Quiescent affinity inactivators of protein tyrosine phosphatases

William P. Taylor, Zhong Yin Zhang, Theodore S. Widlanski

Research output: Contribution to journalArticlepeer-review

39 Scopus citations

Abstract

-Halobenzylphosphonates were investigated as possible inactivators of protein tyrosine phosphatases (PTPases). These compounds inactivate the Yersinia PTPase (Yop51*Δ162) in a time- and concentration-dependent fashion. This inactivation is active-site directed and irreversible, and is surprisingly rapid in light of the stability of the α-halobenzylphosphonates toward nucleophiles in solution. The potential of these molecules for probing the stereochemistry of PTPase inactivation, as well as for providing a useful paradigm for the design of more potent PTPase inhibitors is discussed.

Original languageEnglish (US)
Pages (from-to)1515-1520
Number of pages6
JournalBioorganic and Medicinal Chemistry
Volume4
Issue number9
DOIs
StatePublished - Jan 1 1996
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry

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