Open AccessCytochrome P450 168A1 from Pseudomonas aeruginosa is involved in the hydroxylation of biologically relevant fatty acids
Author(s) -
Claire Price,
Andrew G. S. Warrilow,
Nicola J. Rolley,
Josie E. Parker,
Vera Thoss,
Diane Kelly,
Nicolae Corcionivoschi,
Steven L. Kelly
Publication year - 2022
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0265227
Subject(s) - stearic acid , palmitic acid , biochemistry , pseudomonas aeruginosa , hydroxylation , cytochrome p450 , oleic acid , chemistry , fatty acid , myristic acid , biology , palmitoleic acid , phosphatidylcholine , escherichia coli , metabolism , bacteria , phospholipid , organic chemistry , enzyme , gene , membrane , genetics
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 .