Enzyme kinetic characterization of protein tyrosine phosphatases

Günther H.J. Peters, S. Branner, K. B. Møller, J.N. Andersen, N.P.H. Møller

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

Protein tyrosine phosphatases (PTPs) play a central role in cellular signaling processes, resulting in an increased interest in modulating the activities of PTPs. We therefore decided to undertake a detailed enzyme kinetic evaluation of various transmembrane and cytosolic PTPs (PTPalpha, PTPbeta, PTPis an element of, CD45, LAR, PTP1B and SHP-1), using pNPP as substrate. Most noticeable is the increase in the turnover number for PTPbeta with increasing pH and the weak pH-dependence of the turnover number of CD45. The kinetic data for PTPalpha-D1 and PTPalpha-D1D2 suggest that D2 affects the catalysis of pNPP. PTPis an element of and the closely homologous PTPalpha behave differently. The K-m data were lower for PTPis an element of than those for PTPalpha, while the inverse was observed for the catalytic efficiencies.
Original languageEnglish
JournalBiochimie
Volume85
Issue number5
Pages (from-to)527-534
Number of pages8
ISSN0300-9084
DOIs
Publication statusPublished - 2003

Keywords

  • pH-profile
  • p-Nitrophenyl phosphate
  • Protein tyrosine phosphatase catalysis
  • Substrate recognition

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