Protein-tyrosine phosphatases: Biological function, structural characteristics, and mechanism of catalysis

Critical Reviews in Biochemistry and Molecular Biology

Volumn 33, Issue 1, 1998, Pages 1-52

  Zhang, Zhong Yin ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

Cancer; Diabetes; Infectious diseases; Kinetic isotope effect; Loop dynamics; Rate limiting step; Transition state

Indexed keywords

ARGININE; CYSTEINE; ORGANOPHOSPHATE; PROTEIN TYROSINE PHOSPHATASE; SERINE; THREONINE;

CARCINOGENESIS; CATALYSIS; CONFORMATIONAL TRANSITION; DIABETES MELLITUS; DYNAMICS; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME KINETICS; ENZYME MECHANISM; ENZYME STRUCTURE; HYDROLYSIS; INFECTION; NONHUMAN; PRIORITY JOURNAL; REVIEW; SIGNAL TRANSDUCTION;

AMINO ACID SEQUENCE; BINDING SITES; CATALYSIS; EUKARYOTIC CELLS; HYDROLYSIS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN-TYROSINE-PHOSPHATASE; SEQUENCE ALIGNMENT;

EID: 0031893253     PISSN: 10409238     EISSN: None     Source Type: Journal    
DOI: 10.1080/10409239891204161     Document Type: Review

References (236)

1. Admiraal, S. J. and Herschlag, D. 1995. Mapping the transition state for ATP hydrolysis: implications for enzymatic catalysis. Chem. Biol. 2: 729-739.
2. Ahmad, F., Li, P.-M., Meyerovitch, J., and Goldstein, B. J. 1995. Osmotic loading of neutralizing antibodies demonstrates a role for protein-tyrosine phosphatase 1B in negative regulation of the insulin action pathway. J. Biol. Chem. 270: 20503-20508.
3. Aroca, P., Bottaro, D. P., Ishibashi, T., Aaronson, S. A., and Santos, E. 1995. Human dual specificity phosphatase VHR activates maturation promotion factor and triggers meiotic maturation in Xenopus oocytes. J. Biol. Chem. 270: 14229-14234.
4. Bakalara, N., Seyfang, A., Baltz, T., and Davis, C. 1995a. Trypanosoma brucei and Trypanosoma cruzi: life cycle-regulated protein tyrosine phosphatase activity. Exp. Parasitol. 81: 302-312.
5. Bakalara, N., Seyfang, A., Davis, C., and Baltz, T. 1995b. Characterization of a life-cycle-regulated membrane protein tyrosine phosphatase in Trypanosoma brucei. Eur. J. Biochem. 234: 871-877.
6. Barford, D., Flint, A. J., and Tonks, N. K. 1994. Crystal structure of human protein tyrosine phosphatase 1B. Science 263: 1397-1404.
7. Barford, D., Jia, Z., and Tonks, N. K. 1995. Protein tyrosine phosphatases take off. Nat. Struct. Biol. 2: 1043-1053.
8. Barford, D. 1996. Molecular mechanism of the protein serine/threonine phosphatases. Trends Biochem. Sci. 21: 407-412.
9. Beechem, J. M. and Brand, L. 1985. Time-resolved fluorescence of proteins. Annu. Rev. Biochem. 54: 43-71.
10. Benkovic, S. J. and Schray, K. J. 1978. The mechanism of phosphoryl transfer. In: Transition States of Biochemical Processes, pp. 493-527. Gandour, R. D. and Schowen, R. L., Eds., Plenum Press, New York.
11. Bilwes, A. M. den Hertog, J., Hunter, T., and Noel, J. P. 1996. Structural basis for inhibition of receptor protein-tyrosine phosphatase-alpha by dimerization. Nature 382: 555-559.
12. Bishop, J. M. 1983. Cellular oncogenes and retroviruses. Ann Rev. Biochem. 52: 301-354.
13. cas as a substrate of Yersinia YopH (Yop51), a bacterial protein tyrosine phosphatase that translocate into mammalian cells and targets focal adhesions. EMBO J. 16: 2730-2744.
14. Bliska, J. B., Guan, K. L., Dixon, J. E., and Falkow, S. 1991. Tyrosine phosphate hydrolysis of host proteins by an essential Yersinia virulence determinant. Proc. Natl. Acad. Sci. USA 88: 1187-1191.
15. Bliska, J. B., Clemens, J. C., Dixon, J. E., and Falkow, S. 1992. The Yersinia tyrosine phosphatase: specificity of a bacterial virulence determinant for phosphoproteins in the J774A. 1 macrophage. J. Exp. Med. 176: 1625-1630.
16. Bliska, J. B., Galan, J. E., and Falkow, S. 1993. Signal transduction in the mammalian cell during bacterial attachment and entry. Cell 73: 903-920.
17. Bolin, I. and Wolf-Watz, H. 1988. The plasmid-encoded Yop2b protein of Yersinia pseudotuberculosis is a virulence determinant by calcium and temperature at the level of transcription. Mol. Microbiol. 2: 237-245.
18. 3) to nitrogen nucleophiles from pyridino-N-phosphonates. J. Am. Chem. Soc. 106: 7591-7596.
19. Brautigan, D. L. 1994. Protein phosphatases. Recent Prog. Horm. Res. 49: 197-215.
20. Brown-Shimer, S., Johnson, K. A., Hill, D. E., and Bruskin, A. M. 1992. Effect of protein tyrosine phosphatase 1B expression on transformation by the human neu oncogene. Cancer Res. 52: 478-482.
21. Brubaker, R. R. 1991. Factors promoting acute and chronic diseases caused by Yersiniae. Clin. Microbiol. Rev. 4: 309-324.
22. Bruice, T. C. and Benkovic, S. J. 1966. Phosphate esters. In: Bioorganic Mechanisms. Vol. II. pp. 1-103. Benjamin, W. A., Inc., New York.
23. Bulter, T. 1985. Yersinia Infections. In: Textbook of Medicine. pp. 1600-1603. Wyngaarden, J. B. and Smith, L. H., Eds., Saunders, Philadelphia, PA.
24. Butcher, W. W. and Westheimer, F. H. 1955. The Lanthanum hydroxide gel promoted hydrolysis of phosphate esters. J. Am. Chem. Soc. 77: 2420-2424.
25. Caldwell, S. R., Raushel, F. M., Weiss, P. M., and Cleland, W. W. 1991. Transition-state structures for enzymatic and alkaline phosphotriester hydrolysis. Biochemistry 30: 7444-7450.
26. Cantley, L. C., Auger, K. R., Carpenter, C., Duckworth, B., Graziani, A., Kapeller, R., and Soltoff, S. 1991. Oncogenes and signal transduction. Cell 64: 281-302.
