Structure and function of the protein tyrosine phosphatases

Trends Biochem Sci. 1996 Nov;21(11):413-7. doi: 10.1016/s0968-0004(96)10059-1.

Abstract

The tyrosine and dual-specificity phosphatases are involved in signaling, cell growth and differentiation, and the cell cycle. The enzymes share a common catalytic mechanism mediated by an active site cysteine, arginine and aspartic acid. Supplementary domains assist in targeting and substrate specificity.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Cell Cycle Proteins / chemistry
  • Cell Cycle Proteins / metabolism
  • Cell Cycle Proteins / physiology
  • Conserved Sequence
  • Cyanobacteria / enzymology
  • Cyclin-Dependent Kinase Inhibitor Proteins
  • Dual-Specificity Phosphatases
  • Humans
  • Hydrolysis
  • Models, Molecular
  • Molecular Sequence Data
  • Molecular Weight
  • Phosphoprotein Phosphatases / metabolism
  • Phosphorylation
  • Phosphotyrosine / metabolism
  • Protein Conformation
  • Protein Tyrosine Phosphatases / chemistry*
  • Protein Tyrosine Phosphatases / metabolism*
  • Protein Tyrosine Phosphatases, Non-Receptor
  • Rhodobacter / enzymology
  • Saccharomyces cerevisiae Proteins*
  • Salmonella / enzymology
  • Substrate Specificity
  • Tyrosine / metabolism
  • cdc25 Phosphatases

Substances

  • CDC14 protein, S cerevisiae
  • Cell Cycle Proteins
  • Cyclin-Dependent Kinase Inhibitor Proteins
  • Saccharomyces cerevisiae Proteins
  • Phosphotyrosine
  • Tyrosine
  • Phosphoprotein Phosphatases
  • dual specificity phosphatase 12
  • CDKN3 protein, human
  • Dual-Specificity Phosphatases
  • Protein Tyrosine Phosphatases
  • Protein Tyrosine Phosphatases, Non-Receptor
  • cdc25 Phosphatases
  • myotubularin