A Type III Polyketide Synthase (SfuPKS1) Isolated from the Edible Seaweed Exhibits Broad Substrate and Catalysis Specificity.

A type III polyketide synthase (SfuPKS1) from the edible seaweed was molecularly cloned and biochemically characterized. The recombinant SfuPKS1 catalyzed the condensation of fatty acyl-CoA with two or three malonyl-CoA using lactone-type intramolecular cyclization to produce tri- and/or tetraketides. Moreover, it can also utilize phenylpropanoyl-CoA to synthesize phloroglucinol derivatives through Claisen-type cyclization, exhibiting broad substrate and catalysis specificity. Furthermore, the catalytic efficiency (/) for acetyl-CoA was 11.8-fold higher than that for 4-coumaroyl-CoA. A pathway for the synthesis of naringenin involving SfuPKS1 was also constructed in by recombinant means, resulting in 4.9 mg of naringenin per liter.