Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1990 Jul 15;269(2):389–392. doi: 10.1042/bj2690389

Hysteresis of plant cell-wall beta-glucosidase.

G Cheron 1, G Noat 1, J Ricard 1
PMCID: PMC1131589  PMID: 2117438

Abstract

A transient-kinetic study of beta-glucosidase from soyabean cell walls was performed with the use of a stopped-flow apparatus. The progress curve of the reaction exhibits a 'slow' burst of about 1 s before the steady state is reached. In the time scale investigated this burst may be accounted for by only one exponential, whose time constant varies with the substrate concentration. As this concentration is increased the value of the time constant increases at first, then decreases. Premixing the enzyme with glucose, the last product of the reaction sequence, reverses the 'slow' burst into a 'slow' lag. Taken together, these results are only compatible with a model that involves the existence of a 'slow' conformational transition of the enzyme.

Full text

PDF
389

Selected References

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

  1. Ainslie G. R., Jr, Shill J. P., Neet K. E. Transients and cooperativity. A slow transition model for relating transients and cooperative kinetics of enzymes. J Biol Chem. 1972 Nov 10;247(21):7088–7096. [PubMed] [Google Scholar]
  2. Barshop B. A., Wrenn R. F., Frieden C. Analysis of numerical methods for computer simulation of kinetic processes: development of KINSIM--a flexible, portable system. Anal Biochem. 1983 Apr 1;130(1):134–145. doi: 10.1016/0003-2697(83)90660-7. [DOI] [PubMed] [Google Scholar]
  3. Bearer C. F., Neet K. E. Threonine inhibition of the aspartokinase--homoserine dehydrogenase I of Escherichia coli. Stopped-flow kinetics and the cooperativity of inhibition of the homoserine dehydrogenase activity. Biochemistry. 1978 Aug 22;17(17):3517–3522. doi: 10.1021/bi00610a015. [DOI] [PubMed] [Google Scholar]
  4. Cornish-Bowden A., Cárdenas M. L. Co-operativity in monomeric enzymes. J Theor Biol. 1987 Jan 7;124(1):1–23. doi: 10.1016/s0022-5193(87)80248-5. [DOI] [PubMed] [Google Scholar]
  5. Frieden C. Kinetic aspects of regulation of metabolic processes. The hysteretic enzyme concept. J Biol Chem. 1970 Nov 10;245(21):5788–5799. [PubMed] [Google Scholar]
  6. Frieden C. Slow transitions and hysteretic behavior in enzymes. Annu Rev Biochem. 1979;48:471–489. doi: 10.1146/annurev.bi.48.070179.002351. [DOI] [PubMed] [Google Scholar]
  7. Hatfield G. W., Ray W. J., Jr, Umbarger H. E. Threonine deaminase from Bacillus subtilis. 3. Pre-steady state kinetic properties. J Biol Chem. 1970 Apr 10;245(7):1748–1753. [PubMed] [Google Scholar]
  8. Meunier J. C., Buc J., Ricard J. Enzyme memory. Effect of glucose 6-phosphate and temperature on the molecular transition of wheat-germ hexokinase LI. Eur J Biochem. 1979 Jul;97(2):573–583. doi: 10.1111/j.1432-1033.1979.tb13146.x. [DOI] [PubMed] [Google Scholar]
  9. Nari J., Noat G., Ricard J. pH-induced co-operative effects in hysteretic enzymes. 2. pH-induced co-operative effects in a cell-wall beta-glucosyltransferase. Eur J Biochem. 1984 Dec 3;145(2):319–322. doi: 10.1111/j.1432-1033.1984.tb08555.x. [DOI] [PubMed] [Google Scholar]
  10. Neet K. E., Ainslie G. R., Jr Hysteretic enzymes. Methods Enzymol. 1980;64:192–226. doi: 10.1016/s0076-6879(80)64010-5. [DOI] [PubMed] [Google Scholar]
  11. Ricard J., Buc J., Meunier J. C. Enzyme memory. 1. A transient kinetic study of wheat-germ hexokinase LI. Eur J Biochem. 1977 Nov 1;80(2):581–592. doi: 10.1111/j.1432-1033.1977.tb11915.x. [DOI] [PubMed] [Google Scholar]
  12. WILKINSON G. N. Statistical estimations in enzyme kinetics. Biochem J. 1961 Aug;80:324–332. doi: 10.1042/bj0800324. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES