Different primary specificity of porcine pancreatic β-kallikrein-B and bovine β-trypsin. A comparative steady-state and pre-steady-state study

Palo Ascenzi, Enea Menegatti, Mario Guarneri, Martino Bolognesi, Gino Amiconi

Research output: Contribution to journalArticlepeer-review

Abstract

The values of pre-steady-state and steady-state parameters for the β-trypsin catalyzed hydrolysis of Z-Arg-ONp and Z-Lys-ONp are superimposable between pH 2.4 and 8. At variance, the kinetic parameters for the β-kallikrein-B catalyzed hydrolysis of Z-Arg-ONp are more favourable than those observed for Z-Lys-ONp and depend on different pKa values. The different primary specificity and the catalytic behaviour of β-trypsin and β-kallikrein-B reflect structural differences at their S1 subsite, especially at level at the 226 residue as well as the 217-220 segment.

Original languageEnglish
Pages (from-to)99-103
Number of pages5
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume789
Issue number1
DOIs
Publication statusPublished - Aug 28 1984

Keywords

  • (Pancreas)
  • Kallikrein
  • Proteinase kinetics
  • Substrate specificity
  • Trypsin

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology
  • Structural Biology

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