Discovery and Characterization of a Baeyer‐Villiger Monooxygenase Using Sequence Similarity Network Analysis

Baeyer‐Villiger monooxygenases (BVMOs) are important flavin‐dependent enzymes which perform oxygen insertion reactions leading to valuable products. As reported in many studies, BVMOs are usually unstable during application, preventing a wider usage in biocatalysis. Here, we discovered a novel NADPH...

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Bibliographic Details
Published in:Chembiochem : a European journal of chemical biology 2023-05, Vol.24 (10), p.e202200746-n/a
Main Authors: Sakoleva, Thaleia, Austin, Harry P., Tzima, Chrysoula, Dörr, Mark, Bornscheuer, Uwe T.
Format: Article
Language:English
Subjects:
Aliphatic compounds
aliphatic ketones
Alkanes
Baeyer-Villiger monooxygenase
Biocatalysis
Catalysis
Flavin
Ketones
Ketones - chemistry
Mixed Function Oxygenases - chemistry
Network analysis
Oxidation-Reduction
Similarity
Substrate Specificity
Substrates
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Summary:Baeyer‐Villiger monooxygenases (BVMOs) are important flavin‐dependent enzymes which perform oxygen insertion reactions leading to valuable products. As reported in many studies, BVMOs are usually unstable during application, preventing a wider usage in biocatalysis. Here, we discovered a novel NADPH‐dependent BVMO which originates from Halopolyspora algeriensis using sequence similarity networks (SSNs). The enzyme is stable at temperatures between 10 °C to 30 °C up to five days after the purification, and yields the normal ester product. In this study, the substrate scope was investigated for a broad range of aliphatic ketones and the enzyme was biochemically characterized to identify optimum reaction conditions. The best substrate (86 % conversion) was 2‐dodecanone using purified enzyme. This novel BVMO could potentially be applied as part of an enzymatic cascade or in bioprocesses which utilize aliphatic alkanes as feedstock. We discovered a Baeyer‐Villiger monooxygenase from Halopolyspora algeriensis (BVMOHalo) derived from a marine metagenome dataset using a sequence similarity network analysis. The enzyme was recombinantly expressed in E. coli and biochemically characterized. It converts a range of aliphatic ketones and 2‐chlorophenylacetone into the corresponding esters with high conversions of up to 86 %.
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.202200746