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Gene Review

Echs1  -  enoyl CoA hydratase, short chain, 1,...

Rattus norvegicus

Synonyms: Enoyl-CoA hydratase 1, Enoyl-CoA hydratase, mitochondrial, SCEH, Short-chain enoyl-CoA hydratase
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Disease relevance of Echs1

  • This dehydratase catalyzes the reversible dehydration of D-3-hydroxyacyl-CoA to 2-trans-enoyl-CoA, but, in contrast to enoyl-CoA hydratase, does not act on 2-cis-enoyl-CoA [1].
  • Rates of the NAD+-dependent oxidation of 2-trans,4-trans-decadienoyl-CoA, a metabolite of trans-omega-6-unsaturated fatty acids, catalyzed by the mitochondrial enoyl-CoA hydratase plus 3-hydroxyacyl-CoA dehydrogenase and by the corresponding enzymes from peroxisomes, as well as Escherichia coli, were compared [2].
  • ECH and other peroxisomal enzymes such as acyl CoA oxidase, catalase and carnitine-dependent acetyltransferase were also either not or only weakly expressed in most hepatic hyperplastic nodules and hepatomas induced by ciprofibrate (0.025% in diet), Wy-14,643 (0.1%) or BR-931 (0.2%), while being strongly induced in surrounding hepatocytes [3].
  • A 257-amino acid (aa) open reading frame in the photosynthetic bacterium, Rhodobacter capsulatus, shows significant homology to the mitochondrial enoyl-CoA hydratase (290 aa) [4].
  • Total peroxisomal beta-oxidation was decreased in a dose-related manner, whereas the liver to body weight ratio and the activities of individual enzymes comprising the peroxisomal beta-oxidation system, namely fatty acyl-CoA oxidase, enoyl-CoA hydratase, 3-hydroxy-acyl-CoA dehydrogenase, and thiolase, were increased [5].

High impact information on Echs1

  • The liganded PPAR alpha-PRIC complex enhanced transcription from a peroxisomal enoyl-CoA hydratase/l-3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme gene promoter template that contains peroxisome proliferator response elements [6].
  • T3 inhibited ciprofibrate-induced luciferase activity as well as the endogenous peroxisomal beta-oxidation enzymes in transgenic mice carrying a 3.2-kb 5'-flanking region of the rat peroxisomal enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase gene fused to the coding region of luciferase [7].
  • To identify cis-acting promoter elements involved in this induction, 5.8 kilobase pairs of promoter sequence from the gene encoding rat peroxisomal enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase (EC was inserted upstream of a luciferase reporter gene [8].
  • The genes encoding the first two enzymes of the peroxisomal beta-oxidation pathway, acyl-CoA oxidase (AOx) and enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase (HD), contain upstream cis-acting regulatory regions termed peroxisome proliferator response elements (PPRE) [9].
  • The peroxisome proliferator response element of the gene encoding the peroxisomal beta-oxidation enzyme enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase is a target for constitutive androstane receptor beta/9-cis-retinoic acid receptor-mediated transactivation [9].

Chemical compound and disease context of Echs1

  • In addition, benzotript inhibits the activities of multifunctional enzymes having similar structures, such as the peroxisomal enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase bifunctional protein and the Pseudomonas fragi fatty acid oxidation enzyme complex [10].

Biological context of Echs1

  • The extraordinarily high efficiencies of these two multifunctional proteins in catalyzing the degradation of 2-trans,4-trans-decadienoyl-CoA is best explained by the direct transfer of the 3-hydroxy-4-trans-decenoyl-CoA intermediate from the active site of enoyl-CoA hydratase to that of 3-hydroxyacyl-CoA dehydrogenase [2].
  • Based on the data plus our unpublished findings (N. Ishii, T. Osumi, and T. Hashimoto, unpublished data), we propose that the amino-terminal domain, which is principally encoded by Exons I-V, has enoyl-CoA hydratase activity, and the carboxyl-terminal one, which is mainly coded for by Exon VII, has a 3-hydroxyacyl-CoA dehydrogenase function [11].
  • The deduced amino acid sequence of p79 reveals high similarity to those of gastrin-binding protein and mitochondrial enoyl-CoA hydratase/hydroxyacyl-CoA dehydrogenase. p46 is similar to mitochondrial ketoacyl-CoA thiolase [12].
  • At the second step of beta-oxidation, catalysed by enoyl-CoA hydratase, enzyme kinetics were similar using either decenoyl-CoA or 5-hydroxydecenoyl-CoA as substrate [13].
  • Effect of mutagenesis on the stereochemistry of enoyl-CoA hydratase [14].

