Identification of the rate-limiting step in serine proteinases from the effect of temperature on steady-state kinetics

Paul F. Fitzpatrick

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

The effect of temperature on the steady-state kinetics of porcine pancreatic elastase can be used to determine whether acylation or deacylation is the rate-limiting step in catalysis. If acylation is rate-limiting, kcat and kcat/Km will show the same temperature dependence. If deacylation is rate-limiting, kcat will show a greater temperature dependence than kcat/Km. The temperature dependence of the steady-state kinetic parameters of t-Boc-Ala-Ala-Pro-Ala p-nitroanilide and N-acetyl-Ala-Ala-α-Aza-Ala p-nitrophenyl ester have been determined and are consistent with this prediction.

Original languageEnglish (US)
Pages (from-to)201-203
Number of pages3
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume995
Issue number2
DOIs
StatePublished - Apr 6 1989

Keywords

  • Elastase, Kinetics, Proteinase
  • Temperature

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology

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