有哪些信誉好的足球投注网站detailed enzyme kinetics in terms of biochemical species study of citrate synthase详细的酶动力学的生化物种柠檬酸合成酶的研究.pdfVIP
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detailed enzyme kinetics in terms of biochemical species study of citrate synthase详细的酶动力学的生化物种柠檬酸合成酶的研究
Detailed Enzyme Kinetics in Terms of Biochemical Species: Study of Citrate Synthase Daniel A. Beard*, Kalyan C. Vinnakota, Fan Wu Biotechnology and Bioengineering Center and Department of Physiology, Medical College of Wisconsin, Milwaukee, Wisconsin, United States of America Abstract The compulsory-ordered ternary catalytic mechanism for two-substrate two-product enzymes is analyzed to account for binding of inhibitors to each of the four enzyme states and to maintain the relationship between the kinetic constants and the reaction equilibrium constant. The developed quasi-steady flux expression is applied to the analysis of data from citrate synthase to determine and parameterize a kinetic scheme in terms of biochemical species, in which the effects of pH, ionic strength, and cation binding to biochemical species are explicitly accounted for in the analysis of the data. This analysis provides a mechanistic model that is consistent with the data that have been used support competing hypotheses regarding the catalytic mechanism of this enzyme. Citation: Beard DA, Vinnakota KC, Wu F (2008) Detailed Enzyme Kinetics in Terms of Biochemical Species: Study of Citrate Synthase. PLoS ONE 3(3): e1825. doi:10.1371/journal.pone.0001825 Editor: Timothy Secomb, University of Arizona, United States of America Received November 29, 2007; Accepted February 20, 2008; Published March 19, 2008 Copyright: 2008 Beard et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Funding: NIH grants GM068610 and HL072011 Competing Interests: The authors have declared that no competing interests exist. * E-mail: dbeard@ Introduction
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