Secondary Calcium-Binding Parameter of Bacillus amyloliquefaciens α-Amylase Obtained from Inhibition Kinetics

Journal of Bioscience and Bioengineering

Volumn 96, Issue 3, 2003, Pages 262-267

  Tanaka, Atsushi ^a   Hoshino, Eiichi ^a  

^a KAO CORPORATION   (Japan)

Author keywords

Calcium; Competitive inhibition; Enthalpy; Entropy; Thermodynamic parameter; amylase

Indexed keywords

CALCIUM; CATALYSIS; CHEMICAL BONDS; CONCENTRATION (PROCESS); ENTROPY; HYDROLYSIS; IONS;

HYDROLYTIC CATALYSIS;

ENZYMES;

AMYLASE; CALCIUM ION; ENZYME;

ARTICLE; BACILLUS AMYLOLIQUEFACIENS; CALCIUM BINDING; CALCULATION; CATALYSIS; CHEMICAL ANALYSIS; CHEMICAL PARAMETERS; CONCENTRATION (PARAMETERS); CONFORMATION; DISSOCIATION CONSTANT; ENTHALPY; ENTROPY; HYDROLYSIS; INHIBITION KINETICS; MODEL; NONHUMAN; SOLUBILITY; THERMODYNAMICS;

BACILLUS AMYLOLIQUEFACIENS; POSIBACTERIA;

EID: 0141922989     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1389-1723(03)80191-3     Document Type: Article

References (37)

