Delta8-fatty-acid desaturase

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Delta8-fatty-acid desaturase
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EC no. 1.14.19.4
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Delta8-fatty-acid desaturase (EC 1.14.19.4, Delta8-sphingolipid desaturase, EFD1, BoDES8, SLD, Delta8 fatty acid desaturase, Delta8-desaturase) is an enzyme with systematic name phytosphinganine,hydrogen donor:oxygen Delta8-oxidoreductase. [1] [2] [3] [4] This enzyme catalyses the following chemical reaction

phytosphinganine + reduced acceptor + O2 Delta8-phytosphingenine + acceptor + 2 H2O

This enzyme, which has been found mainly in plants, introduces a double bond at Delta8 of C18 and C20 fatty acids.

Related Research Articles

<span class="mw-page-title-main">Lipid</span> Substance of biological origin that is soluble in nonpolar solvents

Lipids are a broad group of organic compounds which include fats, waxes, sterols, fat-soluble vitamins, monoglycerides, diglycerides, phospholipids, and others. The functions of lipids include storing energy, signaling, and acting as structural components of cell membranes. Lipids have applications in the cosmetic and food industries, and in nanotechnology.

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">2,4 Dienoyl-CoA reductase</span> Class of enzymes

2,4 Dienoyl-CoA reductase also known as DECR1 is an enzyme which in humans is encoded by the DECR1 gene which resides on chromosome 8. This enzyme catalyzes the following reactions

<span class="mw-page-title-main">Acyl-(acyl-carrier-protein) desaturase</span> Class of enzymes

In enzymology, an acyl-[acyl-carrier-protein] desaturase (EC 1.14.19.2) is an enzyme that catalyzes the chemical reaction

In enzymology, a Δ7-sterol 5(6)-desaturase is an enzyme that catalyzes the chemical reaction

In enzymology, a linoleoyl-CoA desaturase (also Delta 6 desaturase, EC 1.14.19.3) is an enzyme that converts between types of fatty acids, which are essential nutrients in the human body. The enzyme mainly catalyzes the chemical reaction

<span class="mw-page-title-main">Stearoyl-CoA 9-desaturase</span> Class of enzymes

Stearoyl-CoA desaturase (Δ-9-desaturase) is an endoplasmic reticulum enzyme that catalyzes the rate-limiting step in the formation of monounsaturated fatty acids (MUFAs), specifically oleate and palmitoleate from stearoyl-CoA and palmitoyl-CoA. Oleate and palmitoleate are major components of membrane phospholipids, cholesterol esters and alkyl-diacylglycerol. In humans, the enzyme is encoded by the SCD gene.

<span class="mw-page-title-main">CYP2C18</span> Protein-coding gene in the species Homo sapiens

Cytochrome P450 2C18 is a protein that in humans is encoded by the CYP2C18 gene.

<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">Sterol-C5-desaturase-like</span> Protein-coding gene in the species Homo sapiens

Lathosterol oxidase is a Δ7-sterol 5(6)-desaturase enzyme that in humans is encoded by the SC5D gene.

<span class="mw-page-title-main">CYP4F2</span> Protein-coding gene in the species Homo sapiens

Leukotriene-B(4) omega-hydroxylase 1 is an enzyme protein involved in the metabolism of various endogenous substrates and xenobiotics. The most notable substrate of the enzyme is leukotriene B4, a potent mediator of inflammation. The CYP4F2 gene encodes the enzyme in humans.

Linoleate 8R-lipoxygenase (EC 1.13.11.60, linoleic acid 8R-dioxygenase, 5,8-LDS (bifunctional enzyme), 7,8-LDS (bifunctional enzyme), 5,8-linoleate diol synthase (bifunctional enzyme), 7,8-linoleate diol synthase (bifunctional enzyme), PpoA) is an enzyme with systematic name linoleate:oxygen (8R)-oxidoreductase. This enzyme catalyses the following chemical reaction

Delta11-fatty-acid desaturase (EC 1.14.19.5, Delta11 desaturase, fatty acid Delta11-desaturase, TpDESN, Cro-PG, Delta11 fatty acid desaturase, Z/E11-desaturase, Delta11-palmitoyl-CoA desaturase) is an enzyme with systematic name acyl-CoA,hydrogen donor:oxygen Delta11-oxidoreductase. This enzyme catalyses the following chemical reaction

