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Y Jacquot-Armand1, M Hill

  • 1Laboratoire de Biologie Physico-Chimique, Faculté des Sciences, 91, Orsay, France

FEBS Letters
|December 11, 1970
PubMed
Summary
This summary is machine-generated.

Tryptic hydrolysis rates vary significantly with substrate structure. Replacing the benzoyl group with carbobenzoxy in arginine nitroanilides (BAPNA to L-ZAPNA) enhances tryptic hydrolysis, influenced by enzyme charge.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Proteolysis

Background:

  • Tryptic hydrolysis of arginine nitroanilides is crucial for understanding enzyme kinetics.
  • Substrate structure significantly impacts enzyme activity and specificity.

Purpose of the Study:

  • To investigate the effect of different arginine nitroanilide structures on tryptic hydrolysis.
  • To determine kinetic constants for native and Nepsilon-acetylated trypsin using L-ZAPNA.
  • To explore the relationship between enzyme charge and hydrolysis rate.

Main Methods:

  • Studied tryptic hydrolysis of various arginine nitroanilide substrates.
  • Synthesized and utilized N-alpha-benzyloxycarbonyl-L-arginine p-nitroanilide (L-ZAPNA).
  • Determined kinetic constants for porcine and bovine trypsin (native and Nepsilon-acetylated forms).

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Main Results:

  • Para-nitroanilide was the most readily hydrolyzed substrate.
  • Ortho and meta derivatives showed significantly lower hydrolysis rates.
  • Replacing benzoyl with carbobenzoxy group (L-ZAPNA) increased hydrolysis by threefold.
  • Hydrolysis rate correlated with both global and local charges of the trypsin enzyme.

Conclusions:

  • Arginine nitroanilide structure critically affects tryptic hydrolysis.
  • L-ZAPNA is a more sensitive substrate for trypsin activity assessment.
  • Enzyme charge plays a key role in modulating tryptic hydrolysis rates.