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NTIS 바로가기Journal of microbiology and biotechnology, v.15 no.3, 2005년, pp.587 - 594
PARK HYUN (Korea Polar Research Institute, Korea Ocean Research & Development Institute) , LEE KI-SEOG (Division of Biotechnology and Genetic Engineering, Korea Ocean Research & Development Institute) , PARK SEON-MI (Division of Biotechnology and Genetic Engineering, Korea Ocean Research & Development Institute) , LEE KWANG-WON (Division of Food Science, Korea University) , KIM AUGUSTINE YONGHWI (Department of Food Science & Technology, Sejong University) , CHI YOUNG-MIN (Division of Biotechnology and Genetic Engineering, Korea Ocean Research & Development Institute)
The contribution of electrostriction of water molecules to the stabilization of the negatively charged tetrahedral transition state of a lipase-catalyzed reaction was examined by means of kinetic studies involving high-pressure and solvent dielectric constant. A good correlation was observed between...
Britto, P. J., L. Knipling, and J. Wolff. 2002. The local electrostatic environment determines cysteine reactivity of tubulin. J. Biol. Chem. 277: 29018-29027
Burdette, R. A. and D. M. Quinn. 1986. Interfacial reaction dynamics and acylenzyme mechanism for lipoprotein lipasecatalyzed hydrolysis of lipid p-nitrophenyl ester. J. Biol. Chem. 261: 12016-12021
Castaneda-Agullo, M. and L. M. Del-Castillo. 1958. The influence of the medium dielectric strength upon trypsin kinetics. J. Gen. Physiol. 42: 617-634
Compton, P. D., R. J. Coli, and A. L. Fink. 1986. Effect of methanol cryosolvents on the structural and catalytic properties of bovine trypsin. J. Biol. Chem. 261: 1248-1252
Eckert, C. A. 1972. High pressure kinetics in solution. Annu. Rev. Phys. Chem. 23: 239-264
Fink. A. L. 1974. The trypsin-catalyzed hydrolysis of N-benzyloxycarbonyl-L-lysine p-nitrophenyl ester in dimethylsulfoxide at sub-zero temperatures. J. Biol. Chem. 249: 5027-5032
Hermoso, J., D. Pignol, B. Kerfelec, I. Crenon, C. Chapus, and J. C. Fontecilla-Camps. 1996. Lipase activation by nonionic detergents: The crystal structure of the porcine lipase-colipase-tetraethylene glycol monooctyl ether complex. J. Biol. Chem. 271: 18007-18016
Isaacs, N. S. 1981. Effect of pressure on rate process, pp. 181-354. In: Liquid Phase High-Pressure Chemistry. John Wiley & Sons, New York, U.S.A
Kim, J. B. and J. S. Dordick. 1993. Pressure affects enzyme function in organic media. Biotechnol. Bioeng. 42: 772-776
Liu, R., R. Ravindernath, C. E. Ha, C. E. Petersen, N. V. Bhagavan, and R. G. Eckenhoff. 2002. The role of electrostatic interaction in human serum albumin binding and stabilization by halothane. J. Biol. Chem. 277: 36373-37379
Low, P. S. and G. N. Somero. ]975. Activation volumes in enzyme catalysis: Their sources and modification by lowmolecular-weight solutes. Proc. Nat. Acad. Sci. USA 72: 3014-3018
Low, P. S. and G. N. Somero. 1975. Protein hydration changes during catalysis: A new mechanism of enzyme rateenhancement and ion activation/inhibition of catalysis. Proc. Nat. Acad. Sci. USA 72: 3305-3309
Maurel, P. C. 1978. Relevance of dielectric constant and solvent hydrophobicity to the organic solvent effect in enzymology. J. Biol. Chem. 253: 1677-1683
Michels, P. C., J. S. Dordick, and D. S. Clark. 1997. Dipole formation and solvent electrostriction in subtilisin catalysis. J. Am. Chem. Soc. 119: 9331-9336
Moreau, H., A. Moulin, Y. Gargouri, J. Noel, and R. Verger. 1991. Inactivation of gastric and pancreatic lipases by diethyl p-nitrophenyl phosphate. Biochemistry 30: 1037-1041
Nakasako, M., M. Odaka, M. Yohda, N. Dohmae, K. Takio, N. Kamiya, and J. Endo. 1999. Tertiary and quaternary structure of photoreactive Fe-type nitrile hydratase from Rhodococcus sp. N-771: Roles of hydration water molecules in stabilizing the structure and the structural origin of the substrate specificity of the enzyme. Biochemistry 38: 9887-9898
Nicolas, A., M. Egmond, T. Verrips, J. Vlieg, S. Longhi, C. Cambillau, and C. Martinez. 1996. Contribution of cutinase serine 42 side chain to the stabilization of the oxyanion transition state. Biochemistly 35: 398-410
Petersen, M. T. N., P. Fojan, and S. B. Petersen. 2001. How do lipases and esterases work: The electrostatic contribution. J. Biotechnol. 85: 115-147
Reichardt, C. 1988. Solvent effects on the rate of homogeneous chemical reactions, pp. 121-284. In: Solvents and Solvent Effects in Organic Chemistry, 2nd Ed., VCH, Weinheim
Svendsen, A. 2000. Lipase protein engineering. Biochim. Biophys. Acta 1543: 223-238
Szeltner, Z., D. Rea, V. Renner, L. Juliano, V. Fulop, and L. Polgar. 2003. Electrostatic environment at the active site of prolyl oligopeptidase is highly influential during substrate binding. J. Biol. Chem. 278: 48786-48793
Szeltner, Z., D. Rea, Y. Renner, V. Fulop, and L. Polgar. 2002. Electrostatic effects and binding determinants in the catalysis of prolyl oligopeptidase. J. Biol. Chem. 277: 42613-42622
Taniguchi, Y. and S. Makimoto. 1988. High pressure studies of catalysis. J. Mol. Cat. 47: 323-334
Van-Eldik, R., T. Asano, and W. J. Le Noble. 1989. Activation and reaction volumes in solution. Chem. Rev. 89: 549-688
Warshel, A. 2000. Perspective on the energetics of enzymatic reaction. Theor. Chem. Acc. 103: 337-339
Warshel, A. and S. Russel. 1986. Theoretical correlation of structure and energetics in the catalytic reaction of trypsin. J. Am. Chem. Soc. 108: 6569-6579
Xu, Z. F., A. Affleck, P. Wangikar, V. Suzawa, J. S. Dordick, and D. S. Clark. 1994. Transition state stabilization of subtilisins in organic media. Biotechnol. Bioeng. 43: 515-520
Zandonella, G., P. Stadler, L. Haalck, F. Spener, F. Paltaut, and A. Hermetter. 1999. Interactions of fluorescent triacylglycerol analogs covalently bound to the active site of a lipase from Rhizopus oryzae. Eur. J. Biochem. 262: 63-69
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