27. Campos, M., Fadden, P., Alms, G., Qian, Z., and Haystead, T. A. J. 1996. Identification of protein phosphatase-1-binding proteins by microcystein-biotin affinity chromatography. J. Biol. Chem. 271: 28478-28484.
28. Cates, C. A., Michael, R. L., Stayrook, K. R., Harvey, K. A., Burke, Y. D., Randall, S. K., Crowell, P. L., and Crowell, D. N. 1996. Prenylation of oncogenic human PTPCAAX protein tyrosine phosphatases. Cancer Lett. 110: 49-55.
29. Charbonneau, H., Tonks, N. K., Walsh, K. A., and Fischer, E. H. 1988. The leukocyte common antigen (CD45): a putative receptor-linked protein tyrosine phosphatase, Proc. Natl. Acad. Sci. USA 85: 7182-7186.
30. Charbonneau, H. Tonks, N. K., Kumar, S., Diltz, C. D., Harrylock, M., Cool, D. E., Krebs, E. G., Fischer, E. H., and Walsh, K. A. 1989. Human placenta protein-tyrosine-phosphatase: amino acid sequence and relationship to a family of receptor-like proteins. Proc. Natl. Acad. Sci. USA 86: 5252-5256.
31. Charbonneau, H. and Tonks, N. K. 1992. 1002 protein phosphatases? Ann. Rev. Cell Biol. 8: 463-493.
32. Chernoff, J., Schievella, A. R., Jost, C. A., Erikson, R. L., and Neel, B. G. 1990. Cloning of a cDNA for a major human protein-tyrosine-phosphatase. Proc. Natl. Acad. Sci. USA 87: 2735-2739.
33. Cho, H., Krishnaraj, R., Kitas, E., Bannwarth, W., Walsh, C. T., and Anderson, K. S. 1992. Isolation and structural elucidation of a novel phosphocysteine intermediate in the LAR protein tyrosine phosphatase enzymatic pathway. J. Am. Chem. Soc. 114: 7296-7298.
34. Cho, H., Krishnaraj, R., Itoh, M., Kitas, E., Bannwarth, W., Saito, H., and Walsh, C. T. 1993. Substrate specificities of catalytic fragments of protein tyrosine phosphatases (HPTP beta, LAR, and CD45) toward phosphotyrosylpeptide substrates and thiophosphotyrosylated peptides as inhibitors. Protein Sci. 2: 977-984.
35. Cho, Y., Solski, P. A., Khosravi-Far, R., Der, C. J., and Kelly, K. 1996. The mitogen-activated protein kinase phosphatases PAC1, MKP-1, and MKP-2 have unique substrate specificities and reduced activity in vivo toward the ERK2 sevenmaker mutation. J. Biol. Chem. 271: 6497-6501.
36. Cirri, P., Chiarugi, P., Camici, G., Manao, G., Raugei, G., Cappugi, G., and Ramponi, G. 1993. The role of Cys12, Cys17 and Arg18 in the catalytic mechanism of low-Mr cytosolic phosphotyrosine protein phosphatase. Eur. J. Biochem. 214: 647-657.
37. Cleland, W. W. and Hengge, A. C. 1995. Mechanisms of phosphoryl and acyl transfer. FASEB J. 9: 1585-1594.
38. Cohn, P. 1989. The structure and regulation of protein phosphatases. Annu. Rev. Biochem. 58: 453-508.
39. Cool, D. E. and Blum, J. J. 1993. Protein tyrosine phosphatase activity in Leishmania donovani. Mol. Cell. Biochem. 127/128: 143-149.
40. Cotton, F. A., Hazen, E. E., Jr., Day, V. W., Larsen, S., Norman, J. G., Jr., Wong, S. T. K., and Johnson, K. H. 1973. Biochemical importance of the binding of phosphate by arginyl groups. Model compounds containing methylguanidinium ion. J. Am. Chem. Soc. 95: 2367-2369.
41. Cover, T. L. and Aber, R. C. 1989. Yersinia Enterocolitica. New Engl. J. Med. 312: 16-24.
42. Cox, J. R. and Ramsay, O. B. 1964. Mechanism of nucleophilic substitution in phosphate esters. Chem. Rev. 64: 317-352.
43. Cullis, P. M. 1987.Acyl group transfer - phosphoryl transfer. In: Enzyme Mechanisms. pp. 179-220. Page, M. L. and Williams, A. Eds., The Royal Society of Chemistry, London.
44. Dechert, U., Adam, M., Harder, K. W., Clark-Lewis, I., and Jirik, F. 1994. Characterization of protein tyrosine phosphatase SH-PTP2. Study of phosphopeptide substrates and possible regulatory role of SH2 domains. J. Biol. Chem. 269: 5602-5611.
45. Dechert, U., Affolter, M., Harder, K. W., Matthews, J., Owen, P., Clark-Lewis, I., Thomas, M. L., Aebersold, R., and Jirik, F. R. 1995. Comparison of the specificity of bacterially expressed cytoplasmic protein-tyrosine phosphatases SHP and SH-PTP2 toward synthetic phosphopeptide substrates. Eur. J. Biochem. 231: 673-681.
46. den Hertog, J., Pals, C. E. G. M., Peppelenbosch, M. P., Tertoolen, L. G. J., de Laat, S. W., and Kruijer, W. 1993. Receptor protein tyrosine phosphatase alpha activates pp60c-src and is involved in neuronal differentiation. EMBO J. 12: 3789-3798.
47. Denu, J. M. and Dixon, J. E. 1995. A catalytic mechanism for the dual-specific phosphatases. Proc. Natl. Acad. Sci. USA 92: 5910-5914.
48. Denu, J. M., Zhou, G., Guo, Y., and Dixon, J. E. 1995. The catalytic role of aspartic acid-92 in a human dual-specific protein-tyrosine-phosphatase. Biochemistry 34: 3396-3403.
49. Denu, J. M., Lohse, D. L., Vijayalakshmi, J., Saper, M. A., and Dixon, J. E. 1996. Visualization of intermediate and transition-state structures in protein-tyrosine phosphatase catalysis. Proc. Natl. Acad. Sci. USA 93: 2493-2498
50. Diamond, R. H., Cressman, D. E., Laz, T. M., Abrams, C. S., and Taub, R. 1994. PRL-1, a unique nuclear protein tyrosine phosphatase, affects cell growth. Mol. Cell. Biol. 14: 3752-3762.
51. Dittmer, D. C., Ramsay, O. B., and Spalding, R. E. 1963. Reactivity of thiophosphates. II. Hydrolysis of S-n-butylphosphorothioate and S-(2-aminoethyl) phosphorothioate. J. Org. Chem. 28: 1273-1278.
