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Chemija / Chemistry

ISSN 0235-7216
ISSN 2424-4538 (online)

2016 m. Nr. 1

Characterization of 1,8-cineole degradation encoding operon from Rhodococcus sp. TMP1
Jevgenija JAKUBOVSKA, Rolandas MEŠKYS

Recently isolated bacterial strain Rhodococcus jostii TMP1 proved to be capable of utilizing 1,8-cineole as its sole source of carbon and energy. Bioinformatic analysis of R. jostii TMP1 genome revealed a presence of a novel and more detailed Cin operon – CinTMP1. It was found that CinTMP1 operon contains genes which are known to be involved in biodegradation of 1,8-cineole by Citrobacter braakii. The genes located in this operon – cinA1, cinB1, cinC1, cinD1 and cinBVMO – were proposed to encode putative cytochrome P450 (P450cin), cindoxin reductase, cindoxin, hydroxycineole dehydrogenase and Baeyer-Villiger monooxygenase, respectively. The expression of all recombinant enzymes, except for cindoxin reductase, as well as the coexpression of P450cin system, has been studied and optimized. Recombinant P450cin enzyme of R. jostii TMP1 catalyses the initial monooxygenation of 1,8-cineole, yielding 6-hydroxycineole. Furthemore, P450cin performs a subsequent alcohol oxidation to produce 6-ketocineole in Rhodococcus cells.

: Keywords: 1,8-cineole, Rhodococcus, cytochrome P450, cindoxin reductase, cindoxin, hydroxycineole dehydrogenase, Baeyer-Villiger monooxygenase

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