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How to determine the efficiency of intermediate transfer in an interacting enzyme system?
Author(s) -
Tompa Péter,
Batke József,
Ovádi Judit
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80063-7
Subject(s) - kinetics , transient (computer programming) , channel (broadcasting) , kinetic energy , chemistry , glutamate dehydrogenase , enzyme , enzyme kinetics , thermodynamics , function (biology) , dehydrogenase , molecule , computational chemistry , biophysics , glutamate receptor , biochemistry , physics , computer science , biology , organic chemistry , active site , quantum mechanics , computer network , receptor , operating system , evolutionary biology
A kinetic method, based upon measuring the transient time of coupled reactions, is proposed for the determination of the intermediate channel efficiency in a system of functionally interacting enzymes. The procedure rests upon a novel description in which the transient time is expressed as a function of channel efficiency and lifetime of the intermediate molecules. By this approach the reduction of transient time can be explained even if no changes in the kinetic parameters of the individual reactions occur. For determining channel efficiency, a linearized form has been evaluated and applied to the analysis of the kinetics of the aspartate aminotransferase‐glutamate dehydrogenase coupled reaction, for which the data were taken from the literature [(1982) Eur. J. Biochem. 121, 511–517].