Antimycins are produced as secondary metabolites by Streptomyces bacteria, a soil bacteria. These specialized metabolites likely function to kill neighboring organisms in order to provide the streptomyces bacteria with a competitive edge.
Chemical structures
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Biosynthesis
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Antimycins are produced by a non-ribosomal peptide synthetase (NRPS)/polyketide synthase (PKS) assembly complex which acts as an assembly line for antimycin production. The assembly is genetically coded for by the ant gene family. The assembly requires 14 proteins, AntBCDEFGHIJKLMNO, which shuttle the intermediates along the assembly line through a series of transesterifications, keto reductions, thiolations (addition of a sulfur containing group), condensations, and adenylations. The last two steps involving AntB and AntO are tailoring steps. The following steps describe chemically what the Ant Enzymes do in order to synthesize Antimycin. Synthesis begins with tryptophan, an amino acid.
1. The indole ring of tryptophan, an amino acid, is opened by a pathway-specific tryptophan-2.3-dioxygnease, AntN, to make N-formyl-L-kynurenine.
2. N-formyl-L-kynurenine is converted to anthranilate by the pathway-specific kynureninase, AntP.