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- Title
Cytochrome P450 168A1 from Pseudomonas aeruginosa is involved in the hydroxylation of biologically relevant fatty acids.
- Authors
Price, Claire L.; Warrilow, Andrew G. S.; Rolley, Nicola J.; Parker, Josie E.; Thoss, Vera; Kelly, Diane E.; Corcionivoschi, Nicolae; Kelly, Steven L.
- 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.
- Subjects
CYTOCHROME P-450; SATURATED fatty acids; UNSATURATED fatty acids; PSEUDOMONAS aeruginosa; OLEIC acid; PALMITIC acid; EPOXYEICOSATRIENOIC acids
- Publication
PLoS ONE, 2022, Vol 17, Issue 3, p1
- ISSN
1932-6203
- Publication type
Article
- DOI
10.1371/journal.pone.0265227