1. A three-component monooxygenase from Rhodococcus wratislaviensis may expand industrial applications of bacterial enzymes.
- Author
-
Hibi, Makoto, Fukuda, Dai, Kenchu, Chihiro, Nojiri, Masutoshi, Hara, Ryotaro, Takeuchi, Michiki, Aburaya, Shunsuke, Aoki, Wataru, Mizutani, Kimihiko, Yasohara, Yoshihiko, Ueda, Mitsuyoshi, Mikami, Bunzo, Takahashi, Satomi, and Ogawa, Jun
- Subjects
- *
RHODOCOCCUS , *MONOOXYGENASES , *BACTERIAL enzymes , *HYDROXYLATION , *CHEMICAL reactions , *PROTEOMICS - Abstract
The high-valent iron-oxo species formed in the non-heme diiron enzymes have high oxidative reactivity and catalyze difficult chemical reactions. Although the hydroxylation of inert methyl groups is an industrially promising reaction, utilizing non-heme diiron enzymes as such a biocatalyst has been difficult. Here we show a three-component monooxygenase system for the selective terminal hydroxylation of α-aminoisobutyric acid (Aib) into α-methyl-D-serine. It consists of the hydroxylase component, AibH1H2, and the electron transfer component. Aib hydroxylation is the initial step of Aib catabolism in Rhodococcus wratislaviensis C31-06, which has been fully elucidated through a proteome analysis. The crystal structure analysis revealed that AibH1H2 forms a heterotetramer of two amidohydrolase superfamily proteins, of which AibHm2 is a non-heme diiron protein and functions as a catalytic subunit. The Aib monooxygenase was demonstrated to be a promising biocatalyst that is suitable for bioprocesses in which the inert C–H bond in methyl groups need to be activated. Makoto Hibi et al. report a novel three-component monooxygenase system in Rhodococcus wratislaviensis. This enzyme catalyzes the activation of an inert C–H bond and may be potentially important as a biocatalyst for industrial applications. [ABSTRACT FROM AUTHOR]
- Published
- 2021
- Full Text
- View/download PDF