1. Robyt, J. F. and Whelan, W. J.: The α-amylases, p. 430-476. In Radley, J. A. (ed.), Starch and its derivatives, 4th ed. Chapman & Hall, London (1968).
2. Takagi, T., Toda, H., and Isemura, T.: Bacterial and mold amylases, p. 235-271. In Boyer, P. D. (ed.), The enzymes, 3rd ed. Academic Press, New York (1971).
3. Fogarty, W. M. and Kelly, C. T.: Amylases, amyloglucosidases and related glucanases, p. 115-170. In Rose, A. H. (ed.), Microbial enzymes and bioconversions. Academic Press, London (1980).
4. Kindle, K. L.: Characteristics and production of thermostable α-amylase. Appl. Biochem. Biotechnol., 8, 153-170 (1983).
5. Kulp, K.: Carbohydrases, p. 53-122. In Reed, G. (ed.), Enzymes in food processing, 2nd ed. Academic Press, New York (1975).
6. Reichelt, J. R.: Industrial applications, p. 375-409. In Godfrey, T. and Reichelt, J. R. (ed.), Industrial enzymology. Nature Press, New York (1983).
7. Takkinen, K., Pettersson, R. F., Kalkkinen, N., Palva, I., Soderlund, H., and Kaariainen, L.: Amino acid sequence of α-amylase from Bacillus amyloliquefaciens deduced from the nucleotide sequence of the cloned gene. J. Biol. Chem., 258, 1007-1013 (1983).
8. Vallee, B. L., Stein, E. A., Sumerwell, W. N., and Fischer, E. H.: Metal content of α-amylases of various origins. J. Biol. Chem., 234, 2901-2905 (1959).
9. Payan, F., Haser, R., Pierrot, M., Frey, M., Astier, J. P., Abadie, B., Duee, E., and Buisson, G.: The three-dimensional structure of α-amylase from porcine pancreas at 5 Å resolution. Acta Crystallogr., B36, 416-421 (1980).
10. Kuroki, R., Kawakita, S., Nakamura, H., and Yutani, K.: Entropic stabilization of a mutant human lysozyme induced by calcium binding. Proc. Natl. Acad. Sci. USA, 89, 6803-6807 (1992).
11. Qian, M., Haser, R., Buisson, G., Duee, E., and Payan, F.: The active center of a mammalian α-amylase. Structure of the complex of a pancreatic α-amylase with a carbohydrate inhibitor refined to 2.2-Å resolution. Biochemistry, 33, 6284-6294 (1994).
12. Feller, G., d'Amico, D., and Gerday, C.: Thermodynamic stability of a cold-active α-amylase from the Antarctic bacterium Alteromonas haloplanctis. Biochemistry, 38, 4613-4619 (1999).
13. Suvd, D., Fujimoto, Z., Takase, K., Matsumura, M., and Mizuno, H.: Crystal structure of Bacillus stearothermophilus α-amylase: possible factors determining the thermostability. J. Biochem., 129, 461-468 (2001).
14. Irshad, M. and Sharma, C. B.: Sensitivity of plant α-amylases to calcium ions in vitro. Phytochemistry, 20, 1205-1209 (1981).
15. Boel, E., Brady, L., Brzozowski, A.M., Derewenda, Z., Dodson, G. G., Jensen, V. J., Petersen, S. B., Swift, H., Thim, L., and Woldike, H. E: Calcium binding in α-amylases: an X-ray diffraction study at 2.1-Å resolution of two enzyme from Aspergillus. Biochemistry, 29, 6244-6249 (1990).
16. Saboury, A.A. and Karbassi, F.: Thermodynamic studies on the interaction of calcium ions with α-amylase. Thermochim. Acta, 362, 121-129 (2000).
17. Buchanan, J. D., Corbett, R. J. T., and Roche, R. S.: The thermodynamics of calcium binding to thermolysin. Biophys. Chem., 23, 183-199 (1986).
18. 2+ to a mutant human lysozyme. J. Biol. Chem., 267, 24297-24301 (1992).
19. Matsuura, Y., Kusunoki, M., Harada, W., and Kakudo, M.: Structure and possible catalytic residues of Taka-amylase A. J. Biochem., 95, 697-702 (1984).
20. Kadziola, A., Abe, J., Svensson, B., and Haser, R.: Crystal and molecular structure of barley α-amylase. J. Mol. Biol., 239, 104-121 (1994).
21. Machius, M., Declerck, N., Huber, R., and Wiegand, G.: 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 (1998).
22. Brzozowski, A. M., Lawson, D. M., Turkenburg, J. P., Frantzen, H. B., Svendsen, A., Borchert, T. V., Dauter, Z., Wilson, K. S., and Davies, G. J.: Structural analysis of a chimeric bacterial α-amylase. High-resolution analysis of native and ligand complexes. Biochemistry, 39, 9099-9107 (2000).
23. Machius, M., Wiegand, G., and Huber, R.: Crystal structure of calcium-depleted Bacillus licheniformis α-amylase at 2.2 Å resolution. J. Mol. Biol., 246, 545-559 (1995).
24. Fitter, J., Herrmann, R., Dencher, N. A., Blume, A., and Hauss, T.: Activity and stability of a thermostable α-amylase compared to its mesophilic homologue: mechanisms of thermal adaptation. Biochemistry, 40, 10723-10731 (2001).
25. Suzuki, A., Yamane, T., Ito, Y., Nishio, T., Fujiwara, H., and Ashida, T.: Crystallization and preliminary crystallographic study of bacterial α-amylases. J. Biochem., 108, 379-381 (1990).
26. Strumeyer, D.H.: A modified starch for use in amylose assays. Anal. Biochem., 19, 61-71 (1967).
27. Tanaka, A. and Hoshino, E.: Thermodynamic and activation parameters for the hydrolysis of amylose with Bacillus α-amylases in a diluted anionic surfactant solution. J. Biosci. Bioeng., 93, 485-490 (2002).
28. Bernfeld, P.: Amylases, α and β. Methods Enzymol., 1, 149-158 (1955).
29. Kato, T. and Kinoshita, T.: Fluorometric detection and determination of carbohydrates by high-performance liquid chromatography using ethanolamine. Anal. Biochem., 106, 238-243 (1980).
30. Laidler, K.J.: Influence of ionic strength, p. 197-201. In Chemical kinetics, 3rd ed. Harper Collins Publishers, New York (1987).
31. Dunitz, J. D.: The entropic cost of bound water in crystals and biomolecules. Science, 264, 670 (1994).
32. Snider, M. J., Gaunitz, S., Ridgway, C., Short, S. A., and Wolfenden, R.: Temperature effects on the catalytic efficiency, rate enhancement, and transition state affinity of cytidine deaminase, and the thermodynamic consequences for catalysis of removing a substrate "anchor". Biochemistry, 39, 9746-9753 (2000).
33. 13C nuclear magnetic resonance. Biochim. Biophys. Acta, 995, 214-220 (1989).
34. Tanaka, A. and Hoshino, E.: Calcium-binding parameter of Bacillus amyloliquefaciens α-amylase determined by inactivation kinetics. Biochem. J., 364, 635-639 (2002).
35. Privalov, P. L. and Khechinashvili, N. N.: Thermodynamic approach to the problem of stabilization of globular protein structure. J. Mol. Biol., 86, 665-684 (1974).
36. Elwell, M. L. and Schellman, J. A.: Stability of phage T4 lysozymes. Biochim. Biophys. Acta, 494, 367-383 (1977).
37. Campoy, A. V., Todd, M. J., and Freire, E.: HIV-1 protease inhibitors: enthalpic versus entropic optimization of the binding affinity. Biochemistry, 39, 2201-2207 (2000).