Phytanic acid α-hydroxylation by bacterial cytochrome P450

Abstract

Fatty acid α-hydroxylase, a cytochrome P450 enzyme, from Sphingomonas paucimobilis, utilizes various straight-chain fatty acids as substrates. We investigated whether a recombinant fatty acid α-hydroxylase is able to metabolize phytanic acid, a methyl-branched fatty acid. When phytanic acid was incubated with the recombinant enzyme in the presence of H2O2, a reaction product was detected by gas chromatography, whereas a reaction product was not detected in the absence of H2O2. When a heat-inactivated enzyme was used, a reaction product was not detected with any concentration of H2O2. Analysis of the methylated product by gas chromatography-mass spectrometry revealed a fragmentation pattern of 2-hydroxyphytanic acid methyl ester. By single-ion monitoring, the mass ion and the characteristic fragmentation ions of 2-hydroxyphytanic acid methyl ester were detected at the retention time corresponding to the time of the product observed on the gas chromatogram. The K m value for phytanic acid was approximately 50 μM, which was similar to that for myristic acid, although the calculated V max for phytanic acid was about 15-fold lower than that for myristic acid. These results indicate that a bacterial cytochrome P450 is able to oxidize phytanic acid to form 2-hydroxyphytanic acid.

DOI: 10.1007/s11745-998-0325-4

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@article{Matsunaga1998PhytanicA, title={Phytanic acid α-hydroxylation by bacterial cytochrome P450}, author={Isamu Matsunaga and Tatsuo Sumimoto and Emi Kusunose and Kosuke Ichihara}, journal={Lipids}, year={1998}, volume={33}, pages={1213-1216} }