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2.3.1.240
malonyl-CoA + 6 (2S)-methylmalonyl-CoA + 5 NADPH + 5 H+ = narbonolide + 7 CoA + 7 CO2 + 5 NADP+ + 2 H2O
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2.3.1.240
malonyl-CoA + 6 (2S)-methylmalonyl-CoA + 5 NADPH + 5 H+ = narbonolide + 7 CoA + 7 CO2 + 5 NADP+ + 2 H2O
electron cryo-microscopy (cryo-EM) structures of a full-length polyketide synthase module in three key biochemical states of its catalytic cycle reveals the dynamics of the intramodule acyl carrier protein for sequential binding to catalytic domains within the reaction chamber, and for transferring the elongated and processed polyketide substrate to the next module in the polyketide synthase pathway. During the enzymatic cycle the ketoreductase domain undergoes dramatic conformational rearrangements that enable optimal positioning for reductive processing of the acyl carrier protein-bound polyketide chain elongation intermediate
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