Add time:08/03/2019         Source:sciencedirect.com

Activity of 6-Hydroxymellein (cas 19314-92-2) synthase, an induced polyketide synthetic enzyme in carrot cell extract, was not inhibited by cerulenin which is known as a potent inhibitor for fatty acid synthases and biosynthetic enzymes of various polyketide compounds. However, when 6-hydroxymellein synthase was incubated with [3H]cerulenin in the absence of its substrates, acyl-CoAs, significant radioactivity was found to co-migrate with the enzyme protein in SDS—PAGE analysis. The radioactivity associated with the synthase was not observed when the cerulenin—enzyme complex was post-incubated with acyl-CoAs. These results suggest that cerulenin is able to bind to 6-hydroxymellein synthase and forms a complex. However, the attachment is unstable and the substrates of the synthase are capable of replacing the inhibitor at the reaction centre.

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