• For detailed information about 2-methyl-branched-chain-enoyl-CoA reductase, go to the full flat file . (brenda-enzymes.org)
  • A novel prokaryotic trans-2-enoyl-CoA reductase from the spirochete Treponema denticola. (bvsalud.org)
  • An NADH -dependent trans-2-enoyl- CoA reductase (EC1.1.1.36) from the Gram negative spirochete Treponema denticola was identified, expressed and biochemically characterized. (bvsalud.org)
  • This NADH -dependent trans-2-enoyl- CoA reductase represents the first enzymatically characterized member of a prokaryotic protein family involved in a fatty acid synthesis pathway that is distinct from the familiar fatty acid synthase system. (bvsalud.org)
  • PECR (Peroxisomal Trans-2-Enoyl-CoA Reductase) is a Protein Coding gene. (thermofisher.com)
  • BbsH, a member of the enoyl-CoA hydratase family, converts (E)-benzylidenesuccinyl-CoA to 2-(α-hydroxybenzyl)succinyl-CoA and was subsequently used in a coupled enzyme assay with BbsCD, which belongs to the short-chain dehydrogenases/reductase (SDR) family. (nih.gov)
  • Enoyl-CoA isomerase is involved in the beta-oxidation, one of the most frequently used pathways in fatty acid degradation, of unsaturated fatty acids with double bonds at odd-numbered carbon positions. (wikipedia.org)
  • Since the key step in the degradation of fatty acids with double bonds at even-numbered carbon positions also produces 3-trans-enoyl-CoA in mammals and yeasts, enoyl-CoA isomerase is technically required for their metabolism as well. (wikipedia.org)
  • The reaction mechanism is detailed in figure 1, and the base that initiates the isomerization and NH groups that stabilize the intermediate are located on the active site of enoyl-coA isomerase. (wikipedia.org)
  • As it functions in the step immediately preceding the actual beta-oxidation and forms a double bond extending from the beta-carbon (position 2), enoyl-CoA isomerase is involved in both the NADPH-dependent and NADPH-independent pathways of beta-oxidation. (wikipedia.org)
  • There are two divisions among the mitochondrial enoyl Co-A isomerase: short-chain and long-chain [4]. (wikipedia.org)
  • In an immunoblot, antibodies were run against all enoyl CoA isomerase. (wikipedia.org)
  • Thus, the discovery of three sub-classes of enoyl CoA isomerase was made. (wikipedia.org)
  • Mitochondria (both short- and long-chain) of rat liver contain more than one enoyl Co-A isomerase. (wikipedia.org)
  • To begin with, the peroxisomes of rat liver are a multifunctional enzyme including enoyl-CoA isomerase, enoyl-CoA hydratase, and L-(−)-3-hydroxyacyl-CoA dehydrogenase. (wikipedia.org)
  • delta3,5-delta2,4-dienoyl-CoA isomerase/ e. (cornell.edu)
  • The multifunctional enzymes are found in bacteria and in the peroxisomes of some eukaryotes, but they serve two functions: the N-terminal domain works the same as the other classes of enoyl-CoA isomerases and the C-terminal domain works as a dehydrogenase, specifically, to 3-hydroxyactyl-CoA. (wikipedia.org)
  • The dehydrogenase activity of enoyl-CoA occurs in the carboxyl-terminal. (wikipedia.org)
  • 3-hydroxyacyl-CoA dehydrogenase/ enoyl-CoA hydratase [Arabidopsis thaliana] >gi6728. (cornell.edu)
  • In 1983, Gregersen et al demonstrated a medium-chain acyl-coenzyme A (CoA) dehydrogenase (MCAD) deficiency in a patient with hypoketotic hypoglycemia. (medscape.com)
  • Entry into the beta-oxidation cycle requires the action of acyl-CoA dehydrogenase, the first enzyme in the sequence, which removes electrons from the alpha-carbon and the beta-carbon, introducing a double bond. (medscape.com)
  • This study characterizes two enzymes of this pathway, (E)-benzylidenesuccinyl-CoA hydratase (BbsH), and (S,R)-2-(α-hydroxybenzyl)succinyl-CoA dehydrogenase (BbsCD) from Thauera aromatica. (nih.gov)
  • acyl-CoA dehydrogenase very l. (gsea-msigdb.org)
  • This bacterial enzyme catalyzes the reduction of either (2E,4E)-2,4- dienoyl-CoA or (2E,4Z)-2,4-dienoyl-CoA to (2E)-2-enoyl-CoA. (expasy.org)
  • The recombinant protein is a monomeric enzyme with a molecular mass of 44 kDa with a specific activity of 43+/-4.8 U/mg (micromol mg(-1)min(-1)) and K(m) value of 2.7 microM for crotonoyl- CoA . (bvsalud.org)
  • The AUH gene provides instructions for producing an enzyme called 3-methylglutaconyl-CoA hydratase. (medlineplus.gov)
  • The enzyme converts a molecule called 3-methylglutaconyl-CoA into another molecule called 3-hydroxy-3-methylglutaryl-CoA. (medlineplus.gov)
  • The mutations that cause this condition lead to an absence of 3-methylglutaconyl-CoA hydratase enzyme activity. (medlineplus.gov)
  • Background Enoyl-CoA hydratase short-chain 1 (ECHS1) is an enzyme involved in the metabolism of branched chain amino acids and fatty acids. (mendeley.com)
  • The crystal structure of rat liver mitochondrial enoyl-coenzyme A (CoA) hydratase complexed with the potent inhibitor acetoacetyl-CoA has been refined at 2.5 angstroms resolution. (rcsb.org)
  • Upon further investigation of the CoA binding site on the amino-terminal half of the multifunctional protein, the CoA substrate is not transferred through the aqueous phase from the isomerization phase to the site of hydration or does not have a bulk phase. (wikipedia.org)
