Kinetic and X-ray structural studies of three mutant E. coli alkaline phosphatases: Insights into the catalytic mechanism without the nucleophile Ser102

Journal of Molecular Biology

Volumn 277, Issue 3, 1998, Pages 647-662

  Stec, Boguslaw ^a   Hehir, Michael J ^a   Brennan, Christopher ^a   Nolte, Matthias ^b   Kantrowitz, Evan R ^a  

^a Dept Chem Merkert Chem Ctr B ^*  (United States)

^b HARVARD UNIVERSITY   (United States)

Author keywords

Catalytic water; Crystal structure; Phosphoseryl intermediate; Protein phosphatase

Indexed keywords

ALANINE; ALKALINE PHOSPHATASE; CYSTEINE; GLYCINE; PHOSPHATE; SERINE;

AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME KINETICS; ENZYME MECHANISM; ENZYME STRUCTURE; ESCHERICHIA COLI; HYDROLYSIS; MICHAELIS CONSTANT; NONHUMAN; PRIORITY JOURNAL; X RAY CRYSTALLOGRAPHY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; FELIS CATUS; NEGIBACTERIA;

EID: 0032478539     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1635     Document Type: Article

References (41)

1. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:(248):1976;148-254
2. Brünger A.T. X-PLOR, A System for Crystallography and NMR. 1992;Yale University Press, New Haven, CT
3. Butler-Ransohoff J.E., Kendall D.A., Freeman S., Knowles J.R., Kaiser E.T. Stereochemistry of phospho group transfer catalyzed by a mutant alkaline phosphatase. Biochemistry. 27:(13):1988;4777-4780
4. Butler-Ransohoff J.E., Rokita S.E., Kendall D.A., Banzon J.A., Carano K.S., Kaiser E.T., Matlin A.R. Active-site mutagenesis of E. coli alkaline phosphatase replacement of serine-102 with nonnucleophilic amino acids. J. Org. Chem. 57:1992;142-145
5. Carter P., Bedouelle H., Winter G. Improved oligonucleotide site-directed mutagenesis using M13 vectors. Nucl. Acid Res. 13:(12):1985;4431-4443
6. Chaidaroglou A., Brezinski D.J., Middleton S.A., Kantrowitz E.R. Function of arginine-166 in the active site of Escherichia coli alkaline phosphatase. Biochemistry. 27:(22):1988;8338-8343
7. Coleman J.E. Structure and mechanism of alkaline phosphatase. Annu. Rev. Biophys. Biomol. Struct. 21:1992;441-483
8. Dayan J., Wilson I.B. The phosphorylation of tris by alkaline phosphatase. Biochim. Biophys. Acta. 81:1964;620-623
9. Garen A., Levinthal C. A fine-structure genetic and chemical study of the enzyme alkaline phosphatase of E. coli. I. Purification and characterization of alkaline phosphatase. Biochim. Biophys. 38:1960;470-483
10. Ghosh S.S., Bock S.C., Rokita S.E., Kaiser E.T. Modification of the active site of alkaline phosphatase by site-directed mutagenesis. Science. 231:(4734):1986;145-148
11. Goldberg J., Huang H., Kwon Y., Greengard P., Nairn A.C., Kuriyan J. Three dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1. Nature. 376:1995;. 754-753
12. Griffith J.P., Kim J.L., Kim E.E., Sintchak M.D., Thomson J.A., Fitzgibbon M.J., Fleming M.A., Caron P.R., Hsiao K., Navia M.A. X-ray structure of cacineurin inhibited by the immunophilin-imunosupressant FKBP12-FK506 complex. Cell. 82:1995;507-522
13. Guan K., Dixon J.E. Protein tyrosine phosphatase activity of essential virulence determinant of Yersinia. Science. 249:1990;553-555
14. Han R., Coleman J.E. Dependence of the phosphorylation of alkaline phosphatase by phosphate monoesters on the pKa of the leaving group. Biochemistry. 34:(13):1995;4238-4245
15. Hough E., Hansen L.K., Birknes B., Jynge K., Hansen S., Hordvik A., Little C., Dodson E.J., Derewenda Z. High resolution (1.5 Å) crystal structure of phospholipase C from Bacillus cereus. Nature. 338:1989;357-360
16. 31P nuclear magnetic resonance study of alkaline phosphatase the role of inorganic phosphate in limiting the enzyme turnover rate at alkaline pH. Biochemistry. 15:(7):1976;1547-1561
