Artificial oligomerization of enzymes – a new approach to the catalytic activity regulation in reversed micelles

S. N. Nametkin, A. V. Kabanov, N. L. Klyachko, A. V. Levashov

Department of Chemical Enzymology, M. V. Lomonosov Moscow State University

Abstract: Comparative studies were carried out in the catalytic activity regulation of native α-chymotrypsin and its artificially produced hexameric form as an example of non-dissociating oligomeric enzyme (covalently cross-linked by means of succinimidyl-3-(2-pyridylthiopropionate) in the Aerosol OT reversed micelles in octane. Native (monome-ric) α-chymotrypsin exhibits maximal catalytic activity in the reversed micelles at the hydration degree w₀=10, when the radius of the micelle inner cavity is equal to the radius of the α-chymotrypsin globule. For the α-chymotrypsin hexamer, optimum is observed at w₀=45, with the inner micellar cavity radius (r=68 Å) being approximately equal to the radius of the sphere surrounding the octahedral combination of the six monomeric α-chymotrypsin molecules (r=61 Å). Thus, construction of the corresponding oligomeric structures is made easy, with the optimal catalytic activity in a preset range of the hydration degrees.

Russian Journal of Bioorganic Chemistry 1991, 17 (6):756-759

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