Substrate activation of rat trypsins 1 and 2 |
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Authors: | A Vandermeers M C Vandermeers-Piret J Rathé J Christophe |
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Institution: | Department of Biochemistry and Nutrition, Brussels University School of Medicine, 1000 Brussels, Belgium |
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Abstract: | Qualitative differences in the active center of rat trypsins 1 and 2 resulted in different ratios of Kcat for N1-tosyl-l-arginine methyl ester vs Kcat for N1-benzoyl-l-arginine ethyl ester. These ratios were 2.5 for trypsin 1 and 1.2 for trypsin 2.Substrate activation with N1-tosyl-l-arginine methyl ester enhanced the catalytic rate constant of rat trypsin 1 2.5-fold and that of rat trypsin 2 only 1.5-fold. The increase in the catalytic rate constant found with N1-benzoyl-l-arginine ethyl ester was the same (1.5-fold) for both trypsins. Consequently, at 20 mm substrate concentration, trypsin 1 catalyzed the esterolysis of N1-tosyl-l-arginine methyl ester 4.5 times faster than that of N1-benzoyl-l-arginine ethyl ester, while trypsin 2 was only 1.3 times more efficient with the first substrate.Furthermore, the activation of both rat enzymes by N-acetyl-l-tyrosine ethyl ester was even more effective than that obtained with the two cationic esters; the maximum rates of hydrolysis of this neutral substrate by trypsins 1 and 2 were enhanced 120- and 50-fold, respectively, by high concentrations of N-acetyl-l-tyrosine ethyl ester. |
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