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.
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 (wo = 23) or in a form of separate subunits, a heavy one, beta, and a light one, alpha (wo = 20 and 14, respectively). The reversible dissociation of the enzyme was confirmed by ultracentrifugation followed by electrophoresis.
Kabakov
V E
VE
Department of Chemical Enzymology, Moscow State University, Russia.
Merker
S
S
Klyachko
N L
NL
Martinek
K
K
Levashov
A V
AV
D004143:Dioctyl Sulfosuccinic Acid; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology*; D007700:Kinetics; D046911:Macromolecular Substances; D008823:Micelles; D009795:Octanes / Q000494:pharmacology; D010399:Penicillin Amidase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D010664:Phenylmethylsulfonyl Fluoride / Q000494:pharmacology; D013501:Surface-Active Agents
D046911:Macromolecular Substances; D008823:Micelles; D009795:Octanes; D013501:Surface-Active Agents; D004143:Dioctyl Sulfosuccinic Acid; D010664:Phenylmethylsulfonyl Fluoride; D010399:Penicillin Amidase; C026728:octane