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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
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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 &#x3C9;-1- and &#x3C9;-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 &#x3C9;-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">Swansea University Medical School</level><level id="2">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><orcid>0000-0002-3855-4194</orcid><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>&#xA9; 2022 Price et al. 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spelling 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 0000-0002-3855-4194 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 Swansea University Medical School Medicine Claire Price 0000-0002-6045-4835 1 Andrew Warrilow 2 Nicola Rolley 3 Josie Parker 0000-0002-3855-4194 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
format Journal article
container_title PLOS ONE
container_volume 17
container_issue 3
container_start_page e0265227
publishDate 2022
institution Swansea University
issn 1932-6203
doi_str_mv 10.1371/journal.pone.0265227
publisher Public Library of Science (PLoS)
college_str Swansea University Medical School
hierarchytype
hierarchy_top_id swanseauniversitymedicalschool
hierarchy_top_title Swansea University Medical School
hierarchy_parent_id swanseauniversitymedicalschool
hierarchy_parent_title Swansea University Medical School
department_str Medicine{{{_:::_}}}Swansea University Medical School{{{_:::_}}}Medicine
document_store_str 1
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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 2022-03-21T04:17:04Z
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