fatty acid hydroxylase (ambiguous);
Acting on a peroxide as acceptor;
fatty acid:hydroperoxide oxidoreductase (RH-hydroxylating)
fatty acid + H2O2 = 3- or 2-hydroxy fatty acid + H2O [RN:
A cytosolic heme-thiolate protein with sequence homology to P-450 monooxygenases. Unlike the latter, it needs neither NAD(P)H, dioxygen nor specific reductases for function. Enzymes of this type are produced by bacteria (e.g. Sphingomonas paucimobilis, Bacillus subtilis). Catalytic turnover rates are high compared with those of monooxygenation reactions as well as peroxide shunt reactions catalysed by the common P-450s. A model substrate is myristate, but other saturated and unsaturated fatty acids are also hydroxylated. Oxidizes the peroxidase substrate 3,3',5,5'-tetramethylbenzidine (TMB) and peroxygenates aromatic substrates in a fatty-acid-dependent reaction.
EC 22.214.171.124 created 2011
K15629 fatty-acid peroxygenase
PSTU: UIB01_16925 UIB01_17410
JIE: OH818_06985 OH818_28305
BMED: GYM46_02230 GYM46_08815
RMH: LVO79_13510 LVO79_19135
SMUC: JL100_008485 JL100_036405
BON: A361_11985 A361_27885
HMN: HM131_02160 HM131_17350
SHV: AAT16_05610 AAT16_12110
JEA: JEM45_01515 JEM45_03820
PLW: D5F53_16700 D5F53_33045
AFAS: NZD89_20385 NZD89_24860
PMAR: B0X71_01145 B0X71_04070 B0X71_09890
SSX: SACTE_6029 SACTE_6135
ART: Arth_4205 Arth_4305 Arth_4474
BSD: BLASA_1730 BLASA_3595(cypC)
MTEM: GCE86_14395 GCE86_19020 » show all
Matsunaga I, Yamada M, Kusunose E, Nishiuchi Y, Yano I, Ichihara K
Direct involvement of hydrogen peroxide in bacterial alpha-hydroxylation of fatty acid.
Matsunaga I, Yamada M, Kusunose E, Miki T, Ichihara K
Further characterization of hydrogen peroxide-dependent fatty acid alpha-hydroxylase from Sphingomonas paucimobilis.
Matsunaga I, Ueda A, Fujiwara N, Sumimoto T, Ichihara K
Characterization of the ybdT gene product of Bacillus subtilis: novel fatty acid beta-hydroxylating cytochrome P450.
Imai Y, Matsunaga I, Kusunose E, Ichihara K
Unique heme environment at the putative distal region of hydrogen peroxide-dependent fatty acid alpha-hydroxylase from Sphingomonas paucimobilis (peroxygenase P450(SPalpha).
Matsunaga I, Yamada A, Lee DS, Obayashi E, Fujiwara N, Kobayashi K, Ogura H, Shiro Y
Enzymatic reaction of hydrogen peroxide-dependent peroxygenase cytochrome P450s: kinetic deuterium isotope effects and analyses by resonance Raman spectroscopy.
Lee DS, Yamada A, Sugimoto H, Matsunaga I, Ogura H, Ichihara K, Adachi S, Park SY, Shiro Y
Substrate recognition and molecular mechanism of fatty acid hydroxylation by cytochrome P450 from Bacillus subtilis. Crystallographic, spectroscopic, and mutational studies.
Matsunaga I, Shiro Y
Peroxide-utilizing biocatalysts: structural and functional diversity of heme-containing enzymes.
Shoji O, Wiese C, Fujishiro T, Shirataki C, Wunsch B, Watanabe Y
Aromatic C-H bond hydroxylation by P450 peroxygenases: a facile colorimetric assay for monooxygenation activities of enzymes based on Russig's blue formation.
ExplorEnz - The Enzyme Database: 126.96.36.199
ExPASy - ENZYME nomenclature database: 188.8.131.52