52. Dunphy, W. G. and Kumagai, A. 1991. The cdc25 protein contains an intrinsic phosphatase activity. Cell 67: 189-196.
53. Evans, B., Tishmack, P. A., Pokalsky, C., Zhang, M., and Van Etten, R. L. 1996. Site-directed mutagenesis, kinetic, and spectroscopic studies of the P-loop residues in a low-molecular-weight protein tyrosine phosphatase. Biochemistry 35: 13609-13617.
54. Fauman, E. B. and Saper, M. A. 1996. Structure and function of the protein tyrosine phosphatases. Trends Biochem. Sci. 21: 413-417.
55. Fauman, E. B., Yuvaniyama, C., Schubert, H. L., Stuckey, J. A., and Saper, M. A. 1996. The X-ray crystal structures of Yersinia tyrosine phosphatase with bound tungstate and nitrate. J. Biol. Chem. 271: 18780-18788.
56. Filippini, F., Rossi, V., Marin, O., Trovato, M., Costantino, P., Downey, P. M., and Terzi, M. 1996. A plant oncogene as a phosphatase. Nature 379: 499-500.
57. Flint, A. J., Taganis, T., Barford, D., and Tonks, N. K. 1997. Development of "substrate-trapping" mutants to identify physiological substrates of protein tyrosine phosphatases. Proc. Natl. Acad. Sci. USA 94: 1680-1685.
58. Foster, R., Thorner, J., and Martin, G. S. 1989. Nucleotidylation, not phosphorylation, is the major source of the phosphotyrosine detected in enteric bacteria. J. Bacteriol. 171: 272-279.
59. Frey, P. A. 1989. Chiral phosphorothioates: stereochemical analysis of enzymatic substitution at phosphorus. Adv. Enzymol. 62: 119-201.
60. Friedman, J. M., Freeman, S., and Knowles, J. R. 1988. The quest for free metaphosphate in solution: Racemization at phosphorus in the transfer of the phosphate group from aryl phosphate monoesters to tert-butyl alcohol in acetonitrile or in tert-butyl alcohol. J. Am. Chem. Soc. 110: 1268-1275.
61. Galaktionov, K., Lee, A. K., Eckstein, J., Draetta, G., Meckler, J., Loda, M., and Beach, D. 1995. Cdc25 phosphatases as potential human oncogenes. Science 269: 1575-1577.
62. Galaktionov, K., Chen, X., and Beach, D. 1996. Cdc25 cell-cycle phosphatase as a target of c-myc. Nature 382: 511-517.
63. cas as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST. Mol. Cell. Biol. 16: 6408-6418.
64. cdc2. Cell 67: 197-211
65. Gelderloos, J. A. and Anderson, S. M. 1996. Overexpression of protein tyrosine phosphatase 1 (PTP1) alters IL-3 dependent growth and tyrosine phosphorylation. Oncogene 13: 2367-2378.
66. Glc subunit. Biochemistry 36: 7408-7417.
67. Goldfine, A. B., Simonson, D. C., Folli, F., Patti, M.-E., and Kahn, C. R. 1995. Metabolic effects of sodium metavanadate in humans with insulin-dependent and noninsulin-dependent diabetes mellitus in vivo and in vitro studies. J. Clin. Endocrinol. Metab. 80: 3311-3320.
68. 18O-2,4-dinitrophenyl phosphate. Evidence for monomeric metaphosphate. J. Am. Chem. Soc. 99: 2264-2267.
69. Gottlin, E. B., Xu, X., Epstein, D. M., Burke, S. P., Eckstein, J. W., Ballou, D. P., and Dixon, J. E. 1996. Kinetic analysis of the catalytic domain of human cdc25B. J. Biol. Chem. 271: 27445-27449.
70. Gould, K. L. and Nurse, P. 1989. Tyrosine phosphorylation of the fission yeast cdc2+ protein kinase regulates entry into mitosis. Nature 342: 39-45.
71. Gregoret, L. M., Rader, S. D., Fletterick, R. J., and Cohen, F. E. 1991. Hydrogen bonds involving sulfur atoms in proteins. Prot.: Struct., Funct., Genet. 9: 99-107.
72. Guan, K. L. and Dixon, J. E. 1990. Protein tyrosine phosphatase activity of an essential virulence determinant in Yersinia. Science 249: 553-556.
73. Guan, K. L. and Dixon, J. E. 1991. Evidence for protein-tyrosine phosphatase catalysis proceeding via a cysteine-phosphate intermediate. J. Biol. Chem. 266: 17026-17030.
74. Guan, K. L., Broyles, S., and Dixon, J. E. 1991. A Tyr/Ser protein phosphatase encoded by Vaccinia virus. Nature 350: 359-361.
75. Gyuris, J., Golemis, E., Chertkov, H., and Brebt, R. 1993. Cdil, a human G1 and S phase protein phosphatase that associates with Cdk2. Cell 75: 791-803.
76. Hanks, S. K. and Hunter, T. 1995. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 9: 576-596.
77. Hannon, G., Casso, D., and Beach, D. 1994. KAP: a dual specificity phosphatase that interacts with cyclin-dependent kinases. Proc. Natl. Acad. Sci. USA 91: 1731-1735.
78. cas, a substrate associated with v-Src and v-Crk, localizes to focal adhesions and binds to focal adhesion kinase. J. Biol. Chem. 271: 13649-13655.
79. Hasset, A., Blättler, W., and Knowles, J. R. 1982. Pyruvate kinase: is the mechanism of phospho transfer associative or dissociative? Biochemistry 21: 6335-6340.
80. Haynie, D. T. and Ponting, C. P. 1996. The N-terminal domains of tensin and auxilin are phosphatase homologues. Prot. Sci. 5: 2643-2646.
81. Hengge, A. C. and Cleland, W. W. 1990. Direct measurement of transition-state bond cleavage in hydrolysis of phosphate esters of p-nitrophenol. J. Am. Chem. Soc. 112: 7421-7422.
82. Hengge, A. C., Edens, W. A., and Elsing, H. 1994. Transition-state structures for pgosphoryl-transfer reactions of p-nitrophenyl phosphate. J. Am. Chem. Soc. 116: 5045-5049.
83. Hengge, A. C., Sowa, G, Wu, L., and Zhang, Z.-Y. 1995. Nature of the transition state of the protein-tyrosine phosphatase-catalyzed reaction. Biochemistry 34: 13982-13987.
