Delta12-fatty-acid desaturase

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Delta12-fatty-acid desaturase
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EC no. 1.14.19.6
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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. [1] [2] [3] [4] This enzyme catalyses the following chemical reaction

acyl-CoA + reduced acceptor + O2 Delta12-acyl-CoA + acceptor + 2 H2O

In the yeast Lipomyces starkeyi and in the American cockroach, this microsomal enzyme converts oleoyl-CoA into linoleoyl-CoA.

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.

<span class="mw-page-title-main">Beta oxidation</span> Process of fatty acid breakdown

In biochemistry and metabolism, beta oxidation (also β-oxidation) is the catabolic process by which fatty acid molecules are broken down in the cytosol in prokaryotes and in the mitochondria in eukaryotes to generate acetyl-CoA, which enters the citric acid cycle, and NADH and FADH2, which are co-enzymes used in the electron transport chain. It is named as such because the beta carbon of the fatty acid undergoes oxidation to a carbonyl group. Beta-oxidation is primarily facilitated by the mitochondrial trifunctional protein, an enzyme complex associated with the inner mitochondrial membrane, although very long chain fatty acids are oxidized in peroxisomes.

Fatty acid desaturases are a family of enzymes that convert saturated fatty acids into unsaturated fatty acids and polyunsaturated fatty acids. For the common fatty acids of the C18 variety, desaturases convert stearic acid into oleic acid. Other desaturases convert oleic acid into linolenic acid, which is the precursor to alpha-linolenic acid, gamma-linolenic acid, and eicosatrienoic acid.

<span class="mw-page-title-main">Acyl-CoA</span>

Acyl-CoA is a group of coenzymes that metabolize fatty acids. Acyl-CoA's are susceptible to beta oxidation, forming, ultimately, acetyl-CoA. The acetyl-CoA enters the citric acid cycle, eventually forming several equivalents of ATP. In this way, fats are converted to ATP, the universal biochemical energy carrier.

In biochemistry, fatty acid synthesis is the creation of fatty acids from acetyl-CoA and NADPH through the action of enzymes called fatty acid synthases. This process takes place in the cytoplasm of the cell. Most of the acetyl-CoA which is converted into fatty acids is derived from carbohydrates via the glycolytic pathway. The glycolytic pathway also provides the glycerol with which three fatty acids can combine to form triglycerides, the final product of the lipogenic process. When only two fatty acids combine with glycerol and the third alcohol group is phosphorylated with a group such as phosphatidylcholine, a phospholipid is formed. Phospholipids form the bulk of the lipid bilayers that make up cell membranes and surrounds the organelles within the cells.

In enzymology, a phosphatidylcholine desaturase (EC 1.14.19.22, previously EC 1.3.1.35) is an enzyme that catalyzes the chemical reaction

<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 Delta12-fatty acid dehydrogenase (EC 1.14.99.33) 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">FADS2</span>

Fatty acid desaturase 2 (FADS2) is encoded by the FADS2 gene, the associated enzyme is sometimes known as FADS2 as well. Its main associated enzyme is Delta 6 desaturase (D6D) however the human enzyme was shown to also catalyze some delta-8 and delta-4 desaturation reactions despite naming conventions.

Palmitoyl-CoA hydrolase (EC 3.1.2.2) is an enzyme in the family of hydrolases that specifically acts on thioester bonds. It catalyzes the hydrolysis of long chain fatty acyl thioesters of acyl carrier protein or coenzyme A to form free fatty acid and the corresponding thiol:

<span class="mw-page-title-main">ACOT2</span> Protein-coding gene in the species Homo sapiens

Acyl-CoA thioesterase 2, also known as ACOT2, is an enzyme which in humans is encoded by the ACOT2 gene.

<span class="mw-page-title-main">ACOT6</span> Protein-coding gene in the species Homo sapiens

Acyl-CoA thioesterase 6 is a protein that in humans is encoded by the ACOT6 gene. The protein, also known as C14orf42, is an enzyme with thioesterase activity.

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

Stearoyl-CoA is a coenzyme involved in the metabolism of fatty acids. Stearoyl-CoA is an 18-carbon long fatty acyl-CoA chain that participates in an unsaturation reaction. The reaction is catalyzed by the enzyme stearoyl-CoA desaturase, which is located in the endoplasmic reticulum. It forms a cis-double bond between the ninth and tenth carbons within the chain to form the product oleoyl-CoA.

<span class="mw-page-title-main">Acyl-CoA thioesterase 9</span> Protein-coding gene in humans

Acyl-CoA thioesterase 9 is a protein that is encoded by the human ACOT9 gene. It is a member of the acyl-CoA thioesterase superfamily, which is a group of enzymes that hydrolyze Coenzyme A esters. There is no known function, however it has been shown to act as a long-chain thioesterase at low concentrations, and a short-chain thioesterase at high concentrations.

<i>N</i>-Acylamides

N-acyl amides are a general class of endogenous fatty acid compounds characterized by a fatty acyl group linked to a primary amine metabolite by an amide bond. Broadly speaking, N-acyl amides fall into several categories: amino acid conjugates, neurotransmitter conjugates, ethanolamine conjugates, and taurine conjugates. N-acyl amides have pleiotropic signaling functions in physiology, including in cardiovascular function, metabolic homeostasis, memory, cognition, pain, motor control and others. Initial attention focused on N-acyl amides present in mammalian organisms, however recently lipid signaling systems consisting of N-acyl amides have also been found to be present in invertebrates, such as Drosophila melanogaster. N-acyl amides play important roles in many biochemical pathways involved in a variety of physiological and pathological processes, as well as the metabolic enzymes, transporters, and receptors that regulate their signaling.

<span class="mw-page-title-main">ACOT13</span> Protein-coding gene in the species Homo sapiens

Acyl-CoA thioesterase 13 is a protein that in humans is encoded by the ACOT13 gene. This gene encodes a member of the thioesterase superfamily. In humans, the protein co-localizes with microtubules and is essential for sustained cell proliferation.

<span class="mw-page-title-main">Rodolfo Brenner</span> Argentine biochemist

Rodolfo Roberto Brenner was an Argentine emeritus professor of chemistry. He was the founder and director of the Institute of Biochemical Research of La Plata and the co-founder of the Argentine Society for Biochemical Research.

References

  1. Borgeson CE, de Renobales M, Blomquist GJ (November 1990). "Characterization of the delta 12 desaturase in the American cockroach, Periplaneta americana: the nature of the substrate". Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism. 1047 (2): 135–40. doi:10.1016/0005-2760(90)90039-z. PMID   2248971.
  2. Jurenka RA (June 1997). "Biosynthetic pathway for producing the sex pheromone component (Z,E)-9,12-tetradecadienyl acetate in moths involves a delta 12 desaturase". Cellular and Molecular Life Sciences. 53 (6): 501–5. doi:10.1007/s000180050062. PMID   9230926. S2CID   20152524.
  3. Lomascolo A, Dubreucq E, Galzy P (March 1996). "Study of the delta 12-desaturase system of Lipomyces starkeyi". Lipids. 31 (3): 253–9. doi:10.1007/bf02529871. PMID   8900454. S2CID   27459395.
  4. Tocher DR, Leaver MJ, Hodgson PA (1998). "Recent advances in the biochemistry and molecular biology of fatty acyl desaturases". Progress in Lipid Research. 37 (2–3): 73–117. doi:10.1016/s0163-7827(98)00005-8. PMID   9829122.