EC Number   |
General Information |
Reference |
|---|
    4.2.1.17 | evolution |
the crotonases comprise a widely distributed enzyme superfamily that has multiple roles in both primary and secondary metabolism. Enoyl-CoA hydratase (ECH) and enoyl-CoA isomerase (ECI) are prototypical crotonases. The term crotonase has been used to refer specifically to ECH, but it is also used to refer to the entirety of the superfamily of enzymes bearing the crotonase-type fold |
746582 |
| 4.2.1.17 | evolution |
the crotonases comprise a widely distributed enzyme superfamily that has multiple roles in both primary and secondary metabolism. Enoyl-CoA hydratase (ECH) and enoyl-CoA isomerase (ECI) are prototypical crotonases. The term crotonase has been used to refer specifically to ECH, but it is also used to refer to the entirety of the superfamily of enzymes bearing the crotonase-type fold. Some enzymes (e.g. rat peroxisomal multifunctional enzyme, type 1) have both ECH and ECI activities. These enzymes employ an active site with two glutamate residues. Rat mitochondrial ECH-1 (which has the two glutamate residues typical of ECH) has isomerase activity, albeit much lower than its hydratase activity. While the hydratase activity depends on both glutamate residues, the isomerase activity (as with dedicated ECI enzymes) relies mostly on a single glutamate |
746582 |
| 4.2.1.17 | evolution |
the crotonases comprise a widely distributed enzyme superfamily that has multiple roles in both primary and secondary metabolism. Enoyl-CoA hydratase (ECH) and enoyl-CoA isomerase (ECI) are prototypical crotonases. The term crotonase has been used to refer specifically to ECH, but it is also used to refer to the entirety of the superfamily of enzymes bearing the crotonase-type fold. Some enzymes, e.g. rat peroxisomal multifunctional enzyme, type 1, have both ECH and ECI activities. These enzymes employ an active site with two glutamate residues. Through the use of an additional domain, some multifunctional crotonase enzymes can also catalyze a further step in fatty acid catabolism, i.e. the oxidation of the enoyl-CoA hydratase product. While the hydratase activity depends on both glutamate residues, the isomerase activity (as with dedicated ECI enzymes) relies mostly on a single glutamate |
746582 |
| 4.2.1.17 | malfunction |
deficiency of the enzyme causes an early childhood Leigh syndrome phenotype. Two homozygous truncation mutations in ECHS1 in two siblings lead to development of lethal neonatal lactic acidosis, potential genotype/phenotype correlation, overview |
747603 |
| 4.2.1.17 | malfunction |
Ech1 shRNA interference decreases Hca-F cell proliferation and the in situ adhesive capacity of Hca-F cells to lymph nodes, phenotype, overview |
714400 |
| 4.2.1.17 | malfunction |
inactivation of dspI abolishes biofilm dispersion autoinduction in continuous cultures of Pseudommonas aeruginosa and results in biofilms that are significantly greater in thickness and biomass compared to the parental wild-type strain. But dispersion can be induced in dspI mutants by the exogenous addition of synthetic cis-2-decenoic acid or by complementation of DELTAdspI in trans under the control of an arabinose-inducible promoter |
729933 |
| 4.2.1.17 | malfunction |
mutations in ECHS1 result in short-chain enoyl-CoA hydratase (SCEH) deficiency which mainly affects the catabolism of various amino acids, particularly valine. Patients show a Leigh syndrome-like phenotype, important diagnostic markers for this disorder include S-(2-carboxypropyl)-L-cysteine and S-(2-carboxypropyl)cysteamine (which are derived from methacrylyl-CoA), S-(2-carboxyethyl)-L-cysteine and S-(2-carboxyethyl)cysteamine (which are derived from acryloyl-CoA), and 2-methyl-2,3-dihydroxybutyric acid (MDHB). In a lethal neonatal case, SCEH deficiency is confirmed with very low SCEH activity in fibroblasts and nearly absent immunoreactivity of SCEH. The patient has a severe neonatal course with elevated blood and cerebrospinal fluid (CSF) lactate and pyruvate concentrations, high plasma alanine and slightly low plasma cystine. 2-Methyl-2,3-dihydroxybutyric acid is markedly elevated as are metabolites of the three branched-chain ketoacids on urine organic acids analysis. These urine metabolites notably decrease when lactic acidosis decreases in blood. Lymphocyte pyruvate dehydrogenase complex (PDC) activity is deficient, but PDC and 2-oxoglutarate dehydrogenase complex activities in cultured fibroblasts are normal. Oxidative phosphorylation analysis on intact digitonin-permeabilized fibroblasts is suggestive of slightly reduced PDC activity relative to control range in mitochondria. Review of other cases of mutations with primary short-chain enoyl-CoA hydratase (SCEH) deficiency associated with secondary lymphocyte pyruvate dehydrogenase complex (PDC) deficiency, about half of cases with primary SCEH deficiency also exhibit secondary PDC deficiency, overview. To date, almost half of cases diagnosed with this autosomal recessive disorder perish within the neonatal or infantile period, but survival into adulthood is reported |
748661 |
| 4.2.1.17 | malfunction |
siRNA-mediated knockdown of ECHS1 in the murine hepatocyte cell line alpha mouse liver 12 demonstrate increased cellular lipid accumulation induced by free fatty acid overload. Administering ECHS1 siRNA specifically reduces the expression of ECHS1 protein in mice liver, which significantly exacerbates the hepatic steatosis induced by an high fat diet |
702229 |
| 4.2.1.17 | malfunction |
while mutation of Glu144 to alanine in this enzyme diminishes the isomerase activity by 10fold, mutation of Glu164 to alanine decreases the isomerase activity 1000fold, the hydratase activity is decreased 2000fold for both mutants |
746582 |
| 4.2.1.17 | metabolism |
short-chain enoyl-CoA hydratase (SCEH) is a mitochondrial enzyme involved in the oxidation of fatty acids and the catabolic pathway of valine and, to a lesser extent, isoleucine |
747603 |
