EC 1.11.2.4 - Fatty-acid peroxygenase

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IntEnz Enzyme Nomenclature
EC 1.11.2.4

Names

Accepted name:
fatty-acid peroxygenase
Other names:
fatty acid hydroxylase
P450 peroxygenase
CYP152A1
P450BS
P450SPα
Systematic name:
fatty acid:hydroperoxide oxidoreductase (RH-hydroxylating)

Reactions

Cofactor

Comments:

A cytosolic heme-thiolate protein with sequence homology to P450 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 P450s. 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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00081
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Matsunaga, I., Yamada, M., Kusunose, E., Nishiuchi, Y., Yano, I., Ichihara, K.
    Direct involvement of hydrogen peroxide in bacterial α-hydroxylation of fatty acid.
    FEBS Lett. 386: 252-254 (1996). [PMID: 8647293]
  2. Matsunaga, I., Yamada, M., Kusunose, E., Miki, T., Ichihara, K.
    Further characterization of hydrogen peroxide-dependent fatty acid α-hydroxylase from Sphingomonas paucimobilis.
    J. Biochem. 124: 105-110 (1998). [PMID: 9644252]
  3. Matsunaga, I., Ueda, A., Fujiwara, N., Sumimoto, T., Ichihara, K.
    Characterization of the ybdT gene product of Bacillus subtilis: novel fatty acid β-hydroxylating cytochrome P450.
    Lipids 34: 841-846 (1999). [PMID: 10529095]
  4. Imai, Y., Matsunaga, I., Kusunose, E., Ichihara, K.
    Unique heme environment at the putative distal region of hydrogen peroxide-dependent fatty acid α-hydroxylase from Sphingomonas paucimobilis (peroxygenase P450(SPα).
    J. Biochem. 128: 189-194 (2000). [PMID: 10920253]
  5. Matsunaga, I., Yamada, A., Lee, D. S., 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: 1886-1892 (2002). [PMID: 11827534]
  6. Lee, D. S., Yamada, A., Sugimoto, H., Matsunaga, I., Ogura, H., Ichihara, K., Adachi, S., Park, S. Y., 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: 9761-9767 (2003). [PMID: 12519760]
  7. Matsunaga, I., Shiro, Y.
    Peroxide-utilizing biocatalysts: structural and functional diversity of heme-containing enzymes.
    Curr Opin Chem Biol 8: 127-132 (2004). [PMID: 15062772]
  8. 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: 1109-1115 (2010). [PMID: 20490877]

[EC 1.11.2.4 created 2011]