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

Price, Claire L., Warrilow, Andrew G.S., Rolley, Nicola J, Parker, Josie, Thoss, Vera, Kelly, Diane E, Corcionivoschi, Nicolae and Kelly, Steven L 2022. Cytochrome P450 168A1 from pseudomonas aeruginosa is involved in the hydroxylation of biologically relevant fatty acids. PLoS ONE 17 (3) , pp. 1-20. 10.1371/journal.pone.0265227

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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.

Item Type:	Article
Date Type:	Published Online
Status:	Published
Schools:	Schools > Biosciences
Publisher:	Public Library of Science
ISSN:	1932-6203
Date of First Compliant Deposit:	12 October 2022
Date of Acceptance:	24 February 2022
Last Modified:	04 Jun 2023 11:03
URI:	https://orca.cardiff.ac.uk/id/eprint/153112

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