3.4.21.62	additional information	-	additional information	-	29427, 29448, 29459, 29480	
3.4.21.62	additional information	-	additional information	kinetic analysis of the perhydrolytic wild-type and mutant enzyme activities, overview	732207	
3.4.21.62	additional information	-	additional information	Km of subtilisin Novo chemically attached to soluble DEAE-dextran and insoluble DEAE-Sephadex	29471	
3.4.21.62	additional information	-	additional information	Michaelis-Menten kinetics and thermodynamics	752829	
3.4.21.62	additional information	-	additional information	Michaelis-Menten kinetics using Lineweaver-Burk and Hanes plots	752524	
3.4.21.62	additional information	-	additional information	Michaelis-Menten kinetics using Lineweaver-Burk and Hanes plots at pH 8.5 and 22°C, purified recombinant enzyme	731172	
3.4.21.62	additional information	-	additional information	Michaelis-Menten kinetics, Km is 0.175% w/v	754435	
3.4.21.62	additional information	-	additional information	the temperature dependence of the kinetics and thermodynamic parameters suggest that the enzyme exists in two, i.e. cold and hot forms, at 22°C the cold form turns into the hot one possibly owing to a conformational change	29458	
3.4.21.62	0.000655	-	N-succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide	37°C, pH 10.5	669738	
3.4.21.62	0.0027	-	Suc-Ala-Ala-Pro-Phe-4-nitroanilide	1 mol lactose bound per 1 mol subtilisin, in 10 mM potassium phosphate buffer, pH 7.8, at 25°C	707805