Anatomical context of Echs1


Associations of Echs1 with chemical compounds

  • PPRE of the rat enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase (HD) gene has previously been shown to consist of three imperfect TGACCT half-sites and form two distinct complexes (C1 and C2) with the nuclear extracts from H4IIEC3 cells [20].
  • A direct effect of pyruvate on palmitoyl-CoA oxidase and enoyl-CoA hydratase was excluded by measuring those enzymes individually in separate assays [21].
  • Alteration in glutathione S-transferase (GST) isoenzymes was compared with that of a peroxisomal enzyme, enoyl-CoA hydratase (ECH), during hepatocarcinogenesis caused by clofibrate (CF) administration in male Sprague-Dawley rats [22].
  • The enzymes studied were the palmitoyl-CoA, octanoyl-CoA, butyryl-CoA, glutaryl-CoA, and 3-hydroxyacyl-CoA dehydrogenases, the enoyl-CoA hydratase (crotonase), and the C4- and C10-thiolases [23].
  • Members of the enoyl-CoA hydratase (crotonase) superfamily catalyze different overall reactions that utilize a common catalytic strategy delivered by a shared structural scaffold; the substrates are usually acyl esters of coenzyme A, and the intermediates are usually thioester enolate anions stabilized by a conserved oxyanion hole [24].

