    2.3.1.212 | 4-coumaroyl-CoA + malonyl-CoA + H2O = 2 CoA + 4-hydroxybenzalacetone + 2 CO2 |
the enzyme shows remarkable substrate tolerance and catalytic versatility, structure-function relationship and functional diversity of type III PKS enzymes, the enzyme catalytic mechanism for the thioester bond cleavage of the enzyme-bound diketide intermediate and the decarboxylation reaction to produce benzalacetone involves Cys164, His33, and Asn336, overview. RpBAS initially accepts the aminoacyl-CoA as a starter, and then recruits malonyl-CoA for a Claisen condensation to generate the gamma-amino-beta-ketothioester. The free gamma-amino group of the enzyme-bound intermediate can cleave the thioester bond, with concomitant intramolecular lactamization |
722314 |
