Cannabaceae

Fatty-acid peroxygenase
Identifiers
EC no.1.11.2.4
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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. Bibcode:1996FEBSL.386..252M. 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. S2CID 4017380.
  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. S2CID 23025367.

External links[edit]

One thought on “Cannabaceae

  1. Well, that’s interesting to know that Psilotum nudum are known as whisk ferns. Psilotum nudum is the commoner species of the two. While the P. flaccidum is a rare species and is found in the tropical islands. Both the species are usually epiphytic in habit and grow upon tree ferns. These species may also be terrestrial and grow in humus or in the crevices of the rocks.
    View the detailed Guide of Psilotum nudum: Detailed Study Of Psilotum Nudum (Whisk Fern), Classification, Anatomy, Reproduction

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