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Enoyl CoA hydratase, short chain, 1, mitochondrial

Enoyl-CoA Hydratase
The protein encoded by this gene functions in the second step of the mitochondrial fatty acid beta-oxidation pathway. It catalyzes the hydration of 2-trans-enoyl-coenzyme A (CoA) intermediates to L-3-hydroxyacyl-CoAs. The gene product is a member of the hydratase/isomerase superfamily. It localizes to the mitochondrial matrix. Transcript variants utilizing alternative transcription initiation sites have been described in the literature. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, CAN, catalase, V1a, HAD
Papers on Enoyl-CoA Hydratase
Ethylene and 1-MCP regulate major volatile biosynthetic pathways in apple fruit.
Zhang et al., Guangzhou, China. In Food Chem, Apr 2016
Genes related to fatty acid synthesis and metabolism, including acyl-carrier-proteins (ACPs), malonyl-CoA:ACP transacylase (MCAT), acyl-ACP-desaturase (ACPD), lipoxygenase (LOX), hydroperoxide lyase (HPL), alcohol dehydrogenase (ADH), pyruvate decarboxylase (PDC2), β-oxidation, acyl-CoA synthetase (ACS), enoyl-CoA hydratase (ECHD), acyl-CoA dehydrogenase (ACAD), and alcohol acyltransferases (AATs) also increased during ripening and in response to ethylene treatment.
Biosynthetic pathway for acrylic acid from glycerol in recombinant Escherichia coli.
Zhao et al., Qingdao, China. In Appl Microbiol Biotechnol, Feb 2016
The acrylate production was improved by screening and site-directed mutagenesis of key enzyme enoyl-CoA hydratase and chromosomal integration of some exogenous genes.
Metabolic switch during adipogenesis: From branched chain amino acid catabolism to lipid synthesis.
Adamski et al., München, Germany. In Arch Biochem Biophys, Feb 2016
Our further analysis led to identification of an enzymatic switch comprising the enzymes Hmgcs2 (3-hydroxy-3-methylglutaryl-CoA synthase) and Auh (AU RNA binding protein/enoyl-CoA hydratase) which connects leucine degradation with cholesterol synthesis.
Inhibition of mitochondrial β-oxidation by miR-107 promotes hepatic lipid accumulation and impairs glucose tolerance in vivo.
Datta et al., Delhi, India. In Int J Obes (lond), Nov 2015
Cells were treated with tunicamycin (Tm, 1 h) and 4-PBA (4-phenyl butyric acid, 8 h) or transfected with hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase, apha subunit (HADHA) short interfering RNA or its overexpression vector.
Clinical, biochemical and metabolic characterisation of a mild form of human short-chain enoyl-CoA hydratase deficiency: significance of increased N-acetyl-S-(2-carboxypropyl)cysteine excretion.
Wakamatsu et al., Kasugai, Japan. In J Med Genet, Oct 2015
BACKGROUND: Short-chain enoyl-CoA hydratase-ECHS1-catalyses many metabolic pathways, including mitochondrial short-chain fatty acid β-oxidation and branched-chain amino acid catabolic pathways; however, the metabolic products essential for the diagnosis of ECHS1 deficiency have not yet been determined.
Whole-exome sequencing identifies novel ECHS1 mutations in Leigh syndrome.
Majewski et al., Montréal, Canada. In Hum Genet, Sep 2015
Compound heterozygote variants in ECHS1, encoding the enzyme enoyl-CoA hydratase were identified.
Enoyl-coenzyme A hydratase in cancer.
Tang et al., Dalian, China. In Clin Chim Acta, Sep 2015
Enoyl-CoA hydratase (Ech) catalyzes the second step in the physiologically important beta-oxidation pathway of fatty acid metabolism.
Clinical and biochemical characterization of four patients with mutations in ECHS1.
Wanders et al., Amsterdam, Netherlands. In Orphanet J Rare Dis, 2014
BACKGROUND: Short-chain enoyl-CoA hydratase (SCEH, encoded by ECHS1) catalyzes hydration of 2-trans-enoyl-CoAs to 3(S)-hydroxy-acyl-CoAs. SCEH has a broad substrate specificity and is believed to play an important role in mitochondrial fatty acid oxidation and in the metabolism of branched-chain amino acids.
Silencing ECHS1 attenuates the proliferation and induces the autophagy of hepatocellular carcinoma via impairing cell metabolism and activating AMPK.
Ren et al., In Neoplasma, 2014
Our previous study showed Short chain enoyl-CoA hydratase (ECHS1) could bind to HBsAg (HBs) and that ECHS1's localization in mitochondria induced HepG2 cell apoptosis.
[Roles of metabolic compartmentalization by astrocytes and neurons in the pathophysiology and treatment of Parkinson's disease].
Suzuki et al., In Brain Nerve, 2013
In addition to the allosteric regulation of the PPP, which is associated with the activation of glycolysis, the PPP in astroglia can also be activated by ROS through the Kelch-like enoyl-CoA hydratase-associated protein 1 (Keap1)/nuclear factor-erythroid 2 p45 subunit-related factor 2 (Nrf2) system.
Putting bioactivation reactions to work: Targeting antioxidants to mitochondria.
Anders, Rochester, United States. In Chem Biol Interact, 2011
Hence, 3-(2,6-dimethylphenoxy)acrylate was prepared; it was expected that, after conversion to its CoA thioester, 3-(2,6-dimethylphenoxy)acryloyl-CoA would be a substrate for enoyl-CoA hydratase.
Suppression of virus replication via down-modulation of mitochondrial short chain enoyl-CoA hydratase in human glioblastoma cells.
Takahashi et al., Tokyo, Japan. In Antiviral Res, 2007
Expression of mitochondrial short chain enoyl-CoA hydratase (ECHS)was significantly down-modulated in virus infected glioblastoma cells and ECHS knockdown (siRNA) impaired virus replication and cytopathic effects.
Enoyl-CoA hydratase. reaction, mechanism, and inhibition.
Liu et al., Austin, United States. In Bioorg Med Chem, 2003
Enoyl-CoA hydratase (ECH) catalyzes the second step in the physiologically important beta-oxidation pathway of fatty acid metabolism.
Clinical consequences of defects in peroxisomal beta-oxidation.
Clayton, London, United Kingdom. In Biochem Soc Trans, 2001
The disorders of peroxisomal beta-oxidation, which have been well characterised at the molecular level, include defects of acyl-CoA oxidase, defects of the D-bifunctional protein (D-BP) (including specific defects of its enoyl-CoA hydratase and D-3-hydroxyacyl-CoA dehydrogenase components), defects of the very-long-chain fatty acid (VLCFA)-CoA importer [X-linked adrenoleukodystrophy (ALD)] and alpha-methylacyl-CoA racemase deficiency.
The crotonase superfamily: divergently related enzymes that catalyze different reactions involving acyl coenzyme a thioesters.
Gerlt et al., Urbana, United States. In Acc Chem Res, 2001
The crotonase (or enoyl-CoA hydratase) superfamily is such an example whereby members catalyze a wide range of metabolic reactions but share a common structural solution to a mechanistic problem.
A fetal fatty-acid oxidation disorder as a cause of liver disease in pregnant women.
Strauss et al., Winston-Salem, United States. In N Engl J Med, 1999
This enzyme resides in the mitochondrial trifunctional protein, which also contains the active site of long-chain 2,3-enoyl-CoA hydratase and long-chain 3-ketoacyl-CoA thiolase.
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