84. Hengge, A. C., Denu, J. M., and Dixon, J. E. 1996. Transition-state structures for the native dualspecific phosphatase VHR and D92N and S131A mutants, contributions to the driving force for catalysis. Biochemistry 35: 7084-7092.
85. Hengge, A. C., Zhao, Y., Wu, L., and Zhang, Z.-Y. 1997. Examination of the transition state of the low molecular mass small tyrosine phosphatase. I. Comparisons with other protein phosphatases. Biochemistry 36: 7928-7936.
86. Herbst, R., Cartoll, P. M., Allard, J. D., Schilling, J., Raabe, T., and Simon, M. A. 1996. Daughter of sevenless is a substrate of the phosphotyrosine phosphatase corkscrew and functions during sevenless signaling. Cell, 85: 899-909.
87. Herr, E. B., Jr. and Koshland, D. E., Jr. 1957. Acid and base catalysis in a non-enzymic transfer reaction: a possible model. Biochim. Biophys. Acta 25: 219-220.
88. Herschlag, D. and Jencks, W. P. 1986. Pyrophosphate formation from acetyl phosphate and orthophosphate anions in concentrated aqueous salt solutions does not provide evidence for a metaphosphate intermediate. J. Am. Chem. Soc. 108: 7938-7946.
89. Herschlag, D. and Jencks, W. P. 1989. Evidence that metaphosphate monoanion is not an intermediate in solvolysis reactions in aqueous solution. J. Am. Chem. Soc. 111: 7579-7586.
90. Heyliger, C. E., Tahiliani, A. G., and McNeill, J. H. 1985. Effect of vanadate on elevated blood glucose and depressed cardiac performance of diabetic rats. Science 227: 1474-1477.
91. Hippen, K. L., Jakes, S., Richards, J., Jena, B. P., Beck, B. L., Tabatabai, L. B., and Ingebritsen, T. S. 1993. Acidic residues are involved in substrate recognition by two soluble protein tyrosine phosphatases, PTP-5 and rrbPTP-1. Biochemistry 32: 12405-12412.
92. Hoffmann, I., Draetta, G., and Karsenti, E. 1994. Activation of the phosphatase activity of human cdc25A by a cdk2-cyclin E dependent phosphorylation at the G1/S transition. EMBO J. 13: 4302-4310.
93. Hubbard, M. J. and Cohen, P. 1993. On target with a new mechanism for the regulation of protein phosphorylation. Trends Biochem. Sci. 18: 172-177.
94. Hunter, T. and Sefton, B. M. 1980. Transforming gene product of Rous sarcoma virus phosphorylates tyrosine. Proc. Natl. Acad. Sci. USA 77: 1311-1315.
95. Hunter, T. 1987. A thousand and one protein kinases. Cell 50: 823-829.
96. Hunter, T. 1991. Protein kinase classification. Method Enzymol. 200: 3-37.
97. Hunter, T. and Pines, J. 1994. Cyclins and cancer II: cyclin D and CDK inhibitors come of age. Cell 79: 573-582.
98. Hunter, T. 1995. Protein kinases and phosphatases: the Yin and Yang of protein phosphorylation and signaling. Cell 80: 225-236.
99. Hunter, T. 1996. Tyrosine phosphorylation: past, present and future. Biochem. Soc. Trans. 24: 307-327.
100. Huyer, G., Liu, S., Kelly, J., Moffat, J., Payette, P., Kennedy, B., Tsaprailis, G., Gresser, M. J. and Ramachandran, C. 1997. Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. J. Biol. Chem. 272: 843-851.
101. Ishibashi, T., Bottara, D. P., Chan, A., Miki, T., and Aaronson, S. A. 1992. Expression cloning of a human dual-specificity phosphatase. Proc. Natl. Acad. Sci. USA 89: 12170-12174.
102. Jayaraman, K. S. 1994. Anti-plague efforts hindered by lack of recent experience. Nature 371: 467.
103. Jencks, W. P. 1962. Mechanism of phosphate ester cleavage. Brookhaven Symp. Biol. 15: 135-153.
104. Jencks, W. P. and Gilchrist, M. 1964. Electrophilic catalysis. The hydrolysis of phosphoramidate. J. Am. Chem. Soc. 86: 1410-1417.
105. Jencks, W. P. and Gilchrist, M. 1965. Reactions of nucleophilic reagents with phosphoramidate. J. Am. Chem. Soc. 87: 3199-3209.
106. Jencks, W. P. and Gilchrist, M. 1968. Nonlinear structure-reactivity correlations. The reactivity of nucleophilic reagents toward esters. J. Am. Chem. Soc. 90: 2622-2637.
107. Jencks, W. P. 1980. When is an intermediate not an intermediate? Enforced mechanisms of general acid-base catalyzed, carbocation, carbanion, and ligand exchange reactions. Acc. Chem. Res. 13: 161-169.
108. nuc for phosphoryl transfer to amines. J. Am. Chem. Soc. 108: 479-483.
109. Jia, Z., Barford, D., Flint, A. J., and Tonks, N. K. 1995. Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B. Science 268: 1754-1758.
110. Johnson, P., Ostergaard, H. L., Wasden, C., and Trowbridge, I. S. 1992. Mutational analysis of CD45, a leukocyte-specific protein tyrosine phosphatase. J. Biol. Chem. 267: 8035-8041.
111. Johnson, L. N., Noble, M. E. M., and Owen, D. 1996. Active and inactive protein kinases: structural basis for regulation. Cell 85: 149-158.
112. Juszczak, L. J., Zhang, Z.-Y., Wu, L., Gottfried, D. S., and Eads, D. D. 1997. Rapid loop dynamics of Yersinia protein tyrosine phosphatases. Biochemistry 36: 2227-2236.
113. Kaniga, K., Uralil, J., Bliska, J. B., and Galan, J. E. 1996. A secreted protein tyrosine phosphatase with modular effector domains in the bacterial pathogen Salmonella typhimurium. Mol. Microbiol. 21: 633-641.
114. Karplus, M. and Petsko, G. A. 1990. Molecular dynamics simulations in biology. Nature 347: 631-639.
115. Kenner, K. A., Anyanwu, E., Olefsky, J. M., and Kusari, J. 1996. Protein-tyrosine phosphatase 1B is a negative regulator of insulin- and insulin-like growth factor-I-stimulated signaling. J. Biol. Chem. 271: 19810-19816.
116. Keyse, S. M. 1995. An emerging family of dual specificity MAP kinase phosphatases. Biochim. Biophys. Acta 1265: 152-160.
117. Khan, S. A. and Kirby, A. J. 1970. The reactivity of phosphate esters. Multiple structure-reactivity correlations for the reactions of triesters with nucleophiles. J. Chem. Soc. B: 1172-1182.
