6M2I

Structure of the 2-Aminoisobutyric acid Monooxygenase Hydroxylase

Summary for 6M2I

• Entry DOI: 10.2210/pdb6m2i/pdb
• Descriptor: Amidohydrolase, ZINC ION, SULFATE ION, ... (7 entities in total)
• Functional Keywords: monooxygenase, hydroxylase, oxidoreductase
• Biological source: Rhodococcus wratislaviensis; More
• Total number of polymer chains: 2
• Total formula weight: 87787.86

Authors

Hibi, M.,Mikami, B.,Ogawa, J. (deposition date: 2020-02-27, release date: 2021-01-06, Last modification date: 2024-11-13)

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

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: 33398074
DOI: 10.1038/s42003-020-01555-3

Experimental method

X-RAY DIFFRACTION (2.45 Å)