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Results 1 - 4 of 4
EC Number Reaction Commentary Reference
Show all pathways known for 2.3.1.221Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.2217 malonyl-CoA + hexanoyl-[acyl-carrier protein] = 7 CoA + norsolorinic acid anthrone + [acyl-carrier protein] + 7 CO2 + 2 H2O - -
Show all pathways known for 2.3.1.221Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.2217 malonyl-CoA + hexanoyl-[acyl-carrier protein] = 7 CoA + norsolorinic acid anthrone + [acyl-carrier protein] + 7 CO2 + 2 H2O a product template domain unites with the ketosynthase and thioesterase in this IPKS system to assemble precisely seven malonyl-derived building blocks to a hexanoyl starter unit and mediate a specific cyclization cascade. These mechanistic features are general for IPKS-catalyzed production of aromatic polyketides 721052
Show all pathways known for 2.3.1.221Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.2217 malonyl-CoA + hexanoyl-[acyl-carrier protein] = 7 CoA + norsolorinic acid anthrone + [acyl-carrier protein] + 7 CO2 + 2 H2O mechanism of thioesterase/Claisen cyclase-catalyzed chain-termination of fungal aromatic polyketide biosynthesis. The ACP of the ACP-bound substrate is displaced upon thioesterase-catalyzed transesterification. Rotation of the substrate side chain can occur once the ACP leaves the pocket, and the thioesterase can then close. Thioesterase conformational constraints as observed in the closed-form crystal structure guide Claisen-type cyclization to release noranthrone, i.e. norsolorinic acid anthrone, the polyketide precursor of aflatoxin B1. Domain structure and reaction mechanism, detailed overview 723638
Show all pathways known for 2.3.1.221Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.2217 malonyl-CoA + hexanoyl-[acyl-carrier protein] = 7 CoA + norsolorinic acid anthrone + [acyl-carrier protein] + 7 CO2 + 2 H2O reaction mechanism, overview. The SAT domain in PksA selects a hexanoyl starter unit. The MAT domain loads the free ACP with malonyl units. After seven successive condensation events with malonyl-ACP catalysed in te ketoacyl synthase domain, the linear ACP-bound polyketide is cyclized (C4-C9 and C2-C11 cyclization events) and aromatized in the product template domain to give the bicyclic intermediate. The thioesterase domain catalyses C-C cyclization to release anthrone, which undergoes oxidation to the anthraquinone norsolorinic acid, to initiate the complex biosynthetic pathway to aflatoxin B1 723262
Results 1 - 4 of 4