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Type: Journal article
Title: Selective ϖ-1 oxidation of fatty acids by CYP147G1 from Mycobacterium marinum
Author: Child, S.
Rossi, V.
Bell, S.
Citation: BBA: General Subjects, 2019; 1863(2):408-417
Publisher: Elsevier
Issue Date: 2019
ISSN: 0304-4165
Statement of
Stella A. Child, Vanessa P. Rossi, Stephen G. Bell
Abstract: Background: Cyp147G1 is one of 47 cytochrome P450 encoding genes in Mycobacterium marinum M, a pathogenic bacterium with a high degree of sequence similarity to Mycobacterium tuberculosis and Mycobacterium ulcerans. Cyp147G1 is one of only two of these cyp genes which are closely associated with a complete electron transfer system. Methods: The substrate range of the enzyme was tested in vitro and the activity of CYP147G1 was reconstituted in vivo by co-producing the P450 with the ferredoxin and ferredoxin reductase. Results: Substrates of CYP147G1 include fatty acids ranging from octanoic to hexadecanoic acid. CYP147G1 catalysed the selective hydroxylation of linear and ω-2 methyl branched fatty acids at the ω-1 position (≥ 98%). Oxidation of ω-1 methyl branched fatty acids generated the ω and ω-1 hydroxylation products in almost equal proportions, indicating altered position of hydrogen abstraction. Conclusions: This selectivity of fatty acid hydroxylation inferred that linear species must bind in the active site of the enzyme with the terminal methyl group sequestered so that abstraction at the CH bonds of the ω-1 position is favoured. With branched substrates, one of the methyl groups must be close to the compound I oxygen atom and enable hydroxylation at the terminal methyl group to compete with the reaction at the ω-1CH bond. General Signficance: Hydroxy fatty acids are widely used for industrial, food and medical purposes. CYP147G1 demonstrates high regioselectivity for hydroxylation at a sub-terminal position on a broad range of linear fatty acids, not seen in other CYP enzymes.
Keywords: Enzymology; fatty acid metabolism; electron transfer; biocatalysis; cytochrome P450
Rights: © 2018 Elsevier B.V. All rights reserved.
DOI: 10.1016/j.bbagen.2018.11.013
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