1887

Abstract

The gene coding for the oxygenase component, , of 4-aminobenzenesulfonate (4-ABS) 3,4-dioxygenase in sp. PBC was previously identified via transposon mutagenesis. Expression of wild-type restored the ability of the mutant to grow on 4-ABS. The inclusion of and , coding for a putative glutamine-synthetase-like protein and a plant-type ferredoxin, respectively, further improved the efficiency of 4-ABS degradation. Transcription analysis using the promoter probe plasmid showed that was expressed during growth on 4-ABS and 4-sulfocatechol. Heterologous expression of in led to the biotransformation of 4-ABS to a metabolite which shared a similar retention time and UV/vis profile with 4-sulfocatechol. The putative reductase gene was isolated via degenerate PCR and expression of and in led to maximal 4-ABS biotransformation. In , the deletion of completely eliminated dioxygenase activity while the deletion of or led to a decrease in dioxygenase activity. Phylogenetic analysis of SadB showed that it is closely related to the glutamine-synthetase-like proteins involved in the aniline degradation pathway. This is the first discovery, to our knowledge, of the functional genetic components for 4-ABS aromatic ring hydroxylation in the bacterial domain.

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2012-08-01
2024-04-23
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