Journal
JOURNAL OF BACTERIOLOGY
Volume 185, Issue 2, Pages 399-404Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.185.2.399-404.2003
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Funding
- NIAID NIH HHS [R01 AI047818, R56 AI047818, AI47818] Funding Source: Medline
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R56AI047818, R01AI047818] Funding Source: NIH RePORTER
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The novel benzoyl coenzyme A (benzoyl-CoA) biosynthesis pathway in Streptomyces maritimus was investigated through a series of target-directed mutations. Genes involved in benzoyl-CoA formation were disrupted through single-crossover homologous recombination, and the resulting mutants were analyzed for their ability to biosynthesize the benzoyl-CoA-primed polyketide antibiotic enterocin. Inactivation of the unique phenylalanine ammonia-lyase-encoding gene encP was previously shown to be absolutely required for benzoyl-CoA formation in S. maritimus. The fatty acid P-oxidation-related genes encH, -I, and -J, on the other hand, are necessary but not required. In each case, the yield of benzoyl-CoA-primed enterocin dropped below wild-type levels. We attribute the reduced benzoyl-CoA formation in these specific mutants to functional substitution and cross-talk between the products of genes encH, -I, and -J and the enzyme homologues of primary metabolism. Disruption of the benzoate-CoA ligase encN gene did not perturb enterocin production, however, demonstrating that encN is extraneous and that benzoic acid is not a pathway intermediate. EncN rather serves as a substitute pathway for utilizing exogenous benzoic acid. These experiments provide further support that benzoyl-CoA is formed in a novel bacterial pathway that resembles the eukaryotic assembly of benzoyl-CoA from phenylalanine via a beta-oxidative path.
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