6M1W
Structure of the 2-Aminoisobutyric acid Monooxygenase Hydroxylase
Summary for 6M1W
Entry DOI | 10.2210/pdb6m1w/pdb |
Descriptor | Amidohydrolase, ZINC ION, GLYCEROL, ... (8 entities in total) |
Functional Keywords | monooxygenase, hydroxylase, oxidoreductase |
Biological source | Rhodococcus wratislaviensis More |
Total number of polymer chains | 2 |
Total formula weight | 84537.79 |
Authors | Hibi, M.,Mikami, B.,Ogawa, J. (deposition date: 2020-02-26, release date: 2021-01-06, Last modification date: 2021-01-27) |
Primary citation | Hibi, M.,Fukuda, D.,Kenchu, C.,Nojiri, M.,Hara, R.,Takeuchi, M.,Aburaya, S.,Aoki, W.,Mizutani, K.,Yasohara, Y.,Ueda, M.,Mikami, B.,Takahashi, S.,Ogawa, J. A three-component monooxygenase from Rhodococcus wratislaviensis may expand industrial applications of bacterial enzymes. Commun Biol, 4:16-16, 2021 Cited by PubMed 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. PubMed: 33398074DOI: 10.1038/s42003-020-01555-3 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.75 Å) |
Structure validation
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