Skip to main content
NCBI home page
Biophysical Journal logoLink to Biophysical Journal
. 1983 Jan;41(1):23–28. doi: 10.1016/S0006-3495(83)84401-4

Theoretical analysis of the significance of whether or not enzymes or transport systems in structured media follow Michaelis-Menten kinetics.

J C Vincent, M Thellier
PMCID: PMC1329009  PMID: 6824750

Abstract

Pure Michaelis-Menten enzymes have been studied (i.e., enzymes with a hyperbolic (S, V) behavior in a well-stirred solution). When such enzymes are associated with a structure in vitro, even in the simplest conceivable form (immobilization in a homogeneous gel), they can produce enzymic or transport reactions with many different kinetics (Michaelis-Menten, sigmoidal, dual-phasic, etc.). Therefore, when structured enzyme or transport processes in vivo have sigmoidal kinetics, it is not proof that the corresponding proteins are allosteric. In same manner, when the apparent kinetics are dual-phasic, it is not proof that two enzyme, or transport systems, coexist.

Full text

PDF
23

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bunow B. Cellular enzymology: the steady-state kinetics of compartmentalized enzymes. J Theor Biol. 1980 Jun 21;84(4):611–627. doi: 10.1016/s0022-5193(80)80023-3. [DOI] [PubMed] [Google Scholar]
  2. Desimone J. A., Price S. An alternative to allosteric interactions as causes of sigmoid dose versus response curves. Application to glucose-induced secretion of insulin. Biochim Biophys Acta. 1978 Jan 3;538(1):120–126. doi: 10.1016/0304-4165(78)90256-8. [DOI] [PubMed] [Google Scholar]
  3. Epstein E., Hagen C. E. A KINETIC STUDY OF THE ABSORPTION OF ALKALI CATIONS BY BARLEY ROOTS. Plant Physiol. 1952 Jul;27(3):457–474. doi: 10.1104/pp.27.3.457. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Glass A. D. Regulation of potassium absorption in barley roots: an allosteric model. Plant Physiol. 1976 Jul;58(1):33–37. doi: 10.1104/pp.58.1.33. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. MONOD J., CHANGEUX J. P., JACOB F. Allosteric proteins and cellular control systems. J Mol Biol. 1963 Apr;6:306–329. doi: 10.1016/s0022-2836(63)80091-1. [DOI] [PubMed] [Google Scholar]
  6. MONOD J., WYMAN J., CHANGEUX J. P. ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL. J Mol Biol. 1965 May;12:88–118. doi: 10.1016/s0022-2836(65)80285-6. [DOI] [PubMed] [Google Scholar]
  7. Selegny E., Vincent J. C. Two enzyme active transport in vitro with pH induced asymmetrical functional structures I. The model and its analytical treatment. Biophys Chem. 1980 Aug;12(1):93–106. doi: 10.1016/0301-4622(80)80043-3. [DOI] [PubMed] [Google Scholar]
  8. Selegny E., Vincent J. C. Two enzyme active transport in vitro with pH induced asymmetrical functional structures. II. Properties of the pump and experimental illustrations. Biophys Chem. 1980 Aug;12(1):107–119. doi: 10.1016/0301-4622(80)80044-5. [DOI] [PubMed] [Google Scholar]
  9. Vincent J. C., Selegny E. Oscillations temporelles en milieu enzymatique structuré. Transport vectoriel à oscillation spatio-temporelle. Etude analytique. C R Seances Acad Sci III. 1981 Jan 12;292(2):173–176. [PubMed] [Google Scholar]

Articles from Biophysical Journal are provided here courtesy of The Biophysical Society

RESOURCES