Enzymatic interactions of Echs1


Other interactions of Echs1


Analytical, diagnostic and therapeutic context of Echs1


  1. D-3-hydroxyacyl coenzyme A dehydratase from rat liver peroxisomes. Purification and characterization of a novel enzyme necessary for the epimerization of 3-hydroxyacyl-CoA thioesters. Li, J.X., Smeland, T.E., Schulz, H. J. Biol. Chem. (1990) [Pubmed]
  2. Channeling of 3-hydroxy-4-trans-decenoyl coenzyme A on the bifunctional beta-oxidation enzyme from rat liver peroxisomes and on the large subunit of the fatty acid oxidation complex from Escherichia coli. Yang, S.Y., Cuebas, D., Schulz, H. J. Biol. Chem. (1986) [Pubmed]
  3. Loss of peroxisomal enzyme expression in preneoplastic and neoplastic lesions induced by peroxisome proliferators in rat livers. Yokoyama, Y., Tsuchida, S., Hatayama, I., Satoh, K., Narita, T., Rao, M.S., Reddy, J.K., Yamada, J., Suga, T., Sato, K. Carcinogenesis (1992) [Pubmed]
  4. A bacterial homolog to the mitochondrial enoyl-CoA hydratase. Beckman, D.L., Kranz, R.G. Gene (1991) [Pubmed]
  5. Dose-related effects of perfluorodecanoic acid on growth, feed intake and hepatic peroxisomal beta-oxidation. Borges, T., Robertson, L.W., Peterson, R.E., Glauert, H.P. Arch. Toxicol. (1992) [Pubmed]
  6. Identification of a transcriptionally active peroxisome proliferator-activated receptor alpha -interacting cofactor complex in rat liver and characterization of PRIC285 as a coactivator. Surapureddi, S., Yu, S., Bu, H., Hashimoto, T., Yeldandi, A.V., Kashireddy, P., Cherkaoui-Malki, M., Qi, C., Zhu, Y.J., Rao, M.S., Reddy, J.K. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  7. Thyroid hormone (T3) inhibits ciprofibrate-induced transcription of genes encoding beta-oxidation enzymes: cross talk between peroxisome proliferator and T3 signaling pathways. Chu, R., Madison, L.D., Lin, Y., Kopp, P., Rao, M.S., Jameson, J.L., Reddy, J.K. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  8. Identification of a peroxisome proliferator-responsive element upstream of the gene encoding rat peroxisomal enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase. Zhang, B., Marcus, S.L., Sajjadi, F.G., Alvares, K., Reddy, J.K., Subramani, S., Rachubinski, R.A., Capone, J.P. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  9. The peroxisome proliferator response element of the gene encoding the peroxisomal beta-oxidation enzyme enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase is a target for constitutive androstane receptor beta/9-cis-retinoic acid receptor-mediated transactivation. Kassam, A., Winrow, C.J., Fernandez-Rachubinski, F., Capone, J.P., Rachubinski, R.A. J. Biol. Chem. (2000) [Pubmed]
  10. A new inhibitor of mitochondrial fatty acid oxidation. Hashimoto, T., Shindo, Y., Souri, M., Baldwin, G.S. J. Biochem. (1996) [Pubmed]
  11. Structural organization of the gene for rat enoyl-CoA hydratase:3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme. Ishii, N., Hijikata, M., Osumi, T., Hashimoto, T. J. Biol. Chem. (1987) [Pubmed]
  12. Identification and characterization of an intracellular protein complex that binds fibroblast growth factor-2 in bovine brain. Chevet, E., Lemaître, G., Cailleret, K., Dahan, S., Bergeron, J.J., Katinka, M.D. Biochem. J. (1999) [Pubmed]
  13. 5-Hydroxydecanoate is metabolised in mitochondria and creates a rate-limiting bottleneck for beta-oxidation of fatty acids. Hanley, P.J., Dröse, S., Brandt, U., Lareau, R.A., Banerjee, A.L., Srivastava, D.K., Banaszak, L.J., Barycki, J.J., Van Veldhoven, P.P., Daut, J. J. Physiol. (Lond.) (2005) [Pubmed]
  14. Effect of mutagenesis on the stereochemistry of enoyl-CoA hydratase. Feng, Y., Hofstein, H.A., Zwahlen, J., Tonge, P.J. Biochemistry (2002) [Pubmed]
  15. Different susceptibility to peroxisome proliferator-induced hepatocarcinogenesis in rats with polymorphic glutathione transferase genes. Kudo, T., Asano, J., Shimizu, T., Nanashima, N., Fan, Y., Akita, M., Ookawa, K., Hayakari, M., Yokoyama, Y., Suto, K., Tsuchida, S. Cancer Sci. (2006) [Pubmed]
  16. Molecular cloning of the cDNAs for the subunits of rat mitochondrial fatty acid beta-oxidation multienzyme complex. Structural and functional relationships to other mitochondrial and peroxisomal beta-oxidation enzymes. Kamijo, T., Aoyama, T., Miyazaki, J., Hashimoto, T. J. Biol. Chem. (1993) [Pubmed]
