Polycyclic Ketone Monooxygenase from the Thermophilic Fungus Thermothelomyces thermophila: A Structurally Distinct Biocatalyst for Bulky Substrates

Maximilian J L J Fürst, Simone Savino, Hanna M Dudek, J Rúben Gómez Castellanos, Cora Gutiérrez de Souza, Stefano Rovida, Marco W Fraaije, Andrea Mattevi

Research output: Contribution to journalArticleAcademicpeer-review

37 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)627-630
Number of pages4
JournalJournal of the American Chemical Society
Volume139
Issue number2
DOIs
Publication statusPublished - 3-Jan-2017

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