Abstract:
:Regulation of supra-macromolecular composition and catalytic activity of a heterodimeric enzyme, gamma-glutamyltransferase, in the system of Aerosol OT (sodium bis(2-ethylhexyl) sulfosuccinate) reversed micelles in octane were studied. Variation of the surfactant hydration degree (parameter, determining dimensions of the polar inner cavity of the micelle) causes a reversible dissociation of the enzyme to light and heavy subunits. Both enzyme subunits possess catalytic activity. The light and heavy subunits of the enzyme were separated on a preparative scale in a reversed micelle system using ultracentrifugation. The active centers of gamma-glutamyltransferase were studied using its irreversible inhibitor--AT-125 (L-(alpha S, 5S)-alpha-amino-3-chloro-4,5-dihydro-5-isoxazoleacetic acid). Separation of the gamma-glutamyltransferase subunits results in the 'opening' of a new active center located at the heavy subunit. In the dimer form of the enzyme this center is masked and it is not accessible to both substrate and inhibitor molecules.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Kabanov AV,Nametkin SN,Chernov NN,Klyachko NL,Levashov AVdoi
10.1016/0014-5793(91)81388-osubject
Has Abstractpub_date
1991-12-16 00:00:00pages
73-6issue
1-3eissn
0014-5793issn
1873-3468pii
0014-5793(91)81388-Ojournal_volume
295pub_type
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