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Different kinetic patterns in the α-chymotrypsin-catalysed hydrolysis of synthetic ester substrates

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
190
Issue
2
Identifiers
DOI: 10.1016/0014-5793(85)81312-0
Disciplines
  • Biology

Abstract

Abstract The reaction of α-chymotrypsin with AcTyr-OEt and with AcTrp-OEt at pH 7.0 and 7.8 was studied over a wide range of substrate concentrations. The reaction with AcTyr-OEt at pH 7.8 was shown to be nonhyperbolic using a variety of criteria whereas those at pH 7.0 with the same substrate and at both pH values with AcTrp-OEt were hyperbolic. The non-hyperbolicity of the reaction with AcTyr-OEt at pH 7.8 followed a pattern of negative cooperativity with a Hill coefficient for the high substrate concentration range of 0.48. Although other explanations are possible, the pH dependence of the reaction with AcTyr-OEt could be related to the slow transition of the two known forms of the enzyme. Negative cooperativity Nonhyperbolic kinetics α-Chymotrypsin Hyperbolic kinetics Hill coefficient Slow transition

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