Chemical and mechanistic approaches to the study of protein tyrosine phosphatases

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106 Citations (Scopus)

Abstract

Protein tyrosine phosphatases (PTPs) are signaling enzymes that control a diverse array of cellular processes. Site-directed mutagenesis, combined with detailed kinetic and mechanistic studies of Yersinia PTP, have contributed greatly to the understanding of the chemical mechanism for PTP catalysis, the nature of the enzymatic transition state, and the means by which the transition state is stabilized. Significant progress has been made in developing specific small-molecule inhibitors as tools to dissect the functional roles of PTP both in normal physiology and pathological conditions. Despite the conserved structural and catalytic properties, recent results show that there are sufficient differences in the PTPs so that potent and selective bidentate inhibitors that simultaneously bind both the active site and a unique adjacent site can be obtained.

Original languageEnglish (US)
Pages (from-to)385-392
Number of pages8
JournalAccounts of Chemical Research
Volume36
Issue number6
DOIs
StatePublished - Jun 1 2003
Externally publishedYes

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Protein Tyrosine Phosphatases
Mutagenesis
Physiology
Catalysis
Molecules
Kinetics
Enzymes

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Chemical and mechanistic approaches to the study of protein tyrosine phosphatases. / Zhang, Zhong-Yin.

In: Accounts of Chemical Research, Vol. 36, No. 6, 01.06.2003, p. 385-392.

Research output: Contribution to journalArticle

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