  • Specifically, 3-methylglutaconyl-CoA hydratase is responsible for the fifth step in breaking down the protein building block (amino acid) leucine. (medlineplus.gov)
  • Kurimoto K, Fukai S, Nureki O, Muto Y, Yokoyama S. Crystal structure of human AUH protein, a single-stranded RNA binding homolog of enoyl-CoA hydratase. (medlineplus.gov)
  • Mutations in the ECHS1 gene lead to mitochondrial short-chain enoyl-CoA hydratase 1 deficiency, resulting in the accumulation of intermediates of valine. (mendeley.com)
  • This process is governed by the ER acetylation machinery: the cytosol:ER-lumen acetyl-CoA transporter AT-1 (also known as SLC33A1), and the ER-resident lysine acetyltransferases ATase1 and ATase2 (also known as NAT8B and NAT8, respectively). (biologists.com)
  • Cleavage of the 3-keto compound at the now unstable alpha-beta carbon bond and transfer of another CoA moiety to the new fragment results in 2 products: acetyl-CoA, composed of the carbonyl and original alpha-carbon from the starting molecule, and a new fatty acyl-CoA that is 2 carbons shorter than the original molecule. (medscape.com)
  • Oxidation of the hydroxyl substituent group on the beta-carbon creates an inherently unstable beta-ketoacyl-CoA compound. (medscape.com)
  • Enzymatic indicators of peroxisome proliferation (KCN-insensitive palmitoyl-CoA oxidation or enoyl-CoA hydratase heat labile activity) were not significantly altered compared to controls. (cdc.gov)
  • We demonstrate that ChsH1-ChsH2 catalyzes the hydration of a steroid enoyl-CoA, 3-oxo-4,17-pregnadiene-20-carboxyl-CoA, in the modified β-oxidation pathway for cholesterol side chain degradation. (rhea-db.org)
  • At the beginning of this reaction, 1 molecule of 'H2O', and 1 molecule of 'trans-Oct-2-enoyl-CoA' are present. (reactome.org)
  • At the end of this reaction, 1 molecule of '(S)-Hydroxyoctanoyl-CoA' is present. (reactome.org)
  • In the cytosol, a saturated, straight-chain fatty acid molecule with no double bonds is activated by the action of fatty acyl-CoA synthetase to form its corresponding acyl-CoA. (medscape.com)
  • Once inside the mitochondrion, the action of CPT II at the inner surface of the membrane releases free carnitine, which exits to the cytosol and leaves behind the acyl-CoA molecule. (medscape.com)
  • The next step is the introduction of a water molecule and resaturation of the double bond to form fatty enoyl-CoA. (medscape.com)
  • Enoyl-CoA isomerases can be categorized into three classes: monofunctional mitochondrial monofunctional peroxisomal multifunctional The monofunctional mitochondrial and peroxisomal enzymes are found in the mitochondria and peroxisomes of eukaryotes, respectively. (wikipedia.org)
  • It also acts as a catalyst for the formation of 3-ketoacyl-CoA intermediates from both straight-chain and 2-methyl-branched-chain fatty acids. (nih.gov)
  • FAE ( Fatty Acid Elongation ) like genes take part in the biosynthesis of VLCFAs, growth regulation, and stress responses, and are further comprised of KCS ( Ketoacyl-CoA synthase ) and ELO ( Elongation Defective Elongase ) sub-gene families. (nature.com)
  • It does so by shifting the position of the double bonds in the acyl-CoA intermediates and converting 3-cis or trans-enoyl-CoA to 2-trans-enoyl-CoA. (wikipedia.org)
  • Short-chain enoyl-CoA hydratases are sometimes given EC 4.2.1.17 instead, so those are ignored. (lbl.gov)
  • Enoyl-CoA hydratase is a hexamer of six identical subunits of 161 kDa molecular mass for the complex. (rcsb.org)
  • Comment: Psest_2437 (GFF2389) is the enoyl-CoA hydrotase for both isoleucine and valine degradation, which implies that (S)-3-hydroxybutanoyl-CoA is a substrate. (lbl.gov)
  • This acyl-CoA is linked to carnitine by the action of CPT I, with simultaneous transport across the mitochondrial membrane barrier. (medscape.com)
  • Variants in the ethylmalonyl-CoA decarboxylase (ECHDC1) gene: a novel player in ethylmalonic aciduria? (nih.gov)
  • At least 11 mutations in the AUH gene have been found to cause 3-methylglutaconyl-CoA hydratase deficiency. (medlineplus.gov)
  • Researchers speculate that an accumulation of these acids in the fluid that surrounds and protects the brain and spinal cord (the cerebrospinal fluid or CSF) can damage these structures and contribute to the neurological features of 3-methylglutaconyl-CoA hydratase deficiency. (medlineplus.gov)
  • The enzymes from the plants Ruta graveolens and Ipomoea batatas also act on trans -feruloyl-CoA ( cf . (enzyme-database.org)
  • On the other hand, the cotyledons convert long-chain 3-trans-enoyl-CoA, long-chain 3-cis-enoyl-CoA, and short-chain 3-cis-enoyl-CoA species into their 2- trans-enoyl-CoA respective forms. (wikipedia.org)
  • Here we report the first structure of a heterotetrameric MaoC-like enoyl-CoA hydratase, ChsH1-ChsH2, which is encoded by two adjacent genes from the igr operon. (rhea-db.org)
  • The product spontaneously undergoes trans -cis isomerization followed by lactonization and cyclization, liberating CoA and forming umbelliferone. (enzyme-database.org)