2024-03-29T06:20:59Z
https://nagoya.repo.nii.ac.jp/oai
oai:nagoya.repo.nii.ac.jp:00025140
2023-01-16T04:15:53Z
336:695:696
α-Oxidative decarboxylation of fatty acids catalysed by cytochrome P450 peroxygenases yielding shorter-alkyl-chain fatty acids
Onoda, Hiroki
Shoji, Osami
Suzuki, Kazuto
Sugimoto, Hiroshi
Shiro, Yoshitsugu
Watanabe, Yoshihito
open access
Cytochrome P450 peroxygenases belonging to the CYP152 family catalyse the oxidation of fatty acids using H2O2. CYP152N1 isolated from Exiguobacterium sp. AT1b exclusively catalyses the α-selective hydroxylation of myristic acid at physiological H2O2 concentration. However, a series of shorter-alkyl-chain fatty acids such as tridecanoic acid were produced from myristic acid by increasing the concentration of H2O2 (1–10 mM). The yield of tridecanoic acid from myristic acid reached 17%. An 18O-labeled oxidant study suggested that CYP152N1 catalysed the overoxidation of α-hydroxymyristic acid to form α-ketomyristic acid, which in turn was spontaneously decomposed by H2O2 to yield tridecanoic acid. Crystal structure analysis of CYP152N1 revealed its high similarity to other CYP152 family enzymes, such as CYP152A1 and CYP152B1. MD simulations of α-hydroxymyristic acid accommodated in CYP152N1 proposed a possible pre-oxidation conformation of α-hydroxymyristic acid for the decarboxylation reaction.
Royal Society of Chemistry
2018-01-21
eng
journal article
AM
http://hdl.handle.net/2237/27360
https://nagoya.repo.nii.ac.jp/records/25140
https://doi.org/10.1039/C7CY02263H
2044-4753
Catalysis Science and Technology
8
434
442
https://nagoya.repo.nii.ac.jp/record/25140/files/RSC_171123.pdf
application/pdf
1.8 MB
2019-01-21