ExplorEnz: EC 1.11.2.4

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1.11.2.4

Accepted name:

fatty-acid peroxygenase

Reaction:

fatty acid + H₂O₂ = 3- or 2-hydroxy fatty acid + H₂O

Other name(s):

fatty acid hydroxylase (ambiguous); P450 peroxygenase; CYP152A1; P450BS; P450SPα

Systematic name:

fatty acid:hydroperoxide oxidoreductase (RH-hydroxylating)

Comments:

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.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Matsunaga, I., Yamada, M., Kusunose, E., Nishiuchi, Y., Yano, I. and Ichihara, K. Direct involvement of hydrogen peroxide in bacterial α-hydroxylation of fatty acid. FEBS Lett. 386 (1996) 252–254. [DOI] [PMID: 8647293]
2.	Matsunaga, I., Yamada, M., Kusunose, E., Miki, T. and Ichihara, K. Further characterization of hydrogen peroxide-dependent fatty acid α-hydroxylase from Sphingomonas paucimobilis. J. Biochem. 124 (1998) 105–110. [PMID: 9644252]
3.	Matsunaga, I., Ueda, A., Fujiwara, N., Sumimoto, T. and Ichihara, K. Characterization of the ybdT gene product of Bacillus subtilis: novel fatty acid β-hydroxylating cytochrome P450. Lipids 34 (1999) 841–846. [DOI] [PMID: 10529095]
4.	Imai, Y., Matsunaga, I., Kusunose, E. and Ichihara, K. Unique heme environment at the putative distal region of hydrogen peroxide-dependent fatty acid α-hydroxylase from Sphingomonas paucimobilis (peroxygenase P₄₅₀SPα). J. Biochem. 128 (2000) 189–194. [PMID: 10920253]
5.	Matsunaga, I., Yamada, A., Lee, D.S., Obayashi, E., Fujiwara, N., Kobayashi, K., Ogura, H. and Shiro, Y. Enzymatic reaction of hydrogen peroxide-dependent peroxygenase cytochrome P₄₅₀s: kinetic deuterium isotope effects and analyses by resonance Raman spectroscopy. Biochemistry 41 (2002) 1886–1892. [DOI] [PMID: 11827534]
6.	Lee, D.S., Yamada, A., Sugimoto, H., Matsunaga, I., Ogura, H., Ichihara, K., Adachi, S., Park, S.Y. and 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) 9761–9767. [DOI] [PMID: 12519760]
7.	Matsunaga, I. and Shiro, Y. Peroxide-utilizing biocatalysts: structural and functional diversity of heme-containing enzymes. Curr. Opin. Chem. Biol. 8 (2004) 127–132. [DOI] [PMID: 15062772]
8.	Shoji, O., Wiese, C., Fujishiro, T., Shirataki, C., Wunsch, B. and 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) 1109–1115. [DOI] [PMID: 20490877]

[EC 1.11.2.4 created 2011]