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Trends Biotechnol. 2021 Nov;39(11):1184-1207. doi: 10.1016/j.tibtech.2021.01.011. Epub 2021 Feb 18.

Self-Sufficient Class VII Cytochromes P450: From Full-Length Structure to Synthetic Biology Applications.

Trends in biotechnology

Danilo Correddu, Giovanna Di Nardo, Gianfranco Gilardi

Affiliations

  1. Department of Life Sciences and Systems Biology, University of Torino, Via Accademia Albertina 13, 10123, Torino, Italy.
  2. Department of Life Sciences and Systems Biology, University of Torino, Via Accademia Albertina 13, 10123, Torino, Italy. Electronic address: [email protected].

PMID: 33610332 DOI: 10.1016/j.tibtech.2021.01.011

Abstract

Members of class VII cytochromes P450 are catalytically self-sufficient enzymes containing a phthalate dioxygenase reductase-like domain fused to the P450 catalytic domain. Among these, CYP116B46 is the first enzyme for which the 3D structure of the whole polypeptide chain has been solved, shedding light on the interaction between its domains, which is crucial for catalysis. Most of these enzymes have been isolated from extremophiles or detoxifying bacteria that can carry out regio- and enantioselective oxidation of compounds of biotechnological interest. Protein engineering has generated mutants that can perform challenging organic reactions such as the anti-Markovnikov alkene oxidation. This potential, combined with the detailed 3D structure, forms the basis for further directed evolution studies aimed at widening their biotechnological exploitation.

Copyright © 2021 Elsevier Ltd. All rights reserved.

Keywords: CYP116; biocatalysis; cytochromes P450; fine chemicals; self-sufficient enzyme; synthetic biology

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