118. Kirby, A. J. and Jencks, W. P. 1965. The reactivity of nucleophilic reagents toward the p-nitrophenyl phosphate dianion. J. Am. Chem. Soc. 87: 3209-3216.
119. Kirby, A. J. and Varvoglis, A. G. 1967. The reactivity of phosphate esters. Monoester hydrolysis. J. Am. Chem. Soc. 89: 415-423.
120. Kirby, A. J. and Warren, S. G. 1967. In: The Organic Chemistry of Phosphorus. pp. 274-364. Elsevier Science.
121. Klingmuller, U., Lorenz, U., Cantley, L. C., Neel, B. G., and Lodish, H. F. 1995. Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals. Cell 80: 729-738.
122. Knowles, J. R. 1980. Enzyme-catalyzed phosphoryl transfer reactions. Annu. Rev. Biochem. 49: 877-919.
123. Kole, H. K., Garant, M. J., Kole, S., and Bernier, M. 1996. A peptide-based protein-tyrosine phosphatase inhibitor specifically enhances insulin receptor function in intact cells. J. Biol. Chem. 271: 14302-14307.
124. Kulas, D. T., Zhang, W.-R., Goldstein, B. J., Furlanetto, R. W., and Mooney, R. A. 1995. Insulin receptor signaling is augmented by antisense inhibition of the protein tyrosine phosphatase LAR. J. Biol. Chem. 270: 2435-2438.
125. LaForgia, S., Morse, B., Levy, J., Barnea, G., Ganniz-Weston, L. A., Harris, C. C., Drabkin, H., Patterson, D., Croce, C. M., Schlessinger, J., and Huebner, K. 1991. Receptor protein-tyrosine phosphatase y is a candidate tumor suppressor gene at human chromosome region 3p21. Proc. Natl. Acad. Sci. USA 88: 5036-5040.
126. Lammers, R., Moller, N. P., and Ullrich, A. 1997. The transmembrane protein tyrosine phosphatase alpha dephosphorylates the insulin receptor in intact cells. FEBS Lett. 404: 37-40.
127. Lechleider, R. J., Sugimoto, S., Bennett, A. M., Kashishian, A. S., Cooper, J. A., Shoelson, S. E., Walsh, C. T., and Neel, B. G. 1993. Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor. J. Biol. Chem. 268: 21478-21481.
128. Levinson, A. D., Oppermann, H., Varmus, H. E., and Bishop, J. M. 1980. The purified product of the transforming gene of avian sarcoma virus phosphorylates tyrosine. J. Biol. Chem. 255: 11973-11980.
129. Li, J., Yen, C., Liaw, D., Podsypanina, K., Bose, S., Wang, S. I., Puc, J., Miliaresis, C., Rodgers, L., McCombie, R., Bigner, S. H., Giovanella, B. C., Ittmann, M., Tycko, B., Hibshoosh, H., Wigler, M. H., and Parsons, R. 1997. PTEN, a putative protein tyrosine phosphatase gene mutated in human brain, breast, and prostate cancer. Science 275: 1943-1947.
130. Liaw, D., Marsh, D. J., Li, J., Dahia, P. L. M., Wang, S. I., Zheng, Z., Bose, S., Call, K. M., Tsou, H. C., Peacocke, M., Eng, C., and Parsons, R. 1997. Germline mutations of the PTEN gene in Cowdem disease, an inherited breast and thyroid cancer syndrome. Nature Genet. 16: 64-67.
131. Lightcap, E. S. and Frey, P. A. 1992. J. Am. Chem. Soc. 114: 9750-9755.
132. Lim, K. L., Lai, D. S., Kalousek, M. B., Wang, Y., and Pallen, C. J. 1997. Kinetic analysis of two closely related receptor-like protein-tyrosine phosphatases, PTPα and PTPε. Eur. J. Biochem. 245: 693-700.
133. Liu, K., Lemon, B., and Traktman, P. 1995. The dual-specificity phosphatase encoded by vaccinia cirus, VH1, is essential for viral transcription in vivo and in vitro. J. Virol. 69: 7823-7834.
134. cas. J. Biol. Chem. 271: 31290-31295.
135. Logan, T. M., Zhou, M. M., Nettesheim, D. G., Meadows, R. P., Van Etten, R. L., and Fesik, S. W. 1994. Solution structure of a low-molecular-weight protein tyrosine phosphatase. Biochemistry 33: 11087-11096.
136. Lohse, D. L., Denu, J. M., Santoro, N., and Dixon, J. E. 1997. Roles of aspartic acid-181 and serine-222 in intermediate formation and hydrolysis of the mammalian protein-tyrosine-phosphatase PTP1. Biochemistry 36: 4568-4575.
137. iα2. Nature 379: 840-844.
138. Michielis, T. and Cornelis, G. 1988. Nucleotide sequence and transcription analysis of Yop51 from Yersinia enterocolitica. Microbial. Pathogen 5: 449-459.
139. Mildvan, A. S. and Fry, D. C. 1987. NMR studies of the mechanism of enzyme action. Adv. Enzymol. 59: 241-313.
140. Millar, J. B. A. and Russell, P. 1992. The cdc25 M-phase inducer: an unconventional protein phosphatase. Cell 68: 407-410.
141. Milstien, S. and Fife, T. H. 1967. The hydrolysis of S-aryl phosphorothioates. J. Am. Chem. Soc. 89: 5820-5826.
142. Moller, N. P. H., Moller, K. B., Lammers, R., Kharitonenkov, A., Hoppe, E., Wiberg, F. C., Sures, I., and Ullrich, A. 1995. Selective down-regulation of the insulin receptor signal by protein-tyrosine phosphatases alpha and epsilon. J. Biol. Chem. 270: 23126-23131.
143. Mondesert, O., Moreno, S., and Russell, P. 1994. Low molecular weight protein-tyrosine phosphatases are highly conserved between fission yeast and man. J. Biol. Chem. 269: 27996-27999.
144. Mossman, K., Ostergaard, H., Upton, C., and McFadden, G. 1995. Myxoma virus and Shope fibroma virus encode dual-specificity tyrosine/ serine phosphatase which are essential for virus viability. Virology 206: 572-582.
145. Mumby, M. C. and Walter, G. 1993. Protein serine/ threonine phosphatases: structure, regulation, and functions in cell growth. Physiol. Rev. 73: 673-699.
146. Myers, M. G., Jr. and White, M. F. 1996. Insulin signal transduction and the IRS proteins. Annu. Rev. Pharmacol. Toxicol. 36: 615-58.
