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