1.14.13.196	additional information	-	additional information	monitoring the reductive and oxidative half-reactions of a flavin-dependent monooxygenase using stopped-flow spectrophotometry	725851	
1.14.13.196	additional information	-	additional information	presteady-state kinetic parameters, cofactor: NADPH	725540	
1.14.13.196	0.03	-	L-ornithine	pH 7.6, 25°C, mutant enzyme S257A, cofactor: NADPH	725540	
1.14.13.196	0.03	-	L-ornithine	pH 7.6, 25°C, wild-type enzyme, cofactor: NADPH	725540	
1.14.13.196	0.2	-	L-ornithine	recombinant FAD-reconstituted enzyme-enzyme, pH 7.5, temperature not specified in the publication	745824	
1.14.13.196	0.34	-	L-ornithine	recombinant holo-enzyme, pH 7.5, temperature not specified in the publication	745824	
1.14.13.196	0.48	-	L-ornithine	pH 7.5, 25°C, cosubstrate: NADPH, following the formation of hydroxylated ornithine	724289	
1.14.13.196	0.5	-	L-ornithine	pH 7.5, 25°C, cosubstrate: NADH, following the formation of hydroxylated ornithine	724289	
1.14.13.196	0.6	-	NADPH	pH 7.5, temperature not specified in the publication	724451	
1.14.13.196	0.6	-	NADPH	pH 7.6, 25°C, wild-type enzyme	725540	
1.14.13.196	0.63	-	NADPH	pH 7.5, 25°C, oxygen consumption assay	724289	
1.14.13.196	0.68	-	L-ornithine	pH 7.5, 25°C, cosubstrate: NADH, oxygen consumption assay	724289	
1.14.13.196	0.73	-	NADH	pH 7.5, temperature not specified in the publication	724451	
1.14.13.196	0.85	-	NADPH	pH 7.6, 25°C, mutant enzyme S257A	725540	
1.14.13.196	0.87	-	L-ornithine	pH 7.5, 25°C, cosubstrate: NADPH, oxygen consumption assay	724289	
1.14.13.196	1.18	-	NADH	pH 7.5, 25°C, following the formation of hydroxylated ornithine	724289	
1.14.13.196	1.25	-	NADPH	pH 7.5, 25°C, following the formation of hydroxylated ornithine	724289	
1.14.13.196	1.36	-	NADH	pH 7.5, 25°C, oxygen consumption assay	724289