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Acinetobacter sp. strain ADP1 can use benzoate or anthranilate as a sole carbon source. These structurally similar compounds are independently converted to catechol, allowing further degradation to proceed via the β-ketoadipate pathway. In this study, the first step in anthranilate catabolism was characterized. A mutant unable to grow on anthranilate, ACN26, was selected. The sequence of a wild-type DNA fragment that restored growth revealed theantABC genes, encoding 54-, 19-, and 39-kDa proteins, respectively. The deduced AntABC sequences were homologous to those of class IB multicomponent aromatic ring-dihydroxylating enzymes, including the dioxygenase that initiates benzoate catabolism. Expression ofantABC inEscherichia coli , a bacterium that normally does not degrade anthranilate, enabled the conversion of anthranilate to catechol. Unlike benzoate dioxygenase (BenABC), anthranilate dioxygenase (AntABC) catalyzed catechol formation without requiring a dehydrogenase. InAcinetobacter mutants,benC substituted forantC during growth on anthranilate, suggesting relatively broad substrate specificity of the BenC reductase, which transfers electrons from NADH to the terminal oxygenase. In contrast, thebenAB genes did not substitute forantAB . AnantA point mutation in ACN26 prevented anthranilate degradation, and this mutation was independent of amucK mutation in the same strain that prevented exogenous muconate degradation. Anthranilate induced expression ofantA , although no associated transcriptional regulators were identified. Disruption of three open reading frames in the immediate vicinity ofantABC did not prevent the use of anthranilate as a sole carbon source. TheantABC genes were mapped on the ADP1 chromosome and were not linked to the two known supraoperonic gene clusters involved in aromatic compound degradation.

journal of bacteriology

Similarities between the antABC -Encoded Anthranilate Dioxygenase and the benABC -Encoded Benzoate Dioxygenase of Acinetobacter sp. Strain ADP1