Abstract
Circular dichroism spectra of the native fatty acid synthetase complex from the insect Ceratitis capitata and of the lipidated and cholate- and SDS-treated enzyme have been obtained. Native enzyme has a calculated structure of 43% α-helix, 23% β structure and 31% random coil. Lipidation and cholate-treatment did not modify the structure of the enzyme complex whereas the SDS-treatment changed the native conformation into a structure based on 42.8% α-helix, 8.4% β structure and 48.8% random coil. These data are interpreted in terms of both the enzyme activity and the quaternary structure of the complex.
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