147. Neel, B. G. and Tonks, N. K. 1997. Protein tyrosine phosphatases in signal transduction. Curr. Opin. Cell Biol. 9: 193-204
148. Noguchi, T., Matozaki, T., Horita, K., Fujioka, Y., and Kasuga, M. 1994. Role of SH-PTP2, a protein-tyrosine phosphatase with src homology 2 domains, in insulin-stimulated Ras activation. Mol. Cell. Biol. 14: 6674-6682.
149. O'Leary, M. H. and Marlier, J. F. 1979. Heavy-atom isotope effects on the alkaline hydrolysis and hydrazinolysis of methyl benzoate. J. Am. Chem. Soc. 101: 3300-3306.
150. Ostanin, K., Pokalsky, C., Wang, S., and Van Etten, R. L. 1995. Cloning and characterization of a Saccharomyces cerevisiae gene encoding the low molecular weight protein-tyrosine phosphatase. J. Biol. Chem. 270: 18491-18499.
151. Palmer, A. G. 1993. Dynamic properties of proteins from NMR spectroscopy. Curr. Opin. Biotechnol. 4: 385-391.
152. Mtl. J. Biol. Chem. 266: 6690-6692.
153. Pei, D., Lorenz, U., Klingmuller, U., Neel, B. G., and Walsh, C. T. 1994. Intramolecular regulation of protein tyrosine phosphatase SH-PTP1: a new function for Src homology 2 domains. Biochemistry 33: 15483-15493.
154. Perkins, L. A., Larsen, I., and Perrimon, N. 1992. Corkscrew encodes a putative protein tyrosine phosphatase that functions to transduce the terminal signal from the receptor tyrosine kinase torso. Cell 70: 225-236.
155. Pingel, J. T. and Thomas, M. L. 1989. Evidence that the leukocyte-common antigen is required for antigen-induced T lymphocyte proliferation. Cell 58: 1055-1065.
156. Pluskey, S., Wandless, T. J., Walsh, C. T., and Shoelson, S. E. 1995. Potent stimulation of SH-PTP2 phosphatase activity by simultaneous occupancy of both SH2 domains. J. Biol. Chem. 270: 2897-2900.
157. 160 by the cyclin-dependent kinase-interacting phosphatase KAP in the absence of cyclin. Science 270: 90-93.
158. Ramponi, G. 1994. The low-Mr cytosolic phosphotyrosine protein phosphatases. Adv. Prot. Phosphatases 8: 1-25.
159. Roach, P. J. 1991. Multisite and hierarchal protein phosphorylation. J. Biol. Chem. 266: 14139-14142.
160. Ruzzene, M., Donella-Deana, A., Marin, O., Perich, J. W., Ruzza, P., Borin, G., Calderan, A., and Pinna, L. A. 1993. Specificity of T-cell protein tyrosine phosphatase toward phosphorylated synthetic peptides. Eur. J. Biochem. 211: 289-295.
161. Sabato, G. and Jencks, W. P. 1961. Mechanism and catalysis of reactions of acyl phosphates. II. Hydrolysis. J. Am. Chem. Soc. 83: 4400-4405.
162. Sakai, R., Iwamatsu, A., Hirano, N., Ogawa, S., Tanaka, T., Mano, H., Yazaki, Y., and Hirai, H. 1994. A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner. EMBO J. 13: 3748-3756.
163. Sato, T., Irie, S., Kitada, S., and Reed, J. C. 1995. FAP-1: a protein tyrosine phosphatase that associates with Fas. Science 268: 411-415.
164. Schubert, H. L., Fauman, E. B., Stuckey, J. A., Dixon, J. E., and Saper, M. A. 1995. A ligand-induced conformational change in the Yersinia protein tyrosine phosphatase. Protein Sci. 4: 1904-1913.
165. Sebastian, B., Kakizuka, A., and Hunter T. 1993. Cdc25M2 activation of cyclin-dependent kinases by dephosphorylation of threonine-14 and tyrosine-15. Proc. Natl. Acad. Sci. USA 90: 3521-3524.
166. Sefton, B. M., Hunter, T., Ball, E. H., and Singer, S. J. 1981. Vinculin: a cytoskeletal target of the transforming protein of Rous sarcoma virus. Cell 24: 165-174.
167. Sheng, Z. and Charbonneau, H. 1993. The baculovirus Autographa californica encodes a protein tyrosine phosphatase. J. Biol. Chem. 268: 4728-4733.
168. Shenolikar, S. 1994. Protein serine/threonine phosphatases - new avenues for cell regulation. Annu. Rev. Cell Biol. 10: 55-86.
169. Shultz, L. D., Schweitzer, P. A., Rajan, T. V., Yi, T., Ihle, J. N., Matthews, R. J., Thomas, M. L., and Beier, D. R. 1993. Mutations at the murine motheaten locus are within the hematopoietic cell protein tyrosine phosphatase (Hcph) gene. Cell 73: 1445-1454.
170. Skoog, M. T. and Jencks, W. P. 1984. Reactions of pyridines and primary amines with N-phosphorylated pyridines. J. Am. Chem. Soc. 106: 7597-7606.
171. Sparks, J. W. and Brautigan, D. L. 1985. Specificity of protein phosphotyrosine phosphatases. Comparison with mammalian alkaline phosphatase using polypeptide substrates. J. Biol. Chem. 260: 2042-2045.
172. Spitkovsky, D., Jansen-Durr, P., Karsenti, E., and Hoffmann, I. 1996. S-phase induction by adenovirus E1A requires activation of cdc25A tyrosine phosphatase. Oncogene 12: 2549-2554.
173. Sredy, J., Sawicki, D. R., Flam, B. R., and Sullivan, D. 1995. Insulin resistence is associated with abnormal dephosphorylation of a synthetic phosphopeptide corresponding to the major autophosphorylation sites of the insulin receptor. Metabolism: Clin. Exp. 44: 1074-1081.
174. Steck, P. A., Pershouse, M. A., Jasser, S. A., Yung, W. K. A., Lin, H., Ligon, A. H., Langford, L. A., Baumgard, M. L., Hattier, T., Davis, T., Frye, C., Hu, R., Swedlund, B., Teng, D. H. F., and Tavtigian, S. V. 1997. Identification of a candidate tumour suppressor gene, MMACI, at chromosome 10q23 that is mutated in multiple advanced cancers. Nature Genet. 15: 356-362.
175. Streuli, M., Krueger, N. X., Tsai, A. Y., and Saito, H. 1989. A family of receptor-linked protein tyrosine phosphatases in humans and Drosophila. Proc. Natl. Acad. Sci. U S A. 86: 8698-8702.
176. Streuli, M., Krueger, N. X., Thai, T., Tang, M., and Saito, H. 1990. Distinct functional roles of the two intracellular phosphatase like domains of the receptor-linked protein tyrosine phosphatases LCA and LAR. EMBO J. 9: 2399-2407.
