| Title | Characterization of β-Ketoadipate Pathway from Multi-Drug Resistance Bacterium, Acinetobacter baumannii DU202 by Proteomic Approach |
|---|---|
| Author | Sonn-Ho Park1, Jae-Woo Kim2, Sung-Ho Yun1, Sun Hee Leem3, Hyung-Yeel Kahng4, and Seung Il Kim1* |
| Address | 1Proteomics Team, Korea Basic Science Institute, Daejeon 305-333, Republic of Korea, 2Department of Laboratory Medicine, Dong-A University Medical Center, Busan 602-715, Republic of Korea, 3Department of Biology, Dong-A University, Busan 604-714, Republic of Korea, 4Department of Environmental Education, Sunchon National University, Sunchon 540-742, Republic of Korea |
| Bibliography | Journal of Microbiology, 44(6),632-640, 2006, |
| DOI | |
| Key Words | β-Ketoadipate Pathway, Aromatic compound biodegradation, MDR Acinetobacter baumannii |
| Abstract | In this study, the biodegradative activities of monocyclic aromatic compounds were determined from the multi-drug resistant (MDR) Acinetobacter baumannii, which were studied in the form of clinical isolates from a hospital in Korea. These bacteria were capable of biodegrading monocyclic aromatic compounds, such as benzoate and p-hydroxybenzoate. In order to determine which pathways are available for biodegradation in these stains, we conducted proteome analyses of benzoate and p-hydroxybenzoate-cultured A. baumannii DU202, using 2-DE/MS analysis. As genome DB of A. baumannii was not yet available, MS/MS analysis or de novo sequencing methods were employed in the identification of induced proteins. Benzoate branch enzymes [catechol 1,2-dioxygenase (CatA) and benzoate dioxygenase α subunit (BenA)] of the β-ketoadipate pathway were identified under benzoate culture condition and p-hydroxybenzoate branch enzymes [protocatechuate 3,4-dioxygenase α subunit (PcaG) and 3-carboxy-cis,cis-muconate cycloisomerase (PcaB)] of the β-ketoadipate pathway were identified under p-hydroxybenzoate culture condition, respectively, thereby suggesting that strain DU202 utilized the β-ketoadipate pathway for the biodegradation of monocyclic aromatic compounds. The sequence analysis of two purified dioxygenases (CatA and PcaGH) indicated that CatA is closely associated with the CatA of Acinetobacter radiresistance, but PcaGH is only moderately associated with the PcaGH of Acinetobacter sp. ADP1. Interestingly, the fused form of PcaD and PcaC, carboxymuconolactone decarboxylase (PcaCD), was detected on benzoate-cultured A. baumannii DU202. These results indicate that A. baumannii DU202 exploits a different β-ketoadipate pathway from other Acinetobacter species. |
| Download PDF | JM44(6)-07.pdf |