Characterization and Crystal Structure of a Robust Cyclohexanone Monooxygenase

Cyclohexanone monooxygenase (CHMO) is a promising biocatalyst for industrial reactions owing to its broad substrate spectrum and excellent regio‐, chemo‐, and enantioselectivity. However, the low stability of many Baeyer–Villiger monooxygenases is an obstacle for their exploitation in industry. Char...

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Bibliographic Details
Published in:Angewandte Chemie International Edition 2016-12, Vol.55 (51), p.15852-15855
Main Authors: Romero, Elvira, Castellanos, J. Rubén Gómez, Mattevi, Andrea, Fraaije, Marco W.
Format: Article
Language:English
Subjects:
Actinomycetales - chemistry
Actinomycetales - enzymology
Actinomycetales - metabolism
Baeyer-Villiger oxidation
biocatalysis
Communication
Communications
Crystal structure
Crystallography, X-Ray
cyclohexanone monooxygenase
Cyclohexanones - metabolism
Enzyme Stability
Enzymes
Ketones - metabolism
Models, Molecular
Oxygenases - chemistry
Oxygenases - metabolism
Protein Conformation
Stereoisomerism
Substrate Specificity
Sulfides - metabolism
ϵ-caprolactone
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Summary:Cyclohexanone monooxygenase (CHMO) is a promising biocatalyst for industrial reactions owing to its broad substrate spectrum and excellent regio‐, chemo‐, and enantioselectivity. However, the low stability of many Baeyer–Villiger monooxygenases is an obstacle for their exploitation in industry. Characterization and crystal structure determination of a robust CHMO from Thermocrispum municipale is reported. The enzyme efficiently converts a variety of aliphatic, aromatic, and cyclic ketones, as well as prochiral sulfides. A compact substrate‐binding cavity explains its preference for small rather than bulky substrates. Small‐scale conversions with either purified enzyme or whole cells demonstrated the remarkable properties of this newly discovered CHMO. The exceptional solvent tolerance and thermostability make the enzyme very attractive for biotechnology. Looking like a true survivor: The discovery of a robust cyclohexanone monooxygenase (CHMO) that shows great promise as an oxidative biocatalyst is reported. This enzyme (TmCHMO) efficiently converts a variety of aliphatic, aromatic, and cyclic ketones, as well as prochiral sulfides, and was found to be much more thermostable and solvent tolerant than known CHMOs.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201608951