FMN + NADH + H+	-	Sulfurisphaera tokodaii	FMNH2 + NAD+	-	?	397183	
1.5.1.41	FMN + NADH + H+	-	Sulfurisphaera tokodaii 7	FMNH2 + NAD+	-	?	397183	
1.5.1.41	FMN + NADPH	-	Corynebacterium crenatum	FMNH2 + NADP+	-	r	259298	
1.5.1.41	FMN + NADPH + H+	very low activity	Escherichia coli	FMNH2 + NADP+	-	?	397184	
1.5.1.41	additional information	interactions for flavin substrates are provided by a hydrophobic isoalloxazine binding site that also contains a serine and a threonine, which form hydrogen bonds to the isoalloxazine of bound riboflavin in a substrate complex	Escherichia coli	?	-	?	89	
1.5.1.41	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	?	-	-	89	
1.5.1.41	riboflavin + NADH	preferred substrate	Corynebacterium crenatum	FMNH2 + NAD+	-	r	441958	
1.5.1.41	riboflavin + NADH + H+	-	Escherichia coli	reduced riboflavin + NAD+	-	?	401844	
1.5.1.41	riboflavin + NADPH + H+	-	Escherichia coli	reduced riboflavin + NADP+	-	?	406579