17. 18O] stereochemical course of alkaline phosphatase. Nature. 275:(5680):1978;564-565
18. Jones T.A., Zou J.-Y., Cowan S.W., Kjedgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. Sect. A. 47:1991;110-119
19. Kabsch W. Automatic processing and rotation data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallog. 26:1993;795-800
20. Kim E.E., Wyckoff H.W. Reaction mechanism of alkaline phosphatase based on crystal structures. Two metal ion catalysis. J. Mol. Biol. 218:(2):1991;449-464
21. Koradi R., Billeter M., Wuthrich K. MOLMOL A program for display and analysis of macromolecular structures. J. Mol. Graphics. 14:1996;51-58
22. Ladjimi M.M., Middleton S.A., Kelleher K.S., Kantrowitz E.R. Relationship between domain closure and binding, catalysis, and regulation in Escherichia coli aspartate transcarbamylase. Biochemistry. 27:(1):1988;268-276
23. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:(259):1970;680-685
24. Laskowski R.A., MacArthur M.W., Moss D.S., Thornton J.M. PROCHECK a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;283-291
25. Lipscomb W.N., Sträter N. Recent advances in zinc enzymology. Chem. Rev. 96:1996;2375-2433
26. Luzzati P.V. Traitement statistique des erreurs dans la determination des structures cristallines. Acta Crystallog. 5:1952;802-810
27. Plocke D.J., Vallee B.L. Interaction of alkaline phosphatase of E. coli with metal ions and chelating agents. Biochemistry. 1:1962;1039-1043
28. Sack J.S. Chain a crystallographic modeling protein. J. Mol. Graphics. 6:1988;244-245
29. Schwartz J.H., Lipmann F. Phosphate incorporation into alkaline phosphatase of E. coli. Proc. Natl Acad. Sci. USA. 47:1961;1996-2005
30. Segal I.H. Enzyme Kinetics. 1975;Wiley, New York
31. Sowadski J.M., Handschumacher M.D., Murthy H.M., Kundrot C.E., Wyckoff H.W. Crystallographic observations of the metal ion triple in the active site region of alkaline phosphatase. J. Mol. Biol. 170:(2):1983;575-581
32. Sowadski J.M., Handschumacher M.D., Murthy H.M., Foster B.A., Wyckoff H.W. Refined structure of alkaline phosphatase from Escherichia coli at 2.8 Å resolution. J. Mol. Biol. 186:(2):1985;417-433
33. Steiner T., Saenger W. Role of the C-H...O hydrogen bonds in the coordination of water molecules. Analysis of neutron data. J. Am. Chem. Soc. 115:1993;4540-4547
34. Sträter N., Klabunde T., Tucker P., Withal H., Krebs B. Crystal structure of purple acid phosphatase containing a dinuclear Fe(lll)-Zn(ll) active site. Science. 268:1995;1480-1492
35. Sundell S., Hansen S., Hough E. A proposal for the catalytic mechanism in phospholipase C based on the interaction energy and distance geometry calculations. Protein Eng. 7:1994;571-577
36. Tibbitts T.T., Xu X., Kantrowitz E.R. Kinetics and crystal structure of a mutant Escherichia coli alkaline phosphatase (Asp-369→Asp) a mechanism involving one zinc per active site. Protein Sci. 3:1994;2005-2014
37. Trentham D.R., Gutfreund H. The kinetics of the reaction of nitrophenyl phosphates with alkaline phosphatase from Escherichia coli. Biochem. J. 106:(2):1968;455-460
38. Volbeda A., Lahm A., Sakiyama F., Suck D. Crystal structure of Penicilium citrinum P1 nuclease at 2.8 Å resolution. EMBO J. 10:1991;1607-1618
39. Wilson I.B., Dayan J., Cyr K. Some properties of alkaline phosphatase from Escherichia coli transphosphorylation. J. Biol. Chem. 239:1964;4182-4185
40. Zhang Z.Y., Dixon J.E. Protein tyrosine phosphatases mechanism of catalysis and substrate specificity. Advan. Enzymol. Relat. Areas Mol. Biol. 68:1994;1-68
41. Zoller M.J., Smith M. Oligonucleotide-directed mutagenesis using M12-derived vectors an efficient and general procedure for the production of point mutations in any fragment of DNA. Nucl. Acids Res. 10:(20):1982;6487-6500