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Cytochrome P450 168A1 from Pseudomonas aeruginosa is involved in the hydroxylation of biologically relevant fatty acids

Claire Price Orcid Logo, Andrew Warrilow, Nicola Rolley, Josie Parker Orcid Logo, Vera Thoss, Diane Kelly, Nicolae Corcionivoschi Orcid Logo, Steven Kelly Orcid Logo

PLOS ONE, Volume: 17, Issue: 3, Start page: e0265227

Swansea University Authors: Claire Price Orcid Logo, Andrew Warrilow, Nicola Rolley, Josie Parker Orcid Logo, Diane Kelly, Steven Kelly Orcid Logo

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Abstract

The cytochrome P450 CYP168A1 from Pseudomonas aeruginosa was cloned and expressed in Escherichia coli followed by purification and characterization of function. CYP168A1 is a fatty acid hydroxylase that hydroxylates saturated fatty acids, including myristic (0.30 min-1), palmitic (1.61 min-1) and st...

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Published in: PLOS ONE
ISSN: 1932-6203
Published: Public Library of Science (PLoS) 2022
Online Access: Check full text

URI: https://cronfa.swan.ac.uk/Record/cronfa59697
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Abstract: The cytochrome P450 CYP168A1 from Pseudomonas aeruginosa was cloned and expressed in Escherichia coli followed by purification and characterization of function. CYP168A1 is a fatty acid hydroxylase that hydroxylates saturated fatty acids, including myristic (0.30 min-1), palmitic (1.61 min-1) and stearic acids (1.24 min-1), at both the ω-1- and ω-2-positions. However, CYP168A1 only hydroxylates unsaturated fatty acids, including palmitoleic (0.38 min-1), oleic (1.28 min-1) and linoleic acids (0.35 min-1), at the ω-1-position. CYP168A1 exhibited a catalytic preference for palmitic, oleic and stearic acids as substrates in keeping with the phosphatidylcholine-rich environment deep in the lung that is colonized by P. aeruginosa.
College: Swansea University Medical School
Funders: This work was supported by the European Union European Regional Development Fund (ERDF) via the Wales European Funding Office of the Welsh Government through the BEACON funding initiative
Issue: 3
Start Page: e0265227