Oxidoreductases;
Acting on a peroxide as acceptor;
Peroxygenases

fatty acid:hydroperoxide oxidoreductase (RH-hydroxylating)

fatty acid + H2O2 = 3- or 2-hydroxy fatty acid + H2O [RN:R09740 R09741]

R09740 R09741

fatty acid [CPD:C00162];
H2O2 [CPD:C00027]

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 1.11.2.4 created 2011

1  [PMID:8647293]

Matsunaga I, Yamada M, Kusunose E, Nishiuchi Y, Yano I, Ichihara K

Direct involvement of hydrogen peroxide in bacterial alpha-hydroxylation of fatty acid.

FEBS. Lett. 386 (1996) 252-4.

2  [PMID:9644252]

Matsunaga I, Yamada M, Kusunose E, Miki T, Ichihara K

Further characterization of hydrogen peroxide-dependent fatty acid alpha-hydroxylase from Sphingomonas paucimobilis.

J. Biochem. 124 (1998) 105-10.

3  [PMID:10529095]

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.

Lipids. 34 (1999) 841-6.

[bsu:BSU02100]

4  [PMID:10920253]

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).

J. Biochem. 128 (2000) 189-94.

5  [PMID:11827534]

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.

Biochemistry. 41 (2002) 1886-92.

6  [PMID:12519760]

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.

J. Biol. Chem. 278 (2003) 9761-7.

[bsu:BSU02100]

7  [PMID:15062772]

Matsunaga I, Shiro Y

Peroxide-utilizing biocatalysts: structural and functional diversity of heme-containing enzymes.

Curr. Opin. Chem. Biol. 8 (2004) 127-32.

8  [PMID:20490877]

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.

J. Biol. Inorg. Chem. 15 (2010) 1109-15.