Identification and functional analysis of genes required for desulfurization of alkyl dibenzothiophenes of Mycobacterium sp. G3 |
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Authors: | Nomura Nobuhiko Takada Masaki Okada Hideki Shinohara Yuko Nakajima-Kambe Toshiaki Nakahara Tadaatsu Uchiyama Hiroo |
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Affiliation: | Graduate School of Life and Environmental Science, University of Tsukuba, 1-1-1 Tennoudai, Tsukuba City, Ibaraki 305-8572, Japan. nomunobu@sakura.cc.tsukuba.ac.jp |
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Abstract: | Mycobacterium sp. G3 was reported as a dibenzothiophene (DBT)-degrading microorganism and the first strain to have the ability to degrade high-molecular-weight alkyl DBTs, such as 4,6-dibutyl DBT and 4,6-dipentyl DBT, by the C-S bond cleavage pathway. Three genes (mdsA, mdsB, and mdsC) for desulfurization, which form a cluster, were cloned from Mycobacterium sp. G3. The expression of each gene in Escherichia coli JM109 showed that MdsC oxidized DBT to DBT sulfone, MdsA transformed DBT sulfone into 2-(2'-hydroxyphenyl)benzene sulfinate (HPBS), and MdsB desulfinated HPBS into 2-hydroxybiphenyl (HBP), indicating that the gene products of mdsABC are functional in the recombinant. MdsC oxidized 4,6-dimethyl DBT, 4,6-diethyl DBT, 4,6-dipropyl DBT and 4,6-dibutyl DBT to each sulfone form, suggesting that MdsC covers a broad specificity for alkyl DBTs. |
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Keywords: | monooxygenase dibenzothiophene alkyl dibenzothiophene desulfurization desulfinase |
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