ArticleCurrent microbiology2008
Genes involved in the benzoate catabolic pathway in Acinetobacter calcoaceticus PHEA-2.
Article in Current microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 15 citations in OpenAlex.
- Metagenomic analysis of water column samples collected from Green Canyon 233 prior to the Deepwater Horizon incident.Applied and environmental microbiology · 2026Article
- Article
- Identification of genes and pathways related to phenol degradation in metagenomic libraries from petroleum refinery wastewater.PloS one · 2013Article
- Defining bacterial species in the genomic era: insights from the genus Acinetobacter.BMC microbiology · 2012Article
- Genome sequence of Acinetobacter calcoaceticus PHEA-2, isolated from industry wastewater.Journal of bacteriology · 2011Article
- Article
- Benzoate catabolite repression of the phenol degradation in Acinetobacter calcoaceticus PHEA-2.Current microbiology · 2009Article
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Authors and funding
11 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A putative benM gene encoding a LysR-type regulator located upstream from the benA gene was found in Acinetobacter calcoaceticus PHEA-2. Disruption of benM or benA destroyed the ability of PHEA-2 to utilize benzoate. The benM mutant was used to construct a genomic library for isolation of the complete gene cluster responsible for benzoate degradation. Sequence analysis showed that the cluster has three putative operons: benM, benABCDE, and benKP. Unlike many well-characterized benzoate-degrading bacteria, muconate is unable to induce in vivo transcription of the PHEA-2 ben cluster. Reverse transcriptase-polymerase chain reaction (RT-PCR) results showed that the benABCDE operon is activated by the BenM protein in the presence of benzoate. Moreover, a gel-retardation assay demonstrated that BenM binds to the promotor region of the benA gene. The activities of catechol 1,2-dioxygenase (C12O) and catechol 2,3-dioxygenase (C23O) showed that PHEA-2 converted benzoate to catechol for further degradation, possibly via an ortho-cleavage pathway.
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