Abstract
The influence of various effectors (methanol, neutral salts) on the kinetic parameters KM and kcat has been studied. The hypothesis has been expressed that chloride ions are responsible for the worsening of the binding of the substrate to the enzyme. The temperature dependence of the kinetic parameters KM and kcat for the enzymatic hydrolysis of L-asparagine has been obtained. It has been shown that the graph of log kcat versus 1/T has a break at 30°C. The effective activation energies below and above the critical point are 6.5 and 3.6 kcal/mole, respectively.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
Literature cited
M. Ehrman, H. Cedal, and J. H. Schwartz, J. Biol. Chem.,246, 88 (1971).
M. H. O'Leary and S. L. Mattes, Biochim. Biophys. Acta,522, 238 (1978).
L. S. Hersh, J. Polym. Sci., Polym. Symp., No. 47, 55 (1974).
N. Citri and N. Zyk, Biochem.,11, 2103 (1972).
A. J. Charlson, A. J. Coman, T. A. Karossi, F. S. Stephens, R. S. Vagg, and E. C. Watton, Inorg. Chem. Acta,28, 217 (1978).
R. B. Homer and S. R. Allsopp, Biochim. Biophys. Acta, 434, 100 (1976).
I. A. Milman, I. I. Geiman, U. A. Pinka, I. P. Kirstukas, V. A. Slavinskaya, and R. A. Zhagat, Khim. Prir. Soedin., 364 (1978).
Additional information
Institute of Organic Synthesis, Academy of Sciences of the Latvian SSR, Riga. Translated from Khimiya Prirodnykh Soedinenii, No. 5, pp. 707–709, September–October, 1979.
Rights and permissions
About this article
Cite this article
Milman, I.A., Geiman, I.I., Slavinskaya, V.A. et al. Some kinetic features of the hydrolysis of L-asparagine withE. coli asparaginase. Chem Nat Compd 15, 621–623 (1979). https://doi.org/10.1007/BF00565939
Received:
Published:
Issue Date:
DOI: https://doi.org/10.1007/BF00565939