Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

The highest activities of carnitine acetyltransferase (CAT) were found in non-oleaginous yeasts (Candida utilis and Saccharomyces cerevisiae); lower activities, ranging from 50% down to 3% of the highest values, were found in various strains of oleaginous yeasts (Candida curvata, Lipomyces starkeyi, Rhodosporidium toruloides and Trichosporon cutaneum). Supply of acetyl units into the cytosol of the latter, but not of the former yeasts, was therefore necessarily reliant on the action of ATP: citrate lyase (ACL), which was present in all oleaginous yeasts. There was no correlation, however, between the amount of lipid in the oleaginous yeasts and the specific activities of either CAT or ACL. Activity of CAT was increased up to 30-fold by growing yeasts on a triacylglycerol. © 1985.

Original publication

DOI

10.1111/j.1574-6968.1985.tb00681.x

Type

Journal article

Journal

FEMS Microbiology Letters

Publication Date

01/01/1985

Volume

27

Pages

273 - 275