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Phytanic acid α‐hydroxylation by bacterial cytochrome P450
Author(s) -
Matsunaga Isamu,
Sumimoto Tatsuo,
Kusunose Emi,
Ichihara Kosuke
Publication year - 1998
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/s11745-998-0325-4
Subject(s) - phytanic acid , chemistry , myristic acid , fatty acid , chromatography , hydroxylation , enzyme , biochemistry , stereochemistry , organic chemistry , palmitic acid , peroxisome , gene
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 H 2 O 2 , a reaction product was detected by gas chromatography, whereas a reaction product was not detected in the absence of H 2 O 2 . When a heat‐inactivated enzyme was used, a reaction product was not detected with any concentration of H 2 O 2 . 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.