Differential degradation of bicyclics with aromatic and alicyclic rings by Rhodococcus sp. strain DK17
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- Differential degradation of bicyclics with aromatic and alicyclic rings by Rhodococcus sp. strain DK17
- Other Titles
- Rhodococcus sp. strain DK17에 의한 bicyclic rings의 분해에 필수적 hydroxylation 반응
- Kang, Beom Sik
Hong, Soon Gyu
Zylstra, Gerben J.
Ki Young Choi
Kim, Tai Kyoung
- Biotechnology & Applied Microbiology; Microbiology
- 2-dihydronaphthalene; Rhodococcus; degradative pathway; indene; tetralin
- Issue Date
- American Society for Microbiology
- Kang, Beom Sik, et al. 2011. "Differential degradation of bicyclics with aromatic and alicyclic rings by Rhodococcus sp. strain DK17". Applied and Environmental Microbiology, 77(23): 8280-8287.
- The metabolically versatile Rhodococcus sp. strain DK17 is able to grow on tetralin and indan but cannot use their respective desaturated counterparts, 1,2-dihydronaphthalene and indene, as sole carbon and energy sources. Metabolite analyses by gas chromatography-mass spectrometry and nuclear magnetic resonance spectrometry clearly show that (1) the meta-cleavage dioxygenase mutant strain DK180 accumulates 5,6,7,8-tetrahydro-1,2-naphthalene diol, 1,2-indene diol, and 3,4-dihydro-naphthalene-1,2-diol from tetralin, indene, and 1,2-dihydronaphthalene, respectively and (2) when expressed in E. coli, the DK17 o-xylene dioxygenase transforms tetralin, indene, and 1,2-dihydronaphthalene into tetralin cis-dihydrodiol, indan-1,2-diol, and cis-1,2-dihydroxy-1,2,3,4-tetrahydronaphthalene, respectively. Tetralin, which is activated by aromatic hydroxylation, is degraded successfully via the ring-cleavage pathway to support growth of DK17. Indene and 1,2-dihydronaphthalene do not serve as growth substrates because DK17 hydroxylates them on the alicyclic ring and further metabolism results in a dead-end metabolite. This study reveals that aromatic hydroxylation is a prerequisite for proper degradation of bicyclics with aromatic and alicyclic rings by DK17, and confirms the unique ability of the DK17 o-xylene dioxygenase to perform distinct regioselective hydroxylations.
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