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Cytochrome P450 168A1 from Pseudomonas aeruginosa is involved in the hydroxylation of biologically relevant fatty acids
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...
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ISSN: | 1932-6203 |
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2022
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URI: | https://cronfa.swan.ac.uk/Record/cronfa59697 |
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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.</abstract><type>Journal Article</type><journal>PLOS ONE</journal><volume>17</volume><journalNumber>3</journalNumber><paginationStart>e0265227</paginationStart><paginationEnd/><publisher>Public Library of Science (PLoS)</publisher><placeOfPublication/><isbnPrint/><isbnElectronic/><issnPrint/><issnElectronic>1932-6203</issnElectronic><keywords/><publishedDay>21</publishedDay><publishedMonth>3</publishedMonth><publishedYear>2022</publishedYear><publishedDate>2022-03-21</publishedDate><doi>10.1371/journal.pone.0265227</doi><url/><notes/><college>COLLEGE NANME</college><department>Biomedical Sciences</department><CollegeCode>COLLEGE CODE</CollegeCode><DepartmentCode>BMS</DepartmentCode><institution>Swansea University</institution><apcterm/><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</funders><lastEdited>2022-04-25T16:21:33.9970708</lastEdited><Created>2022-03-23T10:05:19.2034060</Created><path><level id="1">Faculty of Medicine, Health and Life Sciences</level><level id="2">Swansea University Medical School - Medicine</level></path><authors><author><firstname>Claire</firstname><surname>Price</surname><orcid>0000-0002-6045-4835</orcid><order>1</order></author><author><firstname>Andrew</firstname><surname>Warrilow</surname><order>2</order></author><author><firstname>Nicola</firstname><surname>Rolley</surname><order>3</order></author><author><firstname>Josie</firstname><surname>Parker</surname><order>4</order></author><author><firstname>Vera</firstname><surname>Thoss</surname><order>5</order></author><author><firstname>Diane</firstname><surname>Kelly</surname><order>6</order></author><author><firstname>Nicolae</firstname><surname>Corcionivoschi</surname><orcid>0000-0002-3011-3108</orcid><order>7</order></author><author><firstname>Steven</firstname><surname>Kelly</surname><orcid>0000-0001-7991-5040</orcid><order>8</order></author></authors><documents><document><filename>59697__22655__b84a6650f1944166a54c8a1f9e438058.pdf</filename><originalFilename>journal.pone.0265227.pdf</originalFilename><uploaded>2022-03-23T10:06:13.0531100</uploaded><type>Output</type><contentLength>1539104</contentLength><contentType>application/pdf</contentType><version>Version of Record</version><cronfaStatus>true</cronfaStatus><documentNotes>© 2022 Price et al. 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2022-04-25T16:21:33.9970708 v2 59697 2022-03-23 Cytochrome P450 168A1 from Pseudomonas aeruginosa is involved in the hydroxylation of biologically relevant fatty acids 9a4e4dfa37f4318c6fa67933d4fc9a17 0000-0002-6045-4835 Claire Price Claire Price true false f066e233e8d0136c9f547b86fa43747f Andrew Warrilow Andrew Warrilow true false bf3e225536b328599743bf455cea51e0 Nicola Rolley Nicola Rolley true false e563ed4e1c7db8d1e131fb78a5f8d0d5 Josie Parker Josie Parker true false 5ccf81e5d5beedf32ef8d7c3d7ac6c8c Diane Kelly Diane Kelly true false b17cebaf09b4d737b9378a3581e3de93 0000-0001-7991-5040 Steven Kelly Steven Kelly true false 2022-03-23 BMS 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. Journal Article PLOS ONE 17 3 e0265227 Public Library of Science (PLoS) 1932-6203 21 3 2022 2022-03-21 10.1371/journal.pone.0265227 COLLEGE NANME Biomedical Sciences COLLEGE CODE BMS Swansea University 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 2022-04-25T16:21:33.9970708 2022-03-23T10:05:19.2034060 Faculty of Medicine, Health and Life Sciences Swansea University Medical School - Medicine Claire Price 0000-0002-6045-4835 1 Andrew Warrilow 2 Nicola Rolley 3 Josie Parker 4 Vera Thoss 5 Diane Kelly 6 Nicolae Corcionivoschi 0000-0002-3011-3108 7 Steven Kelly 0000-0001-7991-5040 8 59697__22655__b84a6650f1944166a54c8a1f9e438058.pdf journal.pone.0265227.pdf 2022-03-23T10:06:13.0531100 Output 1539104 application/pdf Version of Record true © 2022 Price et al. This is an open access article distributed under the terms of the Creative Commons Attribution License true eng http://creativecommons.org/licenses/by/4.0/ |
title |
Cytochrome P450 168A1 from Pseudomonas aeruginosa is involved in the hydroxylation of biologically relevant fatty acids |
spellingShingle |
Cytochrome P450 168A1 from Pseudomonas aeruginosa is involved in the hydroxylation of biologically relevant fatty acids Claire Price Andrew Warrilow Nicola Rolley Josie Parker Diane Kelly Steven Kelly |
title_short |
Cytochrome P450 168A1 from Pseudomonas aeruginosa is involved in the hydroxylation of biologically relevant fatty acids |
title_full |
Cytochrome P450 168A1 from Pseudomonas aeruginosa is involved in the hydroxylation of biologically relevant fatty acids |
title_fullStr |
Cytochrome P450 168A1 from Pseudomonas aeruginosa is involved in the hydroxylation of biologically relevant fatty acids |
title_full_unstemmed |
Cytochrome P450 168A1 from Pseudomonas aeruginosa is involved in the hydroxylation of biologically relevant fatty acids |
title_sort |
Cytochrome P450 168A1 from Pseudomonas aeruginosa is involved in the hydroxylation of biologically relevant fatty acids |
author_id_str_mv |
9a4e4dfa37f4318c6fa67933d4fc9a17 f066e233e8d0136c9f547b86fa43747f bf3e225536b328599743bf455cea51e0 e563ed4e1c7db8d1e131fb78a5f8d0d5 5ccf81e5d5beedf32ef8d7c3d7ac6c8c b17cebaf09b4d737b9378a3581e3de93 |
author_id_fullname_str_mv |
9a4e4dfa37f4318c6fa67933d4fc9a17_***_Claire Price f066e233e8d0136c9f547b86fa43747f_***_Andrew Warrilow bf3e225536b328599743bf455cea51e0_***_Nicola Rolley e563ed4e1c7db8d1e131fb78a5f8d0d5_***_Josie Parker 5ccf81e5d5beedf32ef8d7c3d7ac6c8c_***_Diane Kelly b17cebaf09b4d737b9378a3581e3de93_***_Steven Kelly |
author |
Claire Price Andrew Warrilow Nicola Rolley Josie Parker Diane Kelly Steven Kelly |
author2 |
Claire Price Andrew Warrilow Nicola Rolley Josie Parker Vera Thoss Diane Kelly Nicolae Corcionivoschi Steven Kelly |
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PLOS ONE |
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e0265227 |
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1932-6203 |
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10.1371/journal.pone.0265227 |
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Public Library of Science (PLoS) |
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description |
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. |
published_date |
2022-03-21T04:17:12Z |
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11.037056 |