Structure and function of the protein tyrosine phosphatases

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 speci...

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Veröffentlicht in:	Trends in biochemical sciences (Amsterdam. Regular ed.) 1996-11, Vol.21 (11), p.413-417
Hauptverfasser:	Fauman, E B, Saper, M A
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Binding Sites cdc25 Phosphatases 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
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Beschreibung
Zusammenfassung:	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.
ISSN:	0968-0004
DOI:	10.1016/S0968-0004(96)10059-1