1887

Abstract

Bacteria in anoxic environments typically convert aromatic compounds derived from pollutants or green plants to benzoyl-CoA, and then to the C dicarboxylic acid derivative 3-hydroxypimelyl-CoA. Inspection of the recently completed genome sequence of the purple nonsulfur phototroph revealed one predicted cluster of genes for the -oxidation of dicarboxylic acids. These genes, annotated as , are predicted to encode acyl-CoA ligase, enoyl-CoA hydratase, acyl-CoA dehydrogenase and acyl-CoA transferase enzymes, which should allow the conversion of odd-chain dicarboxylic acids to glutaryl-CoA, and even-chain dicarboxylic acids to succinyl-CoA. A mutant strain that was deleted in the gene cluster grew at about half the rate of the wild-type parent when benzoate or pimelate was supplied as the sole carbon source. The mutant grew five times more slowly than the wild-type on the C dicarboxylic acid tetradecanedioate. The mutant was unimpaired in growth on the C-fatty acid caprylate. The acyl-CoA ligase predicted to be encoded by the gene was purified, and found to be active with CC dicarboxylic and fatty acids. The expression of a chromosomal gene fusion increased twofold when cells were grown in the presence of straight-chain CC dicarboxylic and fatty acids. These results suggest that the -oxidation enzymes encoded by the gene cluster are active with medium-chain-length dicarboxylic acids, including pimelate. However, the finding that the operon deletion mutant is still able to grow on dicarboxylic acids, albeit at a slower rate, indicates that has additional genes that can also specify the degradation of these compounds.

Keyword(s): Km, kanamycin
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2005-03-01
2020-10-29
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