ECH1

From Wikipedia, the free encyclopedia

Enoyl Coenzyme A hydratase 1, peroxisomal

Identifiers

ECH1; HPXEL

External IDs

OMIM: 600696 MGI: 1858208 HomoloGene: 1069

Gene ontology
Molecular Function:	• enoyl-CoA hydratase activity • isomerase activity
Cellular Component:	• mitochondrion • peroxisome
Biological Process:	• generation of precursor metabolites and energy • lipid metabolic process • fatty acid metabolic process • fatty acid beta-oxidation • metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001398 (mRNA)
NP_001389 (protein)

NM_016772 (mRNA)
NP_058052 (protein)

Location

Chr 19: 44 - 44.01 Mb

Chr 7: 28.53 - 28.54 Mb

Pubmed search

[1]

[2]

Enoyl Coenzyme A hydratase 1, peroxisomal, also known as ECH1, is a human gene.^[1]

This gene encodes a member of the hydratase/isomerase superfamily. The gene product shows high sequence similarity to enoyl-coenzyme A (CoA) hydratases of several species, particularly within a conserved domain characteristic of these proteins. The encoded protein, which contains a C-terminal peroxisomal targeting sequence, localizes to the peroxisome. The rat ortholog, which localizes to the matrix of both the peroxisome and mitochondria, can isomerize 3-trans,5-cis-dienoyl-CoA to 2-trans,4-trans-dienoyl-CoA, indicating that it is a delta3,5-delta2,4-dienoyl-CoA isomerase. This enzyme functions in the auxiliary step of the fatty acid beta-oxidation pathway. Expression of the rat gene is induced by peroxisome proliferators.^[1]

[edit] References

^ ^a ^b Entrez Gene: ECH1 enoyl Coenzyme A hydratase 1, peroxisomal.

[edit] Further reading

Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
Kovalyov LI, Kovalyova MA, Kovalyov PL, et al. (2006). "Polymorphism of delta3,5-delta2,4-dienoyl-coenzyme A isomerase (the ECH1 gene product protein) in human striated muscle tissue.". Biochemistry Mosc. 71 (4): 448–53. PMID 16615866.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Goehler H, Lalowski M, Stelzl U, et al. (2004). "A protein interaction network links GIT1, an enhancer of huntingtin aggregation, to Huntington's disease.". Mol. Cell 15 (6): 853–65. doi:10.1016/j.molcel.2004.09.016. PMID 15383276.
Jia Y, Qi C, Zhang Z, et al. (2004). "Overexpression of peroxisome proliferator-activated receptor-alpha (PPARalpha)-regulated genes in liver in the absence of peroxisome proliferation in mice deficient in both L- and D-forms of enoyl-CoA hydratase/dehydrogenase enzymes of peroxisomal beta-oxidation system.". J. Biol. Chem. 278 (47): 47232–9. doi:10.1074/jbc.M306363200. PMID 14500732.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Filppula SA, Yagi AI, Kilpeläinen SH, et al. (1998). "Delta3,5-delta2,4-dienoyl-CoA isomerase from rat liver. Molecular characterization.". J. Biol. Chem. 273 (1): 349–55. PMID 9417087.
FitzPatrick DR, Germain-Lee E, Valle D (1995). "Isolation and characterization of rat and human cDNAs encoding a novel putative peroxisomal enoyl-CoA hydratase.". Genomics 27 (3): 457–66. doi:10.1006/geno.1995.1077. PMID 7558027.