STEADY STATE KINETICS OF AN ENZYME REACTION WITH ONE SUBSTRATE AND ONE MODIFIER

被引：10

作者：

LONDON, WP

机构：

[1] Mathematical Research Branch, National Institute of Arthritis and Metabolic Diseases, National Institutes of Health, Bethesda, Maryland

来源：

BULLETIN OF MATHEMATICAL BIOPHYSICS | 1968年 / 30卷 / 02期

关键词：

D O I：

10.1007/BF02476694

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

This study examines the steady state kinetics of a reaction involving an enzyme, a substrate and a modifier when the reaction follows Michaelis-Menten kinetics. Conditions for Michaelis-Menten kinetics are deduced, and it is shown that an analogue of detailed balance determines the complexity of the rate equations in these cases. A scheme to distinguish many cases of Michaelis-Menten kinetics is presented. It is shown that steady state kinetics are, in general, insufficient to specify the mechanism of a reaction, since different effects of a modifier can give identical steady state kinetic data. © 1968 N. Rashevsky.

引用

页码：253 / &

共 13 条

[1] ATKINSON JE, 1966, ANN REV BIOCHEM, V35, P85
[2] BOYER PD, 1959, ENZYMES ED, pCH2
[3] KINETICS OF ENZYME-CATALYZED REACTIONS WITH 2 OR MORE SUBSTRATES OR PRODUCTS .2. INHIBITION - NOMENCLATURE AND THEORY
CLELAND, WW
[J]. BIOCHIMICA ET BIOPHYSICA ACTA, 1963, 67 (02) : 173 - &
[4] Dixon M., 1964, ENZYMES
[5] DOWD JE, 1965, J BIOL CHEM, V240, P863
[6] FRIEDEN C, 1964, J BIOL CHEM, V239, P3522
[7] HEARON JZ, 1959, ENZYMES, pCH2
[8] KELETI T, 1966, ENZYMOLOGIA, V31, P39
[9] GENERAL STEADY-STATE EQUATIONS IN ENZYME AND OTHER CATALYZED REACTIONS
LAIDLER, KJ
[J]. TRANSACTIONS OF THE FARADAY SOCIETY, 1956, 52 (10): : 1374 - 1382
[10] LONDON WP, 1966, J BIOL CHEM, V241, P3008

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