Rethinking Fundamentals of Enzyme Action

作者: Dexter B. Northrop

DOI: 10.1002/9780470123195.CH2

关键词:

摘要: Despite certain limitations, investigators continue to gainfully employ concepts rooted in steady-state kinetics efforts draw mechanistically relevant inferences about enzyme catalysis. By reconsidering kinetic behavior, this review develops ideas that allow one arrive at the following new definitions: (a) V/K, ratio of maximal initial velocity divided by Michaelis-Menten constant, is apparent rate constant for capture substrate into complexes are destined yield product(s) some later point time; (b) V release from captured form free product(s); and (c) K constants capture. The physiologic significance V/K also explored illuminate aspects antibiotic resistance, concept "perfection" catalysis, catalytic proficiency. conceptual basis congruent thermodynamic cycles considered an attempt achieve unambiguous way comparing enzyme-catalyzed reaction with its uncatalyzed reference reaction. Such promise a deeper understanding origins power, as it relates stabilization reactant ground state, transition reciprocal stabilizations states.

参考文章(23)
Richard L. Schowen, Catalytic Power and Transition-State Stabilization Springer, Boston, MA. pp. 77- 114 ,(1978) , 10.1007/978-1-4684-9978-0_2
George Edward Briggs, John Burdon Sanderson Haldane, A Note on the Kinetics of Enzyme Action Biochemical Journal. ,vol. 19, pp. 338- 339 ,(1925) , 10.1042/BJ0190338
W. John Albery, Jeremy R. Knowles, Evolution of enzyme function and the development of catalytic efficiency Biochemistry. ,vol. 15, pp. 5631- 5640 ,(1976) , 10.1021/BI00670A032
A Radzicka, R Wolfenden, A proficient enzyme Science. ,vol. 267, pp. 90- 93 ,(1995) , 10.1126/SCIENCE.7809611
William R. Cannon, Scott F. Singleton, Stephen J. Benkovic, A perspective on biological catalysis. Nature Structural & Molecular Biology. ,vol. 3, pp. 821- 833 ,(1996) , 10.1038/NSB1096-821
G. E. Lienhard, Enzymatic Catalysis and Transition-State Theory Science. ,vol. 180, pp. 149- 154 ,(1973) , 10.1126/SCIENCE.180.4082.149
J Kraut, How do enzymes work? Science. ,vol. 242, pp. 533- 540 ,(1988) , 10.1126/SCIENCE.3051385
F. M. Menger, Analysis of ground-state and transition-state effects in enzyme catalysis. Biochemistry. ,vol. 31, pp. 5368- 5373 ,(1992) , 10.1021/BI00138A018