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

6-Hydroxymellein (cas 19314-92-2) synthase, a multifunctional polyketide biosynthetic enzyme of carrot, lost the binding ability toward its co-substrates, acetyl- and malonyl-CoAs, by the treatment with the blocking reagents for serine-OH. In contrast, the enzyme retained the binding ability even when the two SH groups at the reaction center (cysteine-SH of the condensation enzyme and cysteamine-SH of acyl carrier protein) were blocked, and one substrate bound to the SH-blocked enzyme was readily replaced by the other. It appeared that the cysteine-SH accepted only acetyl moiety while cysteamine-SH was preferentially malonylated in the presence of both of the substrates. These results suggest that transacylase-like domain is involved in the structure of 6-hydroxymellein synthase as a common primary binding site of its co-substrates, and acetyl and malonyl moieties are properly channeled from their CoA esters to cysteine-SH and acyl carrier protein-SH via this domain, respectively.

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