177. Streuli, M. 1996. Protein tyrosine phosphatases in signaling. Curr. Opin. Cell Biol. 8: 182-188.
178. Stuckey, J. A., Schubert, H. L., Fauman, E., Zhang, Z.-Y., Dixon, J. E., and Saper, M. A. 1994. Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 Å and the complex with tungstate. Nature 370: 571-575.
179. Su, X. D., Taddei, N., Stefani, M., Ramponi, G., and Nordlund, P. 1994. The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase. Nature 370: 575-578.
180. Sun, H., Charles, C. H., Lau, L. F., and Tonks, N. K. 1993. MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo. Cell 75: 487-493.
181. Sun, H. and Tonks, N. K. 1994. The coordinated action of protein tyrosine phosphatases and kinases in cell signaling. Trends Biochem. Sci. 19: 480-485.
182. Swarup, G., Cohen, S., and Garbers, D. L. 1982. Inhibition of membrane phosphotyrosyl-protein phosphatase activity by vanadate. Biochem. Biophys. Res. Commun. 107: 1104-1109.
183. Tabiti, K., Smith, D. R., Goh, H.-S., and Pallen, C. J. 1995. Increased mRNA expression of the receptor-like protein tyrosine phosphatase a in late stage colon carcinomas. Cancer Lett. 93: 239-248.
184. Taddei, N., Chiarugi, P., Cirri, P., Fiaschi, T., Stefani, M., Camici, G., Raugei, G., and Ramponi, G. 1994. Aspartic-129 is an essential residue in the catalytic mechanism of the low M(r) phosphotyrosine protein phosphatase. FEBS Lett. 350: 328-332.
185. Takagi, T., Moore, C. R., Diehn, F., and Buratowski, S. 1997. An RNA 5′-triphosphoatase related to the protein tyrosine phosphatases. Cell 89: 867-873.
186. Taylor, S. S., Zheng, J., Sowadski, J. M., Knighton, D. R., Gibbs, C. S., and Zoller, M. J. 1993. A template for the protein kinase family. Trends Biochem. Sci. 18: 84-89.
187. Taylor, S. S., Radzio-Andzelm, E., and Hunter, T. 1995. How do protein kinases discriminate between serine/threonine and tyrosine? structural insights from the insulin receptor protein-tyrosine kinase. FASEB J. 9: 1255-1266.
188. Thatcher, G. R. J. and Kluger, R. 1989. Mechanism and catalysis of nucleophilic substitution in phosphate esters. Adv. Phys. Org. Chem. 25: 99-265.
189. Tonks, N. K., Diltz, C. D., and Fischer, E. H. 1988a. Purification of the major protein-tyrosine phosphatases of human placenta. J. Biol. Chem. 263: 6722-6730.
190. Tonks, N. K., Diltz, C. D., and Fischer, E. H. 1988b. Characterization of the major protein-tyrosine phosphatases of human placenta. J. Biol. Chem. 263: 6731-6737.
191. Tonks, N. K. and Neel, B. G. 1996. From form to function: signaling by protein tyrosine phosphatases. Cell 87: 365-368.
192. Ushiro, H. and Cohen, S. 1980. Identification of phosphotyrosine as a product of epidermal growth factor-activated protein kinase in A-431 cell membranes. J. Biol. Chem. 255: 8363-8365.
193. cellobiose, reveals similarity to eukaryotic protein tyrosine phosphatases. Structure 5: 217-225.
194. Walton, K. M. and Dixon, J. E. 1993. Protein tyrosine phosphatases. Annu. Rev. Biochem. 62: 101-120.
195. max stimulatory effects of glycerol and of a phosphotyrosyl peptide ligand. Biochemistry 36: 2993-2999.
196. Wang, Y. and Pallen, C. J. 1991. The receptor-like protein tyrosine phosphatase HPTP alpha has two active catalytic domains with distinct substrate specificities. EMBO J. 10: 3231-3237.
197. Wary, K. K., Lou, Z., Buchberg, A. M., Siracusa, L. D., Druck, T., LaForgia, S., and Huebner, K. 1993. A homozygous deletion within the carbonic anhydrase-like domain of the Ptprγ gene in murine L-Cells. Cancer Res. 53: 1498-1502.
198. 18O isotope effects on the hydrolysis of glucose 6-phosphate. J. Am. Chem. Soc. 108: 2761-2762.
199. Westheimer, F. H. 1981. Monomeric metaphosphates. Chem. Rev. 81: 313-326.
200. Westheimer, F. H. 1987. Why nature chose phosphates. Science 235: 1173-1178.
201. White, M. F. and Kahn, C. R. 1994. The insulin signaling system. J. Biol. Chem. 269: 1-4.
202. Williams, J. C. and McDermott, A. E. 1995. Dynamics of the flexible loop of triosephosphate isomerase: the loop motion is not ligand gated. Biochemistry 34: 8309-8319.
203. Wo, Y.-Y. P., Zhou, M.-M., Stevis, P., Davis, J. P., Zhang, Z.-Y., and Van Etten, R. L. 1992. Cloning, expression, and catalytic mechanism of a low-molecular-weight phosphotyrosyl protein phosphatase from bovine heart. Biochemistry 31: 1712-1721.
204. Woodford-Thomas, T. A., Rhodes, J. D., and Dixon, J. E. 1992. Expression of a protein tyrosine phosphatase in normal and v-src-transformed mouse 3T3 fibroblasts. J. Cell Biol. 117: 401-414.
205. Wu, L. and Zhang, Z.-Y. 1996. Probing the function of Asp128 in the low-molecular-weight protein-tyrosine phosphatase catalyzed reaction. A pre-steady-state and steady-state kinetic investigation. Biochemistry 35: 5426-5434.
206. Wu, L., Buist, A., den Hertog, J., and Zhang, Z.-Y. 1997. Comparative kinetic analysis and substrate specificity of the tandem catalytic domains of the receptor-like protein-tyrosine phosphatase α. J. Biol. Chem. 272: 6994-7002.
207. Yuvaniyama, J., Denu, J. M., Dixon, J. E., and Saper, M. A. 1996. Crystal structure of the dual specificity protein phosphatase VHR. Science 272: 1328-1331.
208. Zhang, M., Van Etten, R. L., and Stauffacher, C. V. 1994. Crystal structure of bovine heart phosphotyrosyl phosphatase at 2.2-Å resolution. Biochemistry 33: 11097-11105.
209. Zhang, M., Stauffacher, C. V., and Van Etten, R. L. 1995. The three dimensional structure, chemical mechanism and function of the low-molecular-weight protein tyrosine phosphatases. Adv. Prot. Phosphatases 9: 1-23.
