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Results 1 - 10 of 158 > >>
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Reference
-999
-
more
kinetic analysis of the perhydrolytic wild-type and mutant enzyme activities, overview
-999
-
more
Km of subtilisin Novo chemically attached to soluble DEAE-dextran and insoluble DEAE-Sephadex
-999
-
more
Michaelis-Menten kinetics and thermodynamics
-999
-
more
Michaelis-Menten kinetics using Lineweaver-Burk and Hanes plots
-999
-
more
Michaelis-Menten kinetics using Lineweaver-Burk and Hanes plots at pH 8.5 and 22°C, purified recombinant enzyme
-999
-
more
Michaelis-Menten kinetics, Km is 0.175% w/v
-999
-
more
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
0.000655
-
N-succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide
37°C, pH 10.5
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
Results 1 - 10 of 158 > >>