Publication | Closed Access
Protein Tyrosine Phosphatase Activity of an Essential Virulence Determinant in <i>Yersinia</i>
552
Citations
17
References
1990
Year
Microbial PathogensYersinia PhosphataseBacteriophageMolecular BiologyBacterial PathogensEssential Virulence DeterminantHost-pathogen InteractionsProtein Tyrosine PhosphataseBiochemistryVirulence FactorProkaryotic VirusMolecular MicrobiologyClinical MicrobiologyProtein PhosphorylationNatural SciencesPathogenesisSynthetic BiologyMicrobiologyMedicine
Yersinia is the genus of bacteria that is the causative agent in plague or the black death, and on several occasions this organism has killed a significant portion of the world's population. An essential virulence determinant of Yersinia was shown to be a protein tyrosine phosphatase. The recombinant 50-kilodalton Yersinia phosphatase had a specificity for removal of phosphate from Tyr-containing as opposed to Ser/Thr-containing phosphopeptides and proteins. Site-directed mutagenesis was used to show that the Yersinia phosphatase possesses an essential Cys residue required for catalysis. Amino acids surrounding an essential Cys residue are highly conserved, as are other amino acids in the Yersinia and mammalian protein tyrosine phosphatases, suggesting that they use a common catalytic mechanism.
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1988 | 11.3K | |
1985 | 3.2K | |
1989 | 1.2K | |
1988 | 568 | |
1976 | 502 | |
1989 | 447 | |
1988 | 433 | |
1988 | 415 | |
1989 | 326 | |
cDNA isolated from a human T-cell library encodes a member of the protein-tyrosine-phosphatase family. D E Cool, N. K. Tonks, Harry Charbonneau, Proceedings of the National Academy of Sciences Molecular BiologyHuman T-cell LibraryHuman Placenta Protein-tyrosine-phosphataseT7 Rna PolymeraseProtein Synthesis | 1989 | 317 |
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