Cytochrome P450 168A1 from Pseudomonas aeruginosa is involved in the hydroxylation of biologically relevant fatty acids
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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| Veröffentlicht in: | PloS one 2022-03, Vol.17 (3), p.e0265227 |
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| creator | Price, Claire L Warrilow, Andrew G S Rolley, Nicola J Parker, Josie E Thoss, Vera Kelly, Diane E Corcionivoschi, Nicolae Kelly, Steven L |
| 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. |
| doi_str_mv | 10.1371/journal.pone.0265227 |
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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.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0265227</identifier><identifier>PMID: 35312722</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Analysis ; Antifungal agents ; Biodiversity ; Biology and Life Sciences ; Cloning ; Cytochrome ; Cytochrome P-450 ; Cytochrome P-450 Enzyme System - genetics ; Cytochrome P-450 Enzyme System - metabolism ; Cytochrome P450 ; Cytochromes P450 ; E coli ; Enzymes ; Extinction ; Fatty Acids ; Genes ; Genetic aspects ; Glycerol ; Hydroxylase ; Hydroxylation ; Lecithin ; Life sciences ; Ligands ; Lungs ; Medical schools ; Medicine and Health Sciences ; Oxidation ; Phosphatidylcholine ; Physical Sciences ; Potassium ; Proteins ; Pseudomonas aeruginosa ; Pseudomonas aeruginosa - genetics ; Pseudomonas aeruginosa - metabolism ; Stearic Acids ; Substrates ; Surfactants ; Veterinary medicine</subject><ispartof>PloS one, 2022-03, Vol.17 (3), p.e0265227</ispartof><rights>COPYRIGHT 2022 Public Library of Science</rights><rights>2022 Price et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. 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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. 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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><cop>United States</cop><pub>Public Library of Science</pub><pmid>35312722</pmid><doi>10.1371/journal.pone.0265227</doi><tpages>e0265227</tpages><orcidid>https://orcid.org/0000-0002-3011-3108</orcidid><orcidid>https://orcid.org/0000-0002-6045-4835</orcidid><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Public Library of Science (PLoS) Journals Open Access; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Analysis Antifungal agents Biodiversity Biology and Life Sciences Cloning Cytochrome Cytochrome P-450 Cytochrome P-450 Enzyme System - genetics Cytochrome P-450 Enzyme System - metabolism Cytochrome P450 Cytochromes P450 E coli Enzymes Extinction Fatty Acids Genes Genetic aspects Glycerol Hydroxylase Hydroxylation Lecithin Life sciences Ligands Lungs Medical schools Medicine and Health Sciences Oxidation Phosphatidylcholine Physical Sciences Potassium Proteins Pseudomonas aeruginosa Pseudomonas aeruginosa - genetics Pseudomonas aeruginosa - metabolism Stearic Acids Substrates Surfactants Veterinary medicine |
| title | Cytochrome P450 168A1 from Pseudomonas aeruginosa is involved in the hydroxylation of biologically relevant fatty acids |
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