참고문헌
- Barman, T. E. (1969) Enzyme Handbook, Springer-Verlag, New York, USA.
- Bearne, S. L. and Wolfenden, R. (1995) Enzymic hydration of an olefin: the burden borne by fumarase. J. Am. Chem. Soc. 117, 9588-9589. https://doi.org/10.1021/ja00142a037
- Britt, B. M. (1993) A shifting specificity model for enzyme catalysis. J. Theor. Biol. 164, 181-190.
- Britt, B. M. (1997) For enzymes, bigger is better. Biophys. Chem. 69, 63-70. https://doi.org/10.1016/S0301-4622(97)00082-3
- Britt, B. M. (2004) Understanding enzyme structure and function in terms of the shifting specificity model. J. Biochem. Mol. Biol., 37, 394-401. https://doi.org/10.5483/BMBRep.2004.37.4.394
- Creighton, T. E. (1983) Proteins in Catalysis, p. 420, W. H. Freeman and Co., New York, USA.
- Chipman, D. M. (1971) A kinetic analysis of the reaction of lysozyme with oligosaccharides from bacterial cell walls. Biochemistry 10, 1714-1722. https://doi.org/10.1021/bi00785a032
- Fabianowski-Wajewska, K. and Greger, J. (1992) Adenosine deaminase: physical and chemical properties of partially purified mitochondrial and cytosol enzyme from rat liver. Acta Biochimica Polonica 39, 193-204.
- Fersht, A. (2000) Structure and mechanism in protein science; in Enzyme-substrate complementarity and the use of binding energy in catalysis, pp. 349-375, W. H. Freeman and Co., New York, USA.
- Frick, L., MacNeela, J. P. and Wolfenden, R. (1987) Transition state stabilization by deaminases: rates of nonenzymatic hydrolysis of adenosine and cytidine. Bioorg. Chem. 15, 100-108. https://doi.org/10.1016/0045-2068(87)90011-3
- Hall, A. and Knowles, J. (1975) Uncatalyzed rates of enolization of dihydroxyacetone phosphate and of glyceraldehyde 3-phosphate in neutral aqueous solution. Quantitative assessment of the effectiveness of an enzyme catalyst. Biochemistry 14, 4348-4352. https://doi.org/10.1021/bi00690a032
- Harel, M., Quinn, D. M., Nair, I., Silman, I. and Sussman, J. L. (1996) The x-ray structure of a transition state analog complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase. J. Am. Chem. Soc. 118, 2340-2346. https://doi.org/10.1021/ja952232h
-
Hurley, J. H. and Remington, S. J. (1992) Contribution of charged side chains,
$Mg^{2+}$ , and solvent exclusion to enzymic$\beta$ -decarboxylation of$\alpha$ -keto acids. J. Am. Chem. Soc. 114, 4769-4773. https://doi.org/10.1021/ja00038a047 - Koshland, D. E., Jr. (1962) The comparison of non-enzymic and enzymic reaction velocities. J. Theor. Biol. 2, 75-86. https://doi.org/10.1016/0022-5193(62)90037-1
- Olsen, K., Svensson, B. and Cristensen, U. (1992) Stopped-flow fluorescence and steady-state kinetic studies of ligand- binding reactions of glucoamylase from Aspergillus niger. Eur. J. Biochem. 209, 777-784. https://doi.org/10.1111/j.1432-1033.1992.tb17348.x
- Pocker, Y. and Meany, J. E. (1967) A comparative study of enzymatic and metal ion catalyzed hydration of pyridine aldehydes. J. Am. Chem. Soc. 89, 631-636. https://doi.org/10.1021/ja00979a029
- Radzicka, A. and Wolfenden, R. (1995) A proficient enzyme. Science 267, 90-93. https://doi.org/10.1126/science.7809611
- Snider, M. J. and Wolfenden, R. (2000) The rate of spontaneous decarboxylation of amino acids. J. Am. Chem. Soc. 122, 11507-11508. https://doi.org/10.1021/ja002851c
- Tempczyk, A., Tarnowska, M., Liwo, A., and Borowski, E. (1992) A theoretical study of glucosamine synthase. II. combined quantum and molecular mechanics simulation of sulfhydryl attack on the carboxyamide group. Eur. Biophys. J. 21, 137 145.
피인용 문헌
- Partial Phase Diagram of Aqueous Bovine Carbonic Anhydrase: Analyses of the Pressure-Dependent Temperatures of the Low- to Physiological-Temperature Nondenaturational Conformational Change and of Unfolding to the Molten Globule State vol.26, pp.2, 2008, https://doi.org/10.1080/07391102.2008.10507242