210. Zhang, M., Zhou, M., Van Etten, R. L., and Stauffacher, C. V. 1997. Crystal structure of bovine low-molecular-weight phosphotyrosyl phosphatase complexed with the transition state analog vanadate. Biochemistry 36: 15-23.
211. Zhang, W.-R., Li, P.-M., Oswald, M. A., and Goldstein, B. J. 1996. Modulation of insulin signaling transduction by eutopic over-expression of the receptor type protein-tyrosine phosphatase LAR. Mole. Endocrinol. 10: 575-584.
212. Zhang, Z., Harms, E., and Van Etten, R. L. 1994. Asp129 of low-molecular-weight protein tyrosine phosphatase is involved in leaving group protonation. J. Biol. Chem. 269: 25947-25950.
213. Zhang, Z.-Y. 1990. Mechanistic and Kinetic Studies of the Bovine Heart Low-Molecular-Weight Phosphotyrosyl Protein Phosphatase. Ph.D. Thesis, Purdue University, West Lafayette, IN.
214. Zhang, Z.-Y. and Van Etten, R. L. 1990. Purification and characterization of a low molecular weight acid phosphatase - a major phosphotyrosyl-protein phosphatase from bovine heart. Arch. Biochem. Biophys., 282: 39-49.
215. Zhang, Z.-Y. and Van Etten, R. L. 1991a. Presteady-state and steady-state kinetic analysis of the low molecular weight phosphotyrosyl protein phosphatase from bovine heart. J. Biol. Chem., 266: 1516-1525.
216. Zhang, Z.-Y. and Van Etten, R. L. 1991b. Leaving group dependence and proton inventory studies of the phosphorylation of a cytoplasmic phosphotyrosyl protein phosphatase from bovine heart. Biochemistry, 30: 8954-8959.
217. Zhang, Z.-Y., Clemens, J. C., Schubert, H. L., Stuckey, J. A., Fischer, M. W. F., Hume, D. M., Saper, M. A., and Dixon, J. E. 1992. Expression, purification, and physicochemical characterization of a recombinant Yersinia protein tyrosine phosphatase. J. Biol. Chem., 267: 23759-23766.
218. a of the active site cysteine and the function of the conserved histidine 402. Biochemistry 32: 9340-9345.
219. Zhang, Z.-Y., Thieme-Sefler, A. M., Maclean, D., Roeske, R., and Dixon, J. E. 1993a. A continuous spectrophotometric and fluorimetric assay for protein tyrosine phosphatase using phosphotyrosine containing peptides. Anal. Biochem. 211: 7-15.
220. Zhang, Z.-Y., Maclean, D., Thieme-Sefler, A. M., McNamara, D., Dobrusin, E. M., Sawyer, T. K., and Dixon, J. E. 1993b. Substrate specificity of the protein tyrosine phosphatases. Proc. Natl. Acad. Sci. USA 90: 4446-4450.
221. Zhang, Z.-Y., Wang, Y., and Dixon, J. E. 1994a. Dissecting the catalytic mechanism of protein tyrosine phosphatases. Proc. Natl. Acad. Sci. USA 91: 1624-1627.
222. 5Arg catalytic motif in phosphoester hydrolysis. Biochemistry 33: 15266-15270.
223. Zhang, Z.-Y., Malachowski, W. P., Van Etten, R. L., and Dixon, J. E. 1994c. The nature of the rate-determining steps of the Yersinia protein tyrosine phosphatase-catalyzed reactions. J. Biol. Chem. 269: 8140-8145.
224. Zhang, Z.-Y., Maclean, D., McNamara, D. J., Sawyer, T. K., and Dixon, J. E. 1994d. Protein tyrosine phosphatase substrate specificity: the minimum size of the peptide and the positioning of the phosphotyrosine. Biochemistry 33: 2285-2290.
225. Zhang, Z.-Y. 1995. Kinetic and mechanistic characterization of a mammalian protein tyrosine phosphatase, PTP1. J. Biol. Chem. 270: 11199-11204.
226. Zhang, Z.-Y., Zhou, G., Denu, J. M., Wu, L., Tang, X., Mondesert, O., Russell, P., Butch, E., and Guan, K.-L. 1995a. Purification and characterization of the low molecular weight protein tyrosine phosphatase, Stp1, from the fission yeast S. pombe. Biochemistry, 34: 10560-10568.
227. Zhang, Z.-Y., Palfey, B. A., Wu, L., and Zhao, Y. 1995b Catalytic function of the conserved hydroxyl group in the protein-tyrosine phosphatase signature motif. Biochemistry 34: 16389-16396.
228. Zhang, Z.-Y., Wu, L., and Chen, L. 1995c. Transition state and rate-limiting step of the reaction catalyzed by the human dual specificity phosphatase, VHR. Biochemistry 34: 16088-16096.
229. Zhang, Z.-Y. 1997. Structure, mechanism and specificity of protein-tyrosine phosphatases. Curr. Top. Cell. Reg. 35: 21-68.
230. Zhang, Z.-Y. and Wu, L. 1997. The single sulfur to oxygen substitution in the active site nucleophile of the Yersinia protein-tyrosine phosphatase leads to substantial structural and functional perturbations. Biochemistry 36: 1362-1369.
231. 13C NMR relaxation studies of backbone and side chain motion of the catalytic tyrosine residue in free and steroid-bound delta 5-3-ketosteroid isomerase. Biochemistry 35: 1525-1532.
232. Zhao, Y. and Zhang, Z.-Y. 1996. Reactivity of alcohols toward the phosphoenzyme intermediate in the protein-tyrosine phosphatase-catalyzed reaction: probing the transition state of the dephosphorylation step. Biochemistry 35: 11797-11804.
233. Zhao, Z., Bouchard, P., Diltz, C. D., Shen, S. H., and Fischer, E. H. 1993. Purification and characterization of a protein tyrosine phosphatase containing SH2 domains. J. Biol. Chem. 268: 2816-2820.
234. c-src by overexpression of a protein tyrosine phosphatase. Nature 359: 336-339.
235. Zhou, G., Denu, J. M., Wu, L., and Dixon, J. E. 1994. The catalytic role of Cys124 in the dual specificity phosphatase VHR. J. Biol. Chem. 269: 28084-28090.
236. Zhou, M. M., Logan, T. M., Theriault, Y., Van Etten, R. L., and Fesik, S. W. 1994. Backbone 1H, 13C, and 15N assignments and secondary structure of bovine low-molecular-weight phosphotyrosyl protein phosphatase. Biochemistry 33: 5221-5229.