Add time:08/07/2019         Source:sciencedirect.com

6-Hydroxymellein (cas 19314-92-2) synthase, a multifunctional polyketide synthetic enzyme in carrot, is organized as a homodimer, and the activity of the synthase was appreciably inhibited upon the specific alkylation of cysteine- and cysteamine-SHs at the reaction center with iodoacetoamide and chloroacetyl-CoA, respectively. Dissociation and stoichiometric recombination of the unmodified and the SH-modified enzyme subunits yielded a combination of unmodified–unmodified, unmodified–modified and modified–modified hybrid dimers that together exhibit 50% activity. In contrast, hybrid dimers obtained by reconstruction of the two modified enzymes showed essentially no catalytic activity. These results suggest that the two subunits of 6-hydroxymellein synthase are aligned in head-to-tail orientation to organize two reaction centers which are comprised of a cysteine and a complementary cysteamine SH group, belonging to and contributed from the same subunit in the homodimer structure.

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