Fatty-acid peroxygenase

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Fatty-acid peroxygenase
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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.

Related Research Articles

In chemistry, hydroxylation can refer to:

<span class="mw-page-title-main">Cytochrome P450</span> Class of enzymes

Cytochromes P450 are a superfamily of enzymes containing heme as a cofactor that mostly, but not exclusively, function as monooxygenases. In mammals, these proteins oxidize steroids, fatty acids, and xenobiotics, and are important for the clearance of various compounds, as well as for hormone synthesis and breakdown, steroid hormone synthesis, drug metabolism, and the biosynthesis of defensive compounds, fatty acids, and hormones. CYP450 enzymes convert xenobiotics into hydrophilic derivatives, which are more readily excreted. In almost all of the transformations that they catalyze, P450's affect hydroxylation.

<span class="mw-page-title-main">CYP2E1</span> Protein-coding gene in the species Homo sapiens

Cytochrome P450 2E1 is a member of the cytochrome P450 mixed-function oxidase system, which is involved in the metabolism of xenobiotics in the body. This class of enzymes is divided up into a number of subcategories, including CYP1, CYP2, and CYP3, which as a group are largely responsible for the breakdown of foreign compounds in mammals.

Any enzyme system that includes cytochrome P450 protein or domain can be called a P450-containing system.

Omega oxidation (ω-oxidation) is a process of fatty acid metabolism in some species of animals. It is an alternative pathway to beta oxidation that, instead of involving the β carbon, involves the oxidation of the ω carbon. The process is normally a minor catabolic pathway for medium-chain fatty acids, but becomes more important when β oxidation is defective.

<span class="mw-page-title-main">21-Hydroxylase</span> Human enzyme that hydroxylates steroids

Steroid 21-hydroxylase is a protein that in humans is encoded by the CYP21A2 gene. The protein is an enzyme that hydroxylates steroids at the C21 position on the molecule. Naming conventions for enzymes are based on the substrate acted upon and the chemical process performed. Biochemically, this enzyme is involved in the biosynthesis of the adrenal gland hormones aldosterone and cortisol, which are important in blood pressure regulation, sodium homeostasis and blood sugar control. The enzyme converts progesterone and 17α-hydroxyprogesterone into 11-deoxycorticosterone and 11-deoxycortisol, respectively, within metabolic pathways which in humans ultimately lead to aldosterone and cortisol creation—deficiency in the enzyme may cause congenital adrenal hyperplasia.

In enzymology, a 5beta-cholestane-3alpha,7alpha-diol 12alpha-hydroxylase (EC 1.14.13.96) is an enzyme that catalyzes the chemical reaction

In enzymology, a cholestanetriol 26-monooxygenase (EC 1.14.13.15) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Cholesterol 24-hydroxylase</span> Protein family

Cholesterol 24-hydroxylase, also commonly known as cholesterol 24S-hydroxylase, cholesterol 24-monooxygenase, CYP46, or CYP46A1, is an enzyme that catalyzes the conversion of cholesterol to 24S-hydroxycholesterol. It is responsible for the majority of cholesterol turnover in the human central nervous system. The systematic name of this enzyme class is cholesterol,NADPH:oxygen oxidoreductase (24-hydroxylating).

In enzymology, a trans-cinnamate 4-monooxygenase (EC 1.14.14.91) is an enzyme that catalyzes the chemical reaction

In enzymology, an unspecific monooxygenase (EC 1.14.14.1) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">CYP4A11</span> Protein-coding gene in the species Homo sapiens

Cytochrome P450 4A11 is a protein that in humans is codified by the CYP4A11 gene.

<span class="mw-page-title-main">CYP4F2</span> Enzyme protein in the species Homo sapiens

Cytochrome P450 4F2 is a protein that in humans is encoded by the CYP4F2 gene. This protein is an enzyme, a type of protein that catalyzes chemical reactions inside cells. This specific enzyme is part of the superfamily of cytochrome P450 (CYP) enzymes, and the encoding gene is part of a cluster of cytochrome P450 genes located on chromosome 19.

<span class="mw-page-title-main">CYP4F8</span> Protein-coding gene in the species Homo sapiens

Cytochrome P450 4F8 is a protein that in humans is encoded by the CYP4F8 gene.

<span class="mw-page-title-main">CYP4F3</span> Protein-coding gene in the species Homo sapiens

Cytochrome P450 4F3, also leukotriene-B(4) omega-hydroxylase 2, is an enzyme that in humans is encoded by the CYP4F3 gene. CYP4F3 encodes two distinct enzymes, CYP4F3A and CYP4F3B, which originate from the alternative splicing of a single pre-mRNA precursor molecule; selection of either isoform is tissue-specific with CYP3F3A being expressed mostly in leukocytes and CYP4F3B mostly in the liver.

<span class="mw-page-title-main">CYP4F22</span> Protein-coding gene in the species Homo sapiens

CYP4F22 is a protein that in humans is encoded by the CYP4F22 gene.

<span class="mw-page-title-main">CYP4F11</span> Protein-coding gene in the species Homo sapiens

CYP4F11 is a protein that in humans is encoded by the CYP4F11 gene. This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This gene is part of a cluster of cytochrome P450 genes on chromosome 19. Another member of this family, CYP4F2, is approximately 16 kb away. Alternatively spliced transcript variants encoding the same protein have been found for this gene.

<span class="mw-page-title-main">CYP2U1</span> Protein-coding gene in the species Homo sapiens

CYP2U1 is a protein that in humans is encoded by the CYP2U1 gene

Unspecific peroxygenase (EC 1.11.2.1, aromatic peroxygenase, mushroom peroxygenase, haloperoxidase-peroxygenase, Agrocybe aegerita peroxidase) is an enzyme with systematic name substrate:hydrogen peroxide oxidoreductase (RH-hydroxylating or -epoxidising). This enzyme catalyses the following chemical reaction

Cytochrome P450 omega hydroxylases, also termed cytochrome P450 ω-hydroxylases, CYP450 omega hydroxylases, CYP450 ω-hydroxylases, CYP omega hydroxylase, CYP ω-hydroxylases, fatty acid omega hydroxylases, cytochrome P450 monooxygenases, and fatty acid monooxygenases, are a set of cytochrome P450-containing enzymes that catalyze the addition of a hydroxyl residue to a fatty acid substrate. The CYP omega hydroxylases are often referred to as monoxygenases; however, the monooxygenases are CYP450 enzymes that add a hydroxyl group to a wide range of xenobiotic and naturally occurring endobiotic substrates, most of which are not fatty acids. The CYP450 omega hydroxylases are accordingly better viewed as a subset of monooxygenases that have the ability to hydroxylate fatty acids. While once regarded as functioning mainly in the catabolism of dietary fatty acids, the omega oxygenases are now considered critical in the production or break-down of fatty acid-derived mediators which are made by cells and act within their cells of origin as autocrine signaling agents or on nearby cells as paracrine signaling agents to regulate various functions such as blood pressure control and inflammation.

References

  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.