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Phloroglucinol synthase
From Wikipedia, the free encyclopedia
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Phloroglucinol synthase is an acetyltransferase enzyme involved in the synthesis of phloroglucinol (also known as 1,3,5-trihydroxybenzene or cyclohexane-1,3,5-trione), a pharmaceutically and industrially important benzentriol molecule used in medicines and explosives. The enzyme, as taken from the bacterium pseudomonas protegens (Pf-5), is a type III polyketide synthase. The enzyme cyclizes the activated form of 3,5-dioxoheptanedioate. Phloroglucinol synthase exhibits broad substrate specificity, able to accept C4-C12 aliphatic acyl-CoAs and phenylacetyl-CoAs, yielding polyoxoalkylated alpha-pyrones by condensation with malonyl-CoA.[1] The enzyme catalyzes the following reaction,
- 3 malonyl-CoA + 3 H+ = Phloroglucinol + 3 CO2 + 3 CoA
It was shown that the kcat for this enzyme (with malony-CoA as a substrate) was 10 min-1. Its product, phloroglucinol is used in industry as well as in the synthesis of pharmaceuticals. It can be used to make phloroglucinol but it shows low productivity.[2][3]
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