Mechanistic studies on protein tyrosine phosphatases.

摘要: The human genome encodes approximately 100 phosphatases that belong to the protein tyrosine phosphatase (PTP) superfamily. hallmark for this superfamily is active site sequence C(X)5R, also known as PTP signature motif. PTPs are key regulatory components in signal transduction pathways and importance of control cellular signaling well established. Based on structure substrate specificity, divided into four distinct subfamilies: (1) pTyr-specific PTPs, (2) dual specificity phosphatases, (3) Cdc25 (4) LMW PTPs. have similar core structures made a central parallel beta-sheet with flanking a-helices containing beta-loop-alpha-loop encompasses Site-directed mutagenesis conserved amino acids Yersinia several other combined detailed kinetic mechanistic analyses revealed common chemical mechanism phosphate hydrolysis despite differences specificity. This article reviews our current knowledge features important catalysis, nature enzymatic transition state, roles essential residues stabilization. Future studies will focus use physiological substrates determine molecular basis recognition regulation, which understanding specific functional role signaling.