1.14.14.9	FAD	-	438900, 744140	
1.14.14.9	FAD	a flavoprotein, provides reduced flavin FAD- for the enzyme oxygenase component C2 to hydroxylate 4-hydroxyphenylacetate, the complex of C2-FADH2 reacts with oxygen to form C(4a)-hydroperoxy-FAD, the C2-FADH2-4-hydroxyphenylacetate complex reacts more slowly	674577	
1.14.14.9	FAD	alternative to FMN for C1	438900	
1.14.14.9	FAD	as redox chromophore	438893	
1.14.14.9	FAD	binding structure, binding causes conformational changes, overview	687633	
1.14.14.9	FAD	FAD is not tightly bound to HpaC, the flavin reductase component of the enzyme, and is bound in the groove in the extended and folded conformation, binding site structure, overview	689942	
1.14.14.9	FAD	flavoprotein monooxygenase, absolute requirement	438887, 438897	
1.14.14.9	FAD	FMN and FAD can substitute for each other, required	658203	
1.14.14.9	FAD	no stimulation	438894	
1.14.14.9	FAD	reduction of FAD is rate limiting	438896	
1.14.14.9	FAD	required for maximum activity, external flavoprotein monooxygenase	438895	
1.14.14.9	FAD	stimulates	438898, 438899	
1.14.14.9	FAD	tightly associated with small component, native cofactor	438900	
1.14.14.9	FADH2	-	438900, 726623, 726786, 727212	
1.14.14.9	FADH2	bound to the enzyme in vivo, which has a high affinity for FADH2, cosubstrate needs to be protected by the enzyme against oxidation to FAD by O2	658006	
1.14.14.9	FADH2	used as substrate and cofactor, enzyme binds FADH in absence of 4-hydroxyphenlyacetate and protects it from rapid autoxidation by O2	438896	
1.14.14.9	flavin	dependent on	727882	
1.14.14.9	FMN	-	438900, 699778, 727912	
1.14.14.9	FMN	a flavoprotein, provides reduced flavin FMNH- for the enzyme oxygenase component C2 to hydroxylate 4-hydroxyphenylacetate, the complex of C2-FMNH2 reacts with oxygen to form C(4a)-hydroperoxy-FMN, the C2-FMNH2-4-hydroxyphenylacetate complex reacts more slowly	674577	
1.14.14.9	FMN	a flavoprotein, provides reduced flavin for the oxygenase component of the enzyme to hydroxylate 4-hydroxyphenylacetate, the apoenzyme of the FMN reductase component C1 binds to oxidized FMN tightly in presence of the substrate	671960	
1.14.14.9	FMN	can substitute for FAD in the enzyme assay	689942	
1.14.14.9	FMN	dependent on	712503	
1.14.14.9	FMN	FMN and FAD can substitute for each other, required	658203	
1.14.14.9	FMN	involved in reaction step 1 catalyzed by the NADH-dependent FMN reductase enzyme component C1	689748	
1.14.14.9	FMN	native cofactor for C1 component	438900	
1.14.14.9	FMN	used as substrate by HpaC protein	438899	
1.14.14.9	FMN	utilized by C1	685182	
1.14.14.9	FMNH2	-	438900	
1.14.14.9	FMNH2	involved in reaction step 2 catalyzed by the monooxygenase enzyme component C2	689748	
1.14.14.9	FMNH2	utiluzed by C2	685182	
1.14.14.9	additional information	hydroxyphenylacetate forms a dead end complex with the (C2-C4a)-hydroxy-FMN intermediate inhibiting the bound flavin from returning to the oxidized form, FADH2 is equally active, the enzyme oxygenase component C2 has the unusual ability to use both common flavin cofactors in catalysis, kinetics, overview	674577	
1.14.14.9	additional information	no electron donor: NADH	764380	
1.14.14.9	additional information	similar enzyme which oxidizes both NADH and NADPH	288040	
1.14.14.9	NAD(P)H	-	687633	
1.14.14.9	NAD(P)H	product NAD+ is bound in the groove in the extended and folded conformation, binding site structure, overview	689942	
1.14.14.9	NADH	-	438893, 438898, 438899, 438900, 438901, 658006, 671960, 674577, 685182, 686265, 689748, 710753, 712503	
1.14.14.9	NADH	absolute requirement	438887	
1.14.14.9	NADH	can not be replaced by NADPH	288301, 438886	
1.14.14.9	NADH	dependent, not NADPH dependent	438894	
1.14.14.9	NADH	electron donor	438899	
1.14.14.9	NADH	required	658203	
1.14.14.9	NADH	unable to use NADPH	438895	
1.14.14.9	NADPH	-	438900, 710753	
1.14.14.9	riboflavin	-	438900	
1.14.14.9	riboflavin	component C1	438900	
1.14.14.9	riboflavin	used as substrate by HpaC protein	438899