Delta12-fatty-acid desaturase (EC 1.14.19.6, Delta12 fatty acid desaturase, Delta12(omega6)-desaturase, oleoyl-CoA Delta12 desaturase, Delta12 desaturase, Delta12-desaturase) is an enzyme with systematic name acyl-CoA,hydrogen donor:oxygen Delta12-oxidoreductase. This enzyme catalyses the following chemical reaction

Very-long-chain 3-oxoacyl-CoA synthase (EC 2.3.1.199, very-long-chain 3-ketoacyl-CoA synthase, very-long-chain beta-ketoacyl-CoA synthase, condensing enzyme, CUT1 (gene), CERS6 (gene), FAE1 (gene), KCS (gene), ELO (gene)) is an enzyme with systematic name malonyl-CoA:very-long-chain acyl-CoA malonyltransferase (decarboxylating and thioester-hydrolysing). This enzyme catalyses the following chemical reaction

epi-Cedrol synthase (EC 4.2.3.39, 8-epicedrol synthase, epicedrol synthase) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (8-epi-cedrol-forming). This enzyme catalyses the following chemical reaction

(–)-α-Pinene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase [cyclizing, (–)-α-pinene-forming]. This enzyme catalyses the following chemical reaction

(–)-β-Pinene synthase (EC 4.2.3.120, β-geraniolene synthase, (–)-(1S,5S)-pinene synthase, geranyldiphosphate diphosphate lyase (pinene forming)) is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase [cyclizing, (–)-β-pinene-forming]. This enzyme catalyses the following chemical reaction

Odd-chain fatty acids are those fatty acids that contain an odd number of carbon atoms. In addition to being classified according to their saturation or unsaturation, fatty acids are also classified according to their odd or even numbers of constituent carbon atoms. With respect to natural abundance, most fatty acids are even chain, e.g. palmitic (C16) and stearic (C18). In terms of physical properties, odd and even fatty acids are similar, generally being colorless, soluble in alcohols, and often somewhat oily. The odd-chain fatty acids are biosynthesized and metabolized slightly differently from the even-chained relatives. In addition to the usual C12-C22 long chain fatty acids, some very long chain fatty acids (VLCFAs) are also known. Some of these VLCFAs are also of the odd-chain variety.

<span class="mw-page-title-main">C-5 sterol desaturase</span> Class of enzymes

C-5 sterol desaturase is an enzyme that is highly conserved among eukaryotes and catalyzes the dehydrogenation of a C-5(6) bond in a sterol intermediate compound as a step in the biosynthesis of major sterols. The precise structure of the enzyme's substrate varies by species. For example, the human C-5 sterol desaturase oxidizes lathosterol, while its ortholog ERG3 in the yeast Saccharomyces cerevisiae oxidizes episterol.

References

  1. Wallis JG, Browse J (May 1999). "The Delta8-desaturase of Euglena gracilis: an alternate pathway for synthesis of 20-carbon polyunsaturated fatty acids". Archives of Biochemistry and Biophysics. 365 (2): 307–16. doi:10.1006/abbi.1999.1167. PMID   10328826.
  2. Sperling P, Libisch B, Zähringer U, Napier JA, Heinz E (April 2001). "Functional identification of a delta8-sphingolipid desaturase from Borago officinalis". Archives of Biochemistry and Biophysics. 388 (2): 293–8. doi:10.1006/abbi.2001.2308. PMID   11368168.
  3. Takakuwa N, Kinoshita M, Oda Y, Ohnishi M (December 2002). "Isolation and characterization of the genes encoding delta(8)-sphingolipid desaturase from Saccharomyces kluyveri and Kluyveromyces lactis". Current Microbiology. 45 (6): 459–61. doi:10.1007/s00284-002-3860-0. PMID   12402089. S2CID   25735503.
  4. Beckmann C, Rattke J, Oldham NJ, Sperling P, Heinz E, Boland W (July 2002). "Characterization of a Delta8-sphingolipid desaturase from higher plants: a stereochemical and mechanistic study on the origin of E,Z isomers". Angewandte Chemie. 41 (13): 2298–300. doi:10.1002/1521-3773(20020703)41:13<2298::AID-ANIE2298>3.0.CO;2-G. PMID   12203571.