  17. Changes in the activities of the enzymes of hepatic fatty acid oxidation during development of the rat. Foster, P.C., Bailey, E. Biochem. J. (1976) [Pubmed]
  18. Immunochemical visualization and identification of rat liver proteins adducted by 2,6-di-tert-butyl-4-methylphenol (BHT). Reed, M., Thompson, D.C. Chem. Res. Toxicol. (1997) [Pubmed]
  19. Immunocytochemical localization of fatty acid metabolizing heat-stable and heat-labile enoyl-coenzyme A (CoA) hydratases in liver and renal cortex. Bendayan, M., Reddy, M.K., Hashimoto, T., Reddy, J.K. J. Histochem. Cytochem. (1983) [Pubmed]
  20. Cooperative formation of higher order peroxisome proliferator-activated receptor and retinoid X receptor complexes on the peroxisome proliferator responsive element of the rat hydratase-dehydrogenase gene. Chu, R., Lin, Y., Rao, M.S., Reddy, J.K. J. Biol. Chem. (1995) [Pubmed]
  21. L-lactate dehydrogenase A4- and A3B isoforms are bona fide peroxisomal enzymes in rat liver. Evidence for involvement in intraperoxisomal NADH reoxidation. Baumgart, E., Fahimi, H.D., Stich, A., Völkl, A. J. Biol. Chem. (1996) [Pubmed]
  22. Decreased expression of glutathione S-transferases and increased fatty change in peroxisomal enzyme-negative foci induced by clofibrate in rat livers. Nishimura, S., Yokoyama, Y., Nakano, H., Satoh, K., Kano, H., Sato, K., Tsuchida, S. Carcinogenesis (1995) [Pubmed]
  23. Enzymes of fatty acid beta-oxidation in developing brain. Reichmann, H., Maltese, W.A., DeVivo, D.C. J. Neurochem. (1988) [Pubmed]
  24. Evolution of function in the crotonase superfamily: (3S)-methylglutaconyl-CoA hydratase from Pseudomonas putida. Wong, B.J., Gerlt, J.A. Biochemistry (2004) [Pubmed]
  25. The 3-hydroxyacyl-CoA epimerase activity of rat liver peroxisomes is due to the combined actions of two enoyl-CoA hydratases: a revision of the epimerase-dependent pathway of unsaturated fatty acid oxidation. Smeland, T.E., Li, J.X., Chu, C.H., Cuebas, D., Schulz, H. Biochem. Biophys. Res. Commun. (1989) [Pubmed]
  26. Induction of hepatic peroxisome proliferation in nonrodent species, including primates. Reddy, J.K., Lalwani, N.D., Qureshi, S.A., Reddy, M.K., Moehle, C.M. Am. J. Pathol. (1984) [Pubmed]
  27. Lack of peroxisomal enzyme inducibility in rat hepatic preneoplastic lesions induced by mutagenic carcinogens: contrasted expression of glutathione S-transferase P form and enoyl CoA hydratase. Yokoyama, Y., Tsuchida, S., Hatayama, I., Sato, K. Carcinogenesis (1993) [Pubmed]
  28. Gene expression profiling reveals multiple toxicity endpoints induced by hepatotoxicants. Huang, Q., Jin, X., Gaillard, E.T., Knight, B.L., Pack, F.D., Stoltz, J.H., Jayadev, S., Blanchard, K.T. Mutat. Res. (2004) [Pubmed]
  29. Changes induced by oxygen in rat liver proteins identified by high-resolution two-dimensional gel electrophoresis. Miralles, C., Agustí, A.G., Aubry, C., Sanchez, J.C., Walzer, C., Hochstrasser, D., Busquets, X. Eur. J. Biochem. (2000) [Pubmed]
  30. Peroxisome proliferator-activated receptor subtype-specific regulation of hepatic and peripheral gene expression in the Zucker diabetic fatty rat. Dana, S.L., Hoener, P.A., Bilakovics, J.M., Crombie, D.L., Ogilvie, K.M., Kauffman, R.F., Mukherjee, R., Paterniti, J.R. Metab. Clin. Exp. (2001) [Pubmed]
  31. Molecular cloning and sequence analysis of the cDNA for rat mitochondrial enoyl-CoA hydratase. Structural and evolutionary relationships linked to the bifunctional enzyme of the peroxisomal beta-oxidation system. Minami-Ishii, N., Taketani, S., Osumi, T., Hashimoto, T. Eur. J. Biochem. (1989) [Pubmed]
  32. Acyl-Coa oxidase and hydratase-dehydrogenase, two enzymes of the peroxisomal beta-oxidation system, are synthesized on free polysomes of clofibrate-treated rat liver. Rachubinski, R.A., Fujiki, Y., Mortensen, R.M., Lazarow, P.B. J. Cell Biol. (1984) [Pubmed]
  33. AUH, a gene encoding an AU-specific RNA binding protein with intrinsic enoyl-CoA hydratase activity. Nakagawa, J., Waldner, H., Meyer-Monard, S., Hofsteenge, J., Jenö, P., Moroni, C. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  34. Involvement of glycine 141 in substrate activation by enoyl-CoA hydratase. Bell, A.F., Wu, J., Feng, Y., Tonge, P.J. Biochemistry (2001) [Pubmed]
  35. Role of glutamate 144 and glutamate 164 in the catalytic mechanism of enoyl-CoA hydratase. Hofstein, H.A., Feng, Y., Anderson, V.E., Tonge, P.J. Biochemistry (1999) [Pubmed]
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