Journal
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
Volume 97, Issue 13, Pages 6031-6041Publisher
SPRINGER
DOI: 10.1007/s00253-012-4402-8
Keywords
Comamonas testosteroni; Protocatechuate 4,5-cleavage; Vanillate; 3-/4-Hydroxybenzoate; 4-Oxalomesaconate tautomerase
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Funding
- National Natural Science Foundation of China [31230003]
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Comamonas testosteroni strain CNB-1 was isolated from activated sludge and has been investigated for its ability to degrade 4-chloronitrobenzene. Results from this study showed that strain CNB-1 grew on phenol, gentisate, vanillate, 3-hydroxybenzoate (3HB), and 4-hydroxybenzoate (4HB) as carbon and energy sources. Proteomic data and enzyme activity assays suggested that vanillate, 3HB, and 4HB were degraded in strain CNB-1 via protocatechuate (PCA) 4,5-cleavage pathway. The genetics and biochemistry of the PCA 4,5-cleavage pathway were investigated. Results showed that the 4-oxalomesaconate (OMA) hydratase from C. testosteroni takes only enol-OMA as substrate. A previously functionally unknown gene pmdU encodes an OMA tautomerase and catalyzes conversion of OMA(keto) into OMA(enol). The 4-carboxy-4-hydroxy-2-oxoadipate (CHA) aldolase is encoded by pmdF and catalyzes the last step of the PCA 4,5-cleavage pathway. We explored the 1,183 microbial genomes at GenBank for potential PCA 4,5-cleavage pathways, and 33 putative pmd clusters were found. Results suggest that PCA 4,5-cleavage pathways are mainly distributed in alpha- and beta-Proteobacteria.
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