Heterologous Expression of Mycobacterium Alkene Monooxygenases in Gram-Positive and Gram-Negative Bacterial Hosts.

ABSTRACT: Alkene monooxygenases (MOs) are soluble di-iron-containing enzymes found in bacteria that grow on alkenes. Here, we report improved heterologous expression systems for the propene MO (PmoABCD) and ethene MO (EtnABCD) from Mycobacterium chubuense strain NBB4. Strong functional expression of PmoABCD and EtnABCD was achieved in Mycobacterium smegmatis mc²155, yielding epoxidation activities (62 and 27 nmol/min/mg protein, respectively) higher than any reported to date for heterologous expression of a di-iron MO system. Both PmoABCD and EtnABCD were specialized for the oxidation of gaseous alkenes (C₂ to C₄), and their activity was much lower on liquid alkenes (C₅ to C₈). Despite intensive efforts to express the complete EtnA

SUBMITTER: McCarl V 

PROVIDER: S-EPMC6052275 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature