Fatty-acid peroxygenase

Fatty-acid peroxygenase
Identifiers
EC number 1.11.2.4
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Fatty-acid peroxygenase (EC 1.11.2.4, fatty acid hydroxylase (ambiguous), P450 peroxygenase, CYP152A1, P450BS, P450SPalpha) is an enzyme with systematic name fatty acid:hydroperoxide oxidoreductase (RH-hydroxylating).[1][2][3][4][5][6][7][8] This enzyme catalyses the following chemical reaction

fatty acid + H2O2 \rightleftharpoons 3- or 2-hydroxy fatty acid + H2O

Fatty-acid peroxygenase is a cytosolic heme-thiolate protein.

References

  1. ↑ Matsunaga, I., Yamada, M., Kusunose, E., Nishiuchi, Y., Yano, I. and Ichihara, K. (1996). "Direct involvement of hydrogen peroxide in bacterial α-hydroxylation of fatty acid". FEBS Lett. 386 (2-3): 252–254. doi:10.1016/0014-5793(96)00451-6. PMID 8647293.
  2. ↑ Matsunaga, I., Yamada, M., Kusunose, E., Miki, T. and Ichihara, K. (1998). "Further characterization of hydrogen peroxide-dependent fatty acid α-hydroxylase from Sphingomonas paucimobilis". J. Biochem. 124 (1): 105–110. doi:10.1093/oxfordjournals.jbchem.a022068. PMID 9644252.
  3. ↑ Matsunaga, I., Ueda, A., Fujiwara, N., Sumimoto, T. and Ichihara, K. (1999). "Characterization of the ybdT gene product of Bacillus subtilis: novel fatty acid β-hydroxylating cytochrome P450". Lipids 34 (8): 841–846. doi:10.1007/s11745-999-0431-3. PMID 10529095.
  4. ↑ Imai, Y., Matsunaga, I., Kusunose, E. and Ichihara, K. (2000). "Unique heme environment at the putative distal region of hydrogen peroxide-dependent fatty acid α-hydroxylase from Sphingomonas paucimobilis (peroxygenase P450SPα)". J. Biochem. 128 (2): 189–194. doi:10.1093/oxfordjournals.jbchem.a022740. PMID 10920253.
  5. ↑ Matsunaga, I., Yamada, A., Lee, D.S., Obayashi, E., Fujiwara, N., Kobayashi, K., Ogura, H. and Shiro, Y. (2002). "Enzymatic reaction of hydrogen peroxide-dependent peroxygenase cytochrome P450s: kinetic deuterium isotope effects and analyses by resonance Raman spectroscopy". Biochemistry 41 (6): 1886–1892. doi:10.1021/bi011883p. PMID 11827534.
  6. ↑ Lee, D.S., Yamada, A., Sugimoto, H., Matsunaga, I., Ogura, H., Ichihara, K., Adachi, S., Park, S.Y. and Shiro, Y. (2003). "Substrate recognition and molecular mechanism of fatty acid hydroxylation by cytochrome P450 from Bacillus subtilis. Crystallographic, spectroscopic, and mutational studies". J. Biol. Chem. 278 (11): 9761–9767. doi:10.1074/jbc.M211575200. PMID 12519760.
  7. ↑ Matsunaga, I. and Shiro, Y. (2004). "Peroxide-utilizing biocatalysts: structural and functional diversity of heme-containing enzymes". Curr. Opin. Chem. Biol. 8 (2): 127–132. doi:10.1016/j.cbpa.2004.01.001. PMID 15062772.
  8. ↑ Shoji, O., Wiese, C., Fujishiro, T., Shirataki, C., Wunsch, B. and Watanabe, Y. (2010). "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 (7): 1109–1115. doi:10.1007/s00775-010-0671-9. PMID 20490877.

External links

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