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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)) an...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8936499/ https://www.ncbi.nlm.nih.gov/pubmed/35312722 http://dx.doi.org/10.1371/journal.pone.0265227 |
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author | Price, Claire L. Warrilow, Andrew G. S. Rolley, Nicola J. Parker, Josie E. Thoss, Vera Kelly, Diane E. Corcionivoschi, Nicolae Kelly, Steven L. |
author_facet | Price, Claire L. Warrilow, Andrew G. S. Rolley, Nicola J. Parker, Josie E. Thoss, Vera Kelly, Diane E. Corcionivoschi, Nicolae Kelly, Steven L. |
author_sort | Price, Claire L. |
collection | PubMed |
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. |
format | Online Article Text |
id | pubmed-8936499 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-89364992022-03-22 Cytochrome P450 168A1 from Pseudomonas aeruginosa is involved in the hydroxylation of biologically relevant fatty acids Price, Claire L. Warrilow, Andrew G. S. Rolley, Nicola J. Parker, Josie E. Thoss, Vera Kelly, Diane E. Corcionivoschi, Nicolae Kelly, Steven L. PLoS One Research Article 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. Public Library of Science 2022-03-21 /pmc/articles/PMC8936499/ /pubmed/35312722 http://dx.doi.org/10.1371/journal.pone.0265227 Text en © 2022 Price et al https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Price, Claire L. Warrilow, Andrew G. S. Rolley, Nicola J. Parker, Josie E. Thoss, Vera Kelly, Diane E. Corcionivoschi, Nicolae Kelly, Steven L. Cytochrome P450 168A1 from Pseudomonas aeruginosa is involved in the hydroxylation of biologically relevant fatty acids |
title | 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_short | 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 |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8936499/ https://www.ncbi.nlm.nih.gov/pubmed/35312722 http://dx.doi.org/10.1371/journal.pone.0265227 |
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