Structural highlights
Function
G2QA95_THET4
Publication Abstract from PubMed
Regio- and stereoselective Baeyer-Villiger oxidations are difficult to achieve by classical chemical means, particularly when large, functionalized molecules are to be converted. Biocatalysis using flavin-containing Baeyer-Villiger monooxygenases (BVMOs) is a well-established tool to address these challenges, but known BVMOs have shortcomings in either stability or substrate selectivity. We characterized a novel BVMO from the thermophilic fungus Thermothelomyces thermophila, determined its three-dimensional structure, and demonstrated its use as a promising biocatalyst. This fungal enzyme displays excellent enantioselectivity, acts on various ketones, and is particularly active on polycyclic molecules. Most notably we observed that the enzyme can perform oxidations on both the A and D ring when converting steroids. These functional properties can be linked to unique structural features, which identify enzymes acting on bulky substrates as a distinct subgroup of the BVMO class.
Polycyclic Ketone Monooxygenase from the Thermophilic Fungus Thermothelomyces thermophila: A Structurally Distinct Biocatalyst for Bulky Substrates.,Furst MJ, Savino S, Dudek HM, Gomez Castellanos JR, Gutierrez de Souza C, Rovida S, Fraaije MW, Mattevi A J Am Chem Soc. 2017 Jan 3. doi: 10.1021/jacs.6b12246. PMID:28010060[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Furst MJ, Savino S, Dudek HM, Gomez Castellanos JR, Gutierrez de Souza C, Rovida S, Fraaije MW, Mattevi A. Polycyclic Ketone Monooxygenase from the Thermophilic Fungus Thermothelomyces thermophila: A Structurally Distinct Biocatalyst for Bulky Substrates. J Am Chem Soc. 2017 Jan 3. doi: 10.1021/jacs.6b12246. PMID:28010060 doi:https://dx.doi.org/10.1021/jacs.6b12246
