Structural and mechanistic studies of chloride induced activation of human pancreatic α-amylase

Protein Science

Volumn 14, Issue 3, 2005, Pages 743-755

  Maurus, Robert ^a   Begum, Anjuman ^a   Kuo, Hsin Hen ^a   Racaza, Andrew ^a   Numao, Shin ^a   Andersen, Carsten ^b   Tams, Jeppe W ^b   Vind, Jesper ^b   Overall, Christopher M ^a   Withers, Stephen G ^a   Brayer, Gary D ^a  

^a UNIVERSITY OF BRITISH COLUMBIA   (Canada)

^b NOVOZYMES A S   (Denmark)

Author keywords

Acarbose; Active site; Amylase; Catalytic activity; Chloride activation; Inhibition; Kinetics; Protein folding; X ray crystallography

Indexed keywords

AMYLASE; CHLORIDE;

ALLOSTERISM; ARTICLE; CATALYSIS; COMPARATIVE STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME BINDING; ENZYME KINETICS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STRUCTURE; STRUCTURE ACTIVITY RELATION; X RAY CRYSTALLOGRAPHY;

ACARBOSE; ALPHA-AMYLASE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ASPERGILLUS ORYZAE; CHLORIDES; ENZYME ACTIVATION; HUMANS; HYDROGEN BONDING; KINETICS; MUTAGENESIS; PANCREAS; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT;

EID: 20044380522     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.041079305     Document Type: Article

References (38)

