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Enzyme Catalysis

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Abstract

Enzymes catalyze efficiently various reactions with astounding rates. Understanding the dynamics and molecular mechanism of enzymes has been an important research goal for more than half a century.

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References

  • Belasco JG and Knowles JR. Direct observation of substrate distortion by triosephosphate isomerase using Fourier transform infrared spectroscopy. Biochemistry, 1980, 19:472-477.

    Google Scholar 

  • Boehr DD, Nussinov R, and Wright PE. The role of dynamic conformational ensembles in biomolecular recognition. Nature Chemical Biology, 2009, 5(11):789-796.

    Google Scholar 

  • Bracken C. NMR spin relaxation methods for characterization of disorder and folding proteins. Journal of Molecular Graphics and Modelling, 2001, 19:3-12.

    Google Scholar 

  • Clarkson J, Tonge PJ, Taylor KL, Dunaway-Mariano D and Carey PR. Raman study of the polarizing forces promoting catalysis in 4-chlorobenzoate–CoA dehalogenase. Biochemistry, 1997, 36:10192–10199.

    Google Scholar 

  • Deng H, Zheng J, Sloan D, Burgner J and Callender R. A vibrational analysis of the catalytically important C4–H bonds of NADH bound to lactate or malate dehydrogenase: ground-state effects. Biochemistry, 1992, 31:5085–5092.

    Google Scholar 

  • Hedstrom L. Serine protease mechanism and specificity.Chemical Reviews, 2002, 102:4501-4523.

    Google Scholar 

  • Henzler-Wildman K and Kern D. Dynamic personalities of proteins. Nature, 2007, 450:964-972.

    Google Scholar 

  • Hong SY and Yoo YJ. Activity enhancement of Candida antarctica lipase B by flexibility modulation in helix region surrounding the active site. Appl. Biochem. Biotechnol., 2013, 170: 925-933.

    Google Scholar 

  • Hong SY, Park HJ and Yoo YJ. Flexibility analysis of activity-enhanced mutants of bacteriophage T4 lysozyme.J. Mol. Catalysis B : Enzymatic, 2014, 106:95-99.

    Google Scholar 

  • Koshland DE. Application of a theory of enzyme specificity to protein synthesis. Proc Natl Acad Sci USA, 1958, 44:98-104.

    Google Scholar 

  • Koshland DEJ. Mechanism of transfer enzyme in: The Enzymes, revised edition (Boyer P, Lardy H, and Myrback K ed.). Academic Press, New York, 1959, 305-346.

    Google Scholar 

  • Masterson LR, Shi L, Metcalfe E, Gao J, Taylor SS and Veglia G. Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy. Proceedings of the National Academy of Sciences, 2011, 108:6969–6974.

    Google Scholar 

  • Matthews BW. Structural basis of the action of thermolysin and related zinc peptidases. Accounts of Chemical Research, 1988, 21:333-340.

    Google Scholar 

  • Nashine VC, Hammes-Schiffer S and Benkovic SJ. Coupled motions in enzyme catalysis. Current Opinion in Chemical Biology, 2010, 14:644–651.

    Google Scholar 

  • Parkin DW and Schramm VL. Binding modes for substrate and a proposed transition-state analogue of protozoan nucleoside hydrolase. Biochemisty, 1995, 34:13961-13966.

    Google Scholar 

  • Robertus JD, Kraut J, Alden RA and Birktoft JJ. Subtilisin; a stereochemical mechanism involving transition-state stabilization. Biochemistry, 1972, 11:4293–4303.

    Google Scholar 

  • Schramm VL. Enzymatic transition states and transition state analog design. Annual Review of Biochemistry, 1998, 67:693-720.

    Google Scholar 

  • Schwartz SD and Schramm VL. Enzymatic transition states and dynamic motion in barrier crossing. Nature Chemical Biology, 2009, 5:551-558.

    Google Scholar 

  • Skinner JJ, Wood S, Shorter J, Englander SW and Black BE. The Mad2 partial unfolding model: regulating mitosis through Mad2 conformational switching. Journal of Cell Biology, 2008, 183:761–768.

    Google Scholar 

  • Sullivan SM and Holyoak T. Enzymes with lid-gated active sites must operate by an induced fit mechanism instead of conformational selection. Proceedings of the National Academy of Sciences, 2008, 105(37):13829-13834.

    Google Scholar 

  • Warshel A and Levitt M. Theoretical studies of enzymatic reactions: dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme. Journal of Molecular Biology, 1976, 103:227-249.

    Google Scholar 

  • Wolf-Wats M, Thai V, Henzler-Wildman K, Hadjipavlou G, Eisenmesser EZ and Kern D. Linkage between dynamics and catalysis in a thermophilic-mesophilic enzyme pair. Nature Structural & Molecular Biology, 2004, 11:945-949.

    Google Scholar 

  • Yadid I, Kirshenbaum N, Sharon M, Dym O and Tawfik DS. Metamorphic proteins mediate evolutionary transitions of structure. Proceedings of the National Academy of Sciences, 2010, 107:7287–7292.

    Google Scholar 

Download references

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Correspondence to Young Je Yoo .

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Yoo, Y.J., Feng, Y., Kim, Y.H., Yagonia, C.F.J. (2017). Enzyme Catalysis. In: Fundamentals of Enzyme Engineering. Springer, Dordrecht. https://doi.org/10.1007/978-94-024-1026-6_9

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