Harnessing the power of enzymatic oxygen activation

Using technology of SSB, mutant libraries will be prepared and transfered to the relevant partners.

Mutants of LPMOs will be prepared and checked for activity.

Identification and functional characterisation of new cofactor-independent oxygenases within the tautomerase superfamily, with special focus on hypothetical oxygenases for which the genomic context gives clues about their physiological function.

The work will focus on eukaryotic flavin-containing monooxygenases that are essential for the detoxification of xenobiotics. The target enzymes will be produced and purified using protein chromatography.

Investigation of three heme-dependent monooxygenases for the conversion of heterocyclic compounds. Through modelling and random mutagenesis positions will be identified and mutated to elucidate on the molecular level structure-function relationships.

In-depth mechanistic and structural studies of a cofactor-independent monooxygenase from the tautomerase superfamily that catalyses the oxidative cleavage of HPP.

Generate knowledge-based focussed enzyme mutant libraries

Isolation of new cofactor-independent dioxygenases from the alpha/beta hydrolase fold superfamily active toward the Pseudomonas quinolone signal (PQS), exploiting natural genetic diversity; and functional characterisation of PQS-cleaving enzymes, with a focus on substrate specificity and affinity, catalytic efficiency, and applicability to interfere with quorum sensing.

For identifying ESR candidates, OXYTRAIN vacancies advertised.

An OXYTRAIN website will be built and launched

Published in: ISSN 1867-3880
DOI: 10.1002/cctc.201801829

Author(s): Nikola Lončar, Filippo Fiorentini, Gautier Bailleul, Simone Savino, Elvira Romero, Andrea Mattevi, Marco W. Fraaije
Published in: Applied Microbiology and Biotechnology, Issue 103/4, 2019, Page(s) 1755-1764, ISSN 0175-7598
DOI: 10.1007/s00253-018-09579-w