Kinetic of enzyme action

This equation is fundamental to all aspects of the kinetics of enzyme action. The Michaelis-Menten constant, KM, is defined as the concentration of the substrate at which a given enzyme yields one-half of its maximum velocity. is the maximum velocity, which is the rate approached at infinitely high substrate concentration. The Michaelis-Menten equation is the rate equation for a one-substrate enzyme-catalyzed reaction. It provides the quantitative calculation of enzyme characteristics and the analysis for a specific substrate under defined conditions of pH and temperature. KM is a direct measure of the strength of the binding between the enzyme and the substrate. For example, chymotrypsin has a Ku value of 108 mM when glycyltyrosinylglycine is used as its substrate, while the Km value is 2.5 mM when N-20 benzoyltyrosineamide is used as a substrate... 

Laidler, K. J., The Chemical Kinetics of Enzyme Action, Clarendon Press, Oxford, 1958. 

Laidler, K. J., and Bunting, P. S. (1973). The Chemical Kinetics of Enzyme Action. Oxford Univ. Press (Clarendon), London and New York, le Noble, W. J. (1967). Prog. Phys. Org. Chem. 5, 207. 

How can we elucidate the role of serine 195 in chymotrypsin action A study of the enzyme s kinetics provided a second clue to chymotrypsin s catalytic mechanism and the role of serine 195. The kinetics of enzyme action are often easily monitored by having the enzyme act on a substrate analog that forms a colored product. For chymotrypsin, such a chromogenic substrate is A-acetyl-l-phenyManine />-nitrophenyl ester. This substrate is an ester rather than an amide, but many proteases will also hydrolyze esters. One of the products formed by chymotrypsin s cleavage of this substrate is p- nitrophenolate, which has a yellow color (Figure 9.3). Measurements of the absorbance of light revealed the amount of p-nitrophenolate being produced. 

A note on the kinetics of enzyme action. Eiochemical Journal, 19, 338-339. 

K. Laidler and P. S. Bunting, The Chemical Kinetics of Enzyme Action. Clarendon Press, Oxford, 1973. A. G. Marshall, Biophysical Chemistry. Principles, Techniques, and Applications. Wiley, New York, 1978. 

As Dixon (I) recently pointed out, there are some 450 known enzymes, all protein molecules, of which about 100 have been obtained in crystalline form. The physical chemist may expect to help particularly with two fundamental problems of the kinetics of enzyme action, (a) the mechanisms of lowering of the activation-free energy barrier in individual enzymes and... 

Bousquet-Dubouch MP, Graber M, Sousa N et al. (2(X)1) Alcoholysis catalyzed by Candida antarc-tica lipase B in a gas/soUd system obeys a ping pong bi bi mechanism with competitive inhibition by the alcohol substrate and water. Biochim Biophys Acta 1550 90-99 Briggs GE, Haldane IBS (1925) A note on the kinetics of enzyme action. Biochem J 19 338-339 Buchholz K, Kasche V, Bomscheuer UT (2005) Biocatalysts and enzyme technology. Whey VCH, Weinhein, 448 pp... 

Ladero M, Ferrero R, Vian A et al. (2005) Kinetic of the thermal and pH inactivation of a thermostable 3-galactosidase from Thermits sp. strain T2. Enzyme Microb Technol 37 505-513 Laidler KJ, Bunting PS (1973) The chemical kinetics of enzyme action, 2nd edn. Clarendon Press, Oxford, 471 pp... 

Laidler K J, Bunting P S (1973), The chemical kinetics of enzyme action, London, GB, Oxford University Press. 

Rabinovich, M. L, Klesov, A. A, Berezin, 1. V. (1977). The Kinetics of Enzyme Action Tsellyuhticheskih Geotrilium Candidum, Viscometric Analysis of the Kinetics of Hydrolysis of CMC. Bioorganic Chemistry 3(3), 8405 14. 

The fact that the kinetics of enzyme action was of such major interest to physical biochemists resulted in the development of techniques and theoretical analyses which have subsequently found valuable applications to the study of many other proteins. The experiences gained in the study of the physical chemistry of enzymes have contributed a great deal to invest -... 

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