Very-long-chain enoyl-CoA reductase

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Very-long-chain enoyl-CoA reductase
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EC no. 1.3.1.93
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Very-long-chain enoyl-CoA reductase (EC 1.3.1.93, TSC13 (gene name), CER10 (gene)) is an enzyme with systematic name very-long-chain acyl-CoA:NADP+ oxidoreductase. [1] [2] [3] [4] This enzyme catalyses the following chemical reaction

a very-long-chain acyl-CoA + NADP+ a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H+

This is the fourth component of the elongase, a microsomal protein complex responsible for extending palmitoyl-CoA and stearoyl-CoA.

Related Research Articles

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

Enoyl-CoA-(∆) isomerase (EC 5.3.3.8, also known as dodecenoyl-CoA- isomerase, 3,2-trans-enoyl-CoA isomerase, ∆3 ,∆2 -enoyl-CoA isomerase, or acetylene-allene isomerase, is an enzyme that catalyzes the conversion of cis- or trans-double bonds of coenzyme A bound fatty acids at gamma-carbon to trans double bonds at beta-carbon as below:

<span class="mw-page-title-main">Nicotinamide adenine dinucleotide phosphate</span> Chemical compound

Nicotinamide adenine dinucleotide phosphate, abbreviated NADP+ or, in older notation, TPN (triphosphopyridine nucleotide), is a cofactor used in anabolic reactions, such as the Calvin cycle and lipid and nucleic acid syntheses, which require NADPH as a reducing agent ('hydrogen source'). NADPH is the reduced form of NADP+, the oxidized form. NADP+ is used by all forms of cellular life.

<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.

<span class="mw-page-title-main">Enoyl-acyl carrier protein reductase</span> InterPro Family

Enoyl-acyl carrier protein reductase, is a key enzyme of the type II fatty acid synthesis (FAS) system. ENR is an attractive target for narrow-spectrum antibacterial drug discovery because of its essential role in metabolism and its sequence conservation across many bacterial species. In addition, the bacterial ENR sequence and structural organization are distinctly different from those of mammalian fatty acid biosynthesis enzymes.

<span class="mw-page-title-main">Fatty acid synthase</span> Class of enzymes

Fatty acid synthase (FAS) is an enzyme that in humans is encoded by the FASN gene.

<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.

<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">3-oxoacyl-(acyl-carrier-protein) reductase</span> Enzyme

In enzymology, a 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Acyl-CoA dehydrogenase (NADP+)</span> Class of enzymes

In enzymology, an acyl-CoA dehydrogenase (NADP+) (EC 1.3.1.8) is an enzyme that catalyzes the chemical reaction

In enzymology, an enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) (EC 1.3.1.39) is an enzyme that catalyzes the chemical reaction

In enzymology, an enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) (EC 1.3.1.10) is an enzyme that catalyzes the chemical reaction

In enzymology, a trans-2-enoyl-CoA reductase (NADPH) (EC 1.3.1.38) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Fatty-acyl-CoA synthase</span>

Fatty-acyl-CoA Synthase, or more commonly known as yeast fatty acid synthase, is an enzyme complex responsible for fatty acid biosynthesis, and is of Type I Fatty Acid Synthesis (FAS). Yeast fatty acid synthase plays a pivotal role in fatty acid synthesis. It is a 2.6 MDa barrel shaped complex and is composed of two, unique multi-functional subunits: alpha and beta. Together, the alpha and beta units are arranged in an α6β6 structure. The catalytic activities of this enzyme complex involves a coordination system of enzymatic reactions between the alpha and beta subunits. The enzyme complex therefore consists of six functional centers for fatty acid synthesis.

<span class="mw-page-title-main">HSD17B4</span> Protein-coding gene in the species Homo sapiens

D-bifunctional protein (DBP), also known as peroxisomal multifunctional enzyme type 2 (MFP-2), as well as 17β-hydroxysteroid dehydrogenase type IV is a protein that in humans is encoded by the HSD17B4 gene. It's an alcohol oxidoreductase, specifically 17β-Hydroxysteroid dehydrogenase. It is involved in fatty acid β-oxidation and steroid metabolism.

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

Trans-2,3-enoyl-CoA reductase is an enzyme that in humans is encoded by the TECR gene.

Very-long-chain 3-oxoacyl-CoA reductase (EC 1.1.1.330, very-long-chain 3-ketoacyl-CoA reductase, very-long-chain beta-ketoacyl-CoA reductase, KCR (gene), IFA38 (gene)) is an enzyme with systematic name (3R)-3-hydroxyacyl-CoA:NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction

Alcohol-forming fatty acyl-CoA reductase (EC 1.2.1.84, FAR (gene)) is an enzyme with systematic name long-chain acyl-CoA:NADPH reductase. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Short-chain acyl-CoA dehydrogenase</span>

Short-chain acyl-CoA dehydrogenase is an enzyme with systematic name short-chain acyl-CoA:electron-transfer flavoprotein 2,3-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

<span class="mw-page-title-main">Ketoacyl synthase</span> Catalyst for a key step in fatty acid synthesis

Ketoacyl synthases (KSs) catalyze the condensation reaction of acyl-CoA or acyl-acyl ACP with malonyl-CoA to form 3-ketoacyl-CoA or with malonyl-ACP to form 3-ketoacyl-ACP. This reaction is a key step in the fatty acid synthesis cycle, as the resulting acyl chain is two carbon atoms longer than before. KSs exist as individual enzymes, as they do in type II fatty acid synthesis and type II polyketide synthesis, or as domains in large multidomain enzymes, such as type I fatty acid synthases (FASs) and polyketide synthases (PKSs). KSs are divided into five families: KS1, KS2, KS3, KS4, and KS5.

References

  1. Kohlwein SD, Eder S, Oh CS, Martin CE, Gable K, Bacikova D, Dunn T (January 2001). "Tsc13p is required for fatty acid elongation and localizes to a novel structure at the nuclear-vacuolar interface in Saccharomyces cerevisiae". Molecular and Cellular Biology. 21 (1): 109–25. doi:10.1128/MCB.21.1.109-125.2001. PMC   88785 . PMID   11113186.
  2. Gable K, Garton S, Napier JA, Dunn TM (February 2004). "Functional characterization of the Arabidopsis thaliana orthologue of Tsc13p, the enoyl reductase of the yeast microsomal fatty acid elongating system". Journal of Experimental Botany. 55 (396): 543–5. doi: 10.1093/jxb/erh061 . PMID   14673020.
  3. Kvam E, Gable K, Dunn TM, Goldfarb DS (September 2005). "Targeting of Tsc13p to nucleus-vacuole junctions: a role for very-long-chain fatty acids in the biogenesis of microautophagic vesicles". Molecular Biology of the Cell. 16 (9): 3987–98. doi:10.1091/mbc.E05-04-0290. PMC   1196313 . PMID   15958487.
  4. Zheng H, Rowland O, Kunst L (May 2005). "Disruptions of the Arabidopsis Enoyl-CoA reductase gene reveal an essential role for very-long-chain fatty acid synthesis in cell expansion during plant morphogenesis". The Plant Cell. 17 (5): 1467–81. doi:10.1105/tpc.104.030155. PMC   1091768 . PMID   15829606.