Design and synthesis of class-selective activity probes for protein tyrosine phosphatases

J Proteome Res. 2002 Jan-Feb;1(1):35-40. doi: 10.1021/pr015506a.

Abstract

Two mechanism-based activity probes, adopting a cassette-like design, for protein tyrosine phosphatases (PTPs) were synthesized. Both probes carry a phosphate group that serves as the recognition head for the target PTPs but differ in their reporter groups; probe LCL-1 uses a dansyl fluorophore, while LCL-2 has a biotin reporter group. LCL-1 and LCL-2 are specifically activated by phosphatase, leading to its covalent labeling, as exemplified with PTP-1B. However, they show no activation with other classes of hydrolases, including trypsin and beta-galactosidase. LCL-1 and LCL-2 thus represent the first example of class-selective probes for phosphatases.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Enzyme Activation
  • Molecular Probes / chemical synthesis*
  • Molecular Probes / chemistry*
  • Molecular Structure
  • Protein Tyrosine Phosphatase, Non-Receptor Type 1
  • Protein Tyrosine Phosphatases / chemistry
  • Protein Tyrosine Phosphatases / metabolism*
  • Sensitivity and Specificity
  • Substrate Specificity

Substances

  • Molecular Probes
  • Protein Tyrosine Phosphatase, Non-Receptor Type 1
  • Protein Tyrosine Phosphatases