Fatty-acid peroxygenase

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Fatty-acid peroxygenase
Identifiers
EC number1.11.2.4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB 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 3- or 2-hydroxy fatty acid + H2O

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

References[edit]

  1. ^ Matsunaga I, Yamada M, Kusunose E, Nishiuchi Y, Yano I, Ichihara K (May 1996). "Direct involvement of hydrogen peroxide in bacterial alpha-hydroxylation of fatty acid". FEBS Letters. 386 (2–3): 252–4. doi:10.1016/0014-5793(96)00451-6. PMID 8647293.
  2. ^ Matsunaga I, Yamada M, Kusunose E, Miki T, Ichihara K (July 1998). "Further characterization of hydrogen peroxide-dependent fatty acid alpha-hydroxylase from Sphingomonas paucimobilis". Journal of Biochemistry. 124 (1): 105–10. doi:10.1093/oxfordjournals.jbchem.a022068. PMID 9644252.
  3. ^ Matsunaga I, Ueda A, Fujiwara N, Sumimoto T, Ichihara K (August 1999). "Characterization of the ybdT gene product of Bacillus subtilis: novel fatty acid beta-hydroxylating cytochrome P450". Lipids. 34 (8): 841–6. doi:10.1007/s11745-999-0431-3. PMID 10529095.
  4. ^ Imai Y, Matsunaga I, Kusunose E, Ichihara K (August 2000). "Unique heme environment at the putative distal region of hydrogen peroxide-dependent fatty acid alpha-hydroxylase from Sphingomonas paucimobilis (peroxygenase P450(SPalpha)". Journal of Biochemistry. 128 (2): 189–94. doi:10.1093/oxfordjournals.jbchem.a022740. PMID 10920253.
  5. ^ Matsunaga I, Yamada A, Lee DS, Obayashi E, Fujiwara N, Kobayashi K, Ogura H, Shiro Y (February 2002). "Enzymatic reaction of hydrogen peroxide-dependent peroxygenase cytochrome P450s: kinetic deuterium isotope effects and analyses by resonance Raman spectroscopy". Biochemistry. 41 (6): 1886–92. doi:10.1021/bi011883p. PMID 11827534.
  6. ^ Lee DS, Yamada A, Sugimoto H, Matsunaga I, Ogura H, Ichihara K, Adachi S, Park SY, Shiro Y (March 2003). "Substrate recognition and molecular mechanism of fatty acid hydroxylation by cytochrome P450 from Bacillus subtilis. Crystallographic, spectroscopic, and mutational studies". The Journal of Biological Chemistry. 278 (11): 9761–7. doi:10.1074/jbc.M211575200. PMID 12519760.
  7. ^ Matsunaga I, Shiro Y (April 2004). "Peroxide-utilizing biocatalysts: structural and functional diversity of heme-containing enzymes". Current Opinion in Chemical Biology. 8 (2): 127–32. doi:10.1016/j.cbpa.2004.01.001. PMID 15062772.
  8. ^ Shoji O, Wiese C, Fujishiro T, Shirataki C, Wünsch B, Watanabe Y (September 2010). "Aromatic C-H bond hydroxylation by P450 peroxygenases: a facile colorimetric assay for monooxygenation activities of enzymes based on Russig's blue formation". Journal of Biological Inorganic Chemistry. 15 (7): 1109–15. doi:10.1007/s00775-010-0671-9. PMID 20490877.

External links[edit]