1.14.14.21	FADH2	-	735785	
1.14.14.21	FMNH2	-	392304, 658301, 735524, 735525, 735526, 735527, 735585, 735785, 735798, 735833, 736146, 736522, 736585, 736855, 737211	
1.14.14.21	FMNH2	enzyme DszC-FMN crystal structure analysis, FMN-binding site, binding structure and mechanism, modeling, overview	736092	
1.14.14.21	FMNH2	reduced FMN reacts with an oxygen molecule at C4a position of the isoalloxazine ring, producing the C4a-(hydro)peroxyflavin intermediate which is stabilized by residues H391 and S163. H391 may contribute to the formation of the C4a-(hydro)peroxyflavin by acting as a proton donor to the proximal peroxy oxygen, and it might also be involved in the protonation process of C4a-(hydro)peroxyflavin, molecular docking simulation and modeling, overview	737210	
1.14.14.21	FMNH2	the enzyme binds one flavin mononucleotide or reduced flavin mononucleotide (FMNH2) per 90,200-Da homodimer, and FMNH2 is an essential cosubstrate for its activity	736340	
1.14.14.21	FMNH2	the reduced form of flavin serves as a substrate of DszC	735584	
1.14.14.21	additional information	FAD and lumiflavin have only weak activity as reducing agents	735526	
1.14.14.21	additional information	flavin reductaseFRP is essentially required for enzyme activity providing reduction equivalents, Vibrio harveyi FRP produces FMNH2 at the expense of NADPH and is used to provide FMNH2 for the enzymatic reaction	736340	
1.14.14.21	additional information	flavin specificity, overview. No activity with FADH2	736340	
1.14.14.21	additional information	FMN oxidoreductase TdsD, a NADH-dependent FMN oxidoreductase, absolutely required for TdsC activity, maximum activity is obtained at a TdsD/TdsC molar ratio of 0.5, no activity in the absence of TdsD	735526	
1.14.14.21	additional information	no direct activity with NAD(P)H	735584	
1.14.14.21	additional information	the enzyme requires NADH, FMNH2, oxygen, and the aid of NADH-FMN oxidoreductase to catalyze the conversion of dibenzothiophene	736585	
1.14.14.21	additional information	the flavin reductase, EC 1.5.1.36, from Rhodococcus erythropolis strain D-1 grown in a medium containing dibenzothiophene as the sole source of sulfur is essential for the reactions of the two monooxygenases DszC and DszA in vivo. The purified flavin reductase contains no chromogenic cofactors and has a molecular mass of 86 kDa and four identical 22-kDa subunits. The enzyme catalyzes NADH-dependent reduction of flavin mononucleotide, FMN. The flavin reductase does not catalyze reduction of any nitroaromatic compound	392304	
1.14.14.21	additional information	the recombinant enzyme is able to utilize either FMNH2 or FADH2 when coupled with a flavin reductase that reduces either FMN or FAD	735785	
1.14.14.21	NADH	-	735526, 736585	
1.14.14.21	NADH	DszD is responsible for supplying reducing equivalents in the form of FMNH2 to the monooxygenase DszC	737211	
1.14.14.21	NADH	the enzyme does not directly react with NADH, but uses the activity of the FMN:NADH oxidoreductase, DszD	736855	
1.14.14.21	NADPH	can substitute for NADH to some extent	735526	
1.14.14.21	riboflavin	low activity	736340