2.3.1.37	additional information	-	additional information	-	486815, 486820, 486845	
2.3.1.37	additional information	-	additional information	kinetics analysis of wild-type and mutant enzymes, single and multiple turnover and stopped flow measurements, substrate protection study, overview	736116	
2.3.1.37	additional information	-	additional information	Michaelis-Menten steady-state kinetics, overview	735711	
2.3.1.37	additional information	-	additional information	Michaelis-Menten steady-state kinetics, two-step sequential kinetic mechanism , and thermodynamics. Both the reaction for wild-type hALAS2 and those for the X-linked protoporphyria variants comprised a single kinetic step associated with quinonoid intermediate formation followed by one decay step. Rates for the two steps range from 9.8-14.3/s and from 1.37-1.97 s for the reactions of the XLPP variants, whereas those for the wild-type hALAS2-catalyzed reaction are 6.6/s and 0.70/s	735684	
2.3.1.37	additional information	-	additional information	overview	486820	
2.3.1.37	additional information	-	additional information	pre-steady state and steady state kinetics, overview	736454	
2.3.1.37	additional information	-	additional information	pre-steady-state and steady-state kinetics of wild-type and mutant enzymes, stopped-flow measurements, single and mutiple turnover rates, equilibrium dissociation constants, binding isotherms, detailed overview	736491	
2.3.1.37	0.00032	-	glycine	pH 7.5, 30°C, ALAS(K313A mutant)/ALAS	718696	
2.3.1.37	0.00045	-	glycine	pH 7.5, 30°C, ALAS/ALAS	718696	
2.3.1.37	0.00054	-	butanoyl-CoA	mutant R85L/T430V, pH 7.5, 30°C	706627