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Regulation of the supramolecular structure and the catalytic activity of penicillin acylase from Escherichia coli in the system of reversed micelles of Aerosol OT in octane
Author(s) -
Kabakov Vladimir E.,
Merker Steffen,
Klyachko Nataliya L.,
Martinek Karel,
Levashov Andrey V.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81104-t
Subject(s) - micelle , chemistry , dimer , escherichia coli , ultracentrifuge , dissociation (chemistry) , octane , enzyme , catalysis , supramolecular chemistry , stereochemistry , biophysics , chromatography , organic chemistry , biochemistry , molecule , biology , aqueous solution , gene
The properties of penicillin acylase from E. coli solubilized by hydrated reversed micelles (RM) of Aerosol OT in octane were studied. The dependence of catalytic activity on the hydration degree, a parameter which determines the size of the micelle inner cavity, has a curve with three optima, each one corresponding to the enzyme functioning either in a dimer form (w o = 23) or in a form of separate subunits, a heavy one, β, and a light one, α (w o = 20 and 14, respectively). The reversible dissociation of the enzyme was confirmed by ultracentrifugation followed by electrophoresis.