How to determine the efficiency of intermediate transfer in an interacting enzyme system?
- 20 April 1987
- journal article
- Published by Wiley in FEBS Letters
- Vol. 214 (2), 244-248
- https://doi.org/10.1016/0014-5793(87)80063-7
Abstract
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].Keywords
This publication has 9 references indexed in Scilit:
- Cross-linking of the enzymes in the glycosome of Trypanosoma brucei.Journal of Biological Chemistry, 1985
- The evolution of enzyme kinetic powerBiochemical Journal, 1984
- Channelling in Enzyme ComplexesPublished by Springer Nature ,1984
- Kinetics of Coupled Reactions Catalyzed by Aspartate Aminotransferase and Glutamate DehydrogenaseEuropean Journal of Biochemistry, 1982
- A generalized theory of the transition time for sequential enzyme reactionsBiochemical Journal, 1981
- On the role of organized multienzyme systems in cellular metabolism: A general synthesisProgress in Biophysics and Molecular Biology, 1978
- Coupled enzyme assays: A general expression for the transientBiochimica et Biophysica Acta (BBA) - Enzymology, 1973
- Transient time of the pyruvate kinase‐lactate dehydrogenase system of rabbit muscle in vitroFEBS Letters, 1970