학술논문
Cytochrome P450 168A1 from Pseudomonas aeruginosa is involved in the hydroxylation of biologically relevant fatty acids.
Document Type
Article
Author
Source
Subject
*CYTOCHROME P-450
*SATURATED fatty acids
*UNSATURATED fatty acids
*PSEUDOMONAS aeruginosa
*OLEIC acid
*PALMITIC acid
*EPOXYEICOSATRIENOIC acids
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Language
ISSN
1932-6203
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 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 FROM AUTHOR]