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Information on EC - tetracycline polyketide synthase

for references in articles please use BRENDA:EC2.3.1.260
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IUBMB Comments
The synthesis, in the bacterium Streptomyces rimosus, of the tetracycline antibiotics core skeleton requires a minimal polyketide synthase (PKS) consisting of a ketosynthase (KS), a chain length factor (CLF), and an acyl-carrier protein (ACP). Initiation involves an amide-containing starter unit that becomes the C-2 amide that is present in the tetracycline compounds. Following the initiation, the PKS catalyses the iterative condensation of 8 malonyl-CoA molecules to yield the polyketide backbone of tetracycline. Throughout the proccess, the nascent chain is attached to the OxyC acyl-carrier protein.
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The enzyme appears in viruses and cellular organisms
minimal pks, type ii pks, type ii minimal polyketide synthase, oxytetracycline polyketide synthase, more
malonamoyl-[OxyC acyl-carrier protein] + 8 malonyl-CoA = 18-carbamoyl-3,5,7,9,11,13,15,17-octaoxooctadecanoyl-[OxyC acyl-carrier protein] + 8 CO2 + 8 CoA
show the reaction diagram
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