1. Aghajari, N., Feller, G., Gerday, C., and Haser, R. 1998. Crystal structures of the psychrophilic α-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor. Protein Sci. 7: 564-572.
2. _. 2002. Structural basis of α-amylase activation by chloride. Protein Sci. 11: 1435-1441.
3. Boel, E.L., Brady, A.M., Brzozowski, Z., Derewenda, G.G., Dodson, V.J., Jensen, S.B., Petersen, H., Swift, L., Thim, L., and Woldike, H.F. 1990. Calcium binding in α-amylases: An X-ray diffraction study at 2.1-Å resolution of two enzymes from Aspergillus. Biochemistry 29: 6244-6249.
4. Braun, C., Brayer, G.D., and Withers, S.G. 1995. Mechanism-based inhibition of yeast α-glucosidase and human pancreatic α-amylase by a new class of inhibitors: 2-Deoxy-2,2-difluoro α-glycosides. J. Biol. Chem. 270: 26778-26781.
5. Brayer, G.D., Luo, Y.G., and Withers, S.G. 1995. The structure of human pancreatic α-amylase at 1.8 Å resolution and comparisons with related enzymes. Protein Sci. 4: 1730-1742.
6. Brayer, G.D., Sidhu, G., Maurus, R., Rydberg, E., Braun, C., Wang, Y., Nguyen, N., Overall, C., and Withers, S. 2000. Subsite mapping of the human pancreatic α-amylase active site through structural, kinetic and mutagenesis techniques. Biochemistry 39: 4778-4791.
7. Brunger, A.T. 1996. X-PLOR version 3.8. Yale University Press, New Haven, CT.
8. Brunger, A.T., Adams, P.D., Clore, G.M., DeLano, W.L., Gros, P., Grosse-Kunstleve, R.W., Jiang, J.-S., Kuszewski, J., Nilges, M., Pannu, N.S., et al. 1998. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D 54: 905-921.
9. Brzozowski, A.M. and Davies, G.J. 1997. Structure of the Aspergillus oryzae α-amylase complexed with the inhibitor acarbose at 2.0 Å resolution. Biochemistry 36: 10837-10845.
10. Brzozowski, A.M., Lawson, D.M., Turkenburg, J.P., Bisgaard-Frantzen, H., Svendsen, A., Borchert, T.V., Dauter, Z., Wilson, K.S., and Davies, G.J. 2000. Structural analysis of a chimeric bacterial α-amylase. High resolution analysis of native and ligand complexes. Biochemistry 39: 9099-9107.
11. Christensen, T., Woeldike, H., Boel, E., Mortensen, S.B., Hjortshoej, K., Thim, L., and Hansen, M.T. 1988. High level expression of recombinant genes in Aspergillus oryzae. Bio/Technology 6: 1419-1422.
12. D'Amico, S., Gerday, C., and Feller, G. 2000. Structural similarities and evolutionary relationships in chloride-dependent α-amylases. Gene 253: 95-105.
13. Evans, S.V. 1993. SETOR: Hardware lighted three-dimensional solid model representations of macromolecules. J. Mol. Graph. 11: 134-138.
14. Feller, G., Bussy, O., Houssier, C., and C. Gerday, G. 1996. Structural and functional aspects of chloride binding to Alteromonas haloplanctis α-amylase. J. Biol. Chem. 271: 23836-23841.
15. Fujimoto, Z., Takase, K., Doui, N., Momma, M., Matsumoto, T., and Mizuno, H. 1998. Crystal structure of a catalytic-site mutant α-amylase from Bacillus subtilis complexed with maltopentaose. J. Mol. Biol. 277: 393-407.
16. Jones, T.A., Zhou, J.-Y., Cowan, S.W., and Kjeldgaard, M. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47: 110-119.
17. Kadziola, A., Abe, J., Svensson, B., and Haser, R. 1994. Crystal and molecular structure of barley α-amylase. J. Mol. Biol. 239: 104-121.
18. Kraulis, P.J. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24: 946-950.
19. Levitzki, A. and Steer, M.L. 1974. The allosteric activation of mammalian α-amylase by chloride. Eur. J. Biochem. 41: 171-180.
20. Machius, M., Wiegand, G., and Huber, R. 1995. Crystal structure of calcium-depleted Bacillus licheniformis α-amylase at 2.2 Å resolution. J. Mol. Biol. 246: 545-559.
21. Machius, M., Declerck, N., Huber, R., and Wiegand, G. 1998. Activation of Bacillus licheniformis α-amylase through a disorder→order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad. Structure 6: 281-292.
22. Merritt, E.A. and Bacon, D.J. 1997. Raster3D photorealistic molecular graphics. Methods Enzymol. 277: 505-524.
23. Numao, S., Maurus, R., Sidhu, G., Wang, Y., Overall, C.M., Brayer, G.D., and Withers, S.G. 2002. Probing the role of the chloride ion in the mechanism of human pancreatic α-amylase. Biochemistry 41: 215-225.
24. Otwinowski, Z. and Minor, W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276: 307-326.
25. Pereira, P.J.B., Lozanov, V., Patthy, A., Huber, R., Bode, W., Pongor, S., and Strobl, S. 1999. Specific inhibition of insect α-amylases: Yellow meal worm α-amylase in complex with the amaranth α-amylase inhibitor at 2.0 Å resolution. Structure 7: 1079-1088.
26. Ramasubbu, N., Paloth, V., Luo, Y.G., Brayer, G.D., and Levine, M.J. 1996. Structure of human salivary α-amylase at 1.6-Å resolution - Implications for its role in the oral cavity. Acta Crystallogr. D Biol. Crystallogr. 52: 435-446.
27. Rydberg, E.H., Sidhu, G., Vo, H.C., Hewitt, J., Cote, H.C., Wang, Y., Numao, S., MacGillivray, R.T., Overall, C.M., Brayer, G.D., et al. 1999. Cloning, mutagenesis, and structural analysis of human pancreatic α-amylase expressed in Pichia pastoris. Protein Sci. 8: 635-643.
28. Rydberg, E.H., Li, C., Maurus, R., Overall, C.M., Brayer, G.D., and Withers, S.G. 2002. Mechanistic analyses of catalysis in human pancreatic α-amylase: Detailed kinetic and structural studies of mutants of three conserved carboxylic acids. Biochemistry 41: 4492-4502.
29. Sambrook, J., Fritsch, E.F., and Maniatis, T. 1989. Molecular cloning: A laboratory manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
30. Steer, M.L. and Levitzki, A. 1973. The metal specificity of mammalian-amylase as revealed by enzyme activity and structural probes. FEBS Lett. 31: 89-92.
31. Suvd, D., Fujimoto, Z., Takase, K., Matsumura, M., and Mizuno, H. 2001. Crystal structure of Bacillus stearothermophilus α-amylase: Possible factors determining the thermostability. J. Biol. Chem. 129: 461-468.
32. Swift, H.J., Brady, L., Derewenda, Z.S., Dodson, E.J., Dodson, G.G., Turkenburg, J.P., and Wilkinson, A.J. 1991. Structure and molecular model refinement of Aspergillus oryzae (TAKA) α-amylase: An application of the simulated-annealing method. Acta Crystallogr. B 47: 535-544.
33. Tao, B.Y., Reilly, P.J., and Robyt, J.F. 1989. Detection of a covalent intermediate in the mechanism of action of porcine pancreatic α-amylase by using 13C nuclear magnetic resonance. Biochim. Biophys. Acta 995: 214-220.
34. Uitdehaag, J.C., Mosi, R., Kalk, K.H., van der Veen, B.A., Dijkhuizen, L., Withers, S.G., and Dijkstra, B.W. 1999. X-ray structures along the reaction pathway of cyclodextrin glycosyltransferase elucidate catalysis in the α-amylase family. Nat. Struct. Biol. 6: 432-436.
35. Vasella, A., Davies, G.J., and Bohm, M. 2002. Glycosidase mechanisms. Curr. Opin. Chem. Biol. 6: 619-629.
36. Wakim, J., Robinson, M., and Thoma, J.A. 1969. The active site of porcine-pancreatic α-amylase: Factors contributing to catalysis. Carbohydr. Res. 10: 487-503.
37. Wiegand, G., Epp, O., and Huber, R. 1995. The crystal structure of porcine pancreatic α-amylase in complex with the microbial inhibitor Tendamistat. J. Mol Biol. 247: 99-110.
38. Zechel, D.L. and Withers, S.G. 2000. Glycosidase mechanisms: Anatomy of a finely tuned catalyst. Acc. Chem. Res. 33: 11-18.