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Cytochrome P450 168A1 from Pseudomonas aeruginosa is involved in the hydroxylation of biologically relevant fatty acids
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Andrew Warrilow ,
Nicola Rolley,
Josie Parker,
Vera Thoss,
Diane Kelly,
Nicolae Corcionivoschi ,
Steven Kelly
PLOS ONE, Volume: 17, Issue: 3, Start page: e0265227
Swansea University Authors:
Claire Price , Andrew Warrilow , Nicola Rolley, Josie Parker, Diane Kelly, Steven Kelly
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DOI (Published version): 10.1371/journal.pone.0265227
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...
| Published in: | PLOS ONE |
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| ISSN: | 1932-6203 |
| Published: |
Public Library of Science (PLoS)
2022
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| Online Access: |
Check full text
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| URI: | https://cronfa.swan.ac.uk/Record/cronfa59697 |
| 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. |
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| College: |
Faculty of Medicine, Health and Life Sciences |
| 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 |