BIOMAT Database Logo BIOMAT Database Logo

Substrate stereospecificities of rat liver peroxisomal 3-hydroxyacyl-CoA dehydrogenases. 1996

M Dieuaide, and D K Novikov, and H Carchon, and P P Van Veldhoven, and G P Mannaerts
Katholieke Universiteit Leuven, Afdeling Farmacologie, Belgium.

UI MeSH Term Description Entries
D007535 Isomerases A class of enzymes that catalyze geometric or structural changes within a molecule to form a single product. The reactions do not involve a net change in the concentrations of compounds other than the substrate and the product.(from Dorland, 28th ed) EC 5. Isomerase
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D008830 Microbodies Electron-dense cytoplasmic particles bounded by a single membrane, such as PEROXISOMES; GLYOXYSOMES; and glycosomes. Glycosomes,Glycosome,Microbody
D009097 Multienzyme Complexes Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES. Complexes, Multienzyme
D004746 Enoyl-CoA Hydratase An enzyme that catalyzes reversibly the hydration of unsaturated fatty acyl-CoA to yield beta-hydroxyacyl-CoA. It plays a role in the oxidation of fatty acids and in mitochondrial fatty acid synthesis, has broad specificity, and is most active with crotonyl-CoA. EC 4.2.1.17. 3-Hydroxyacyl CoA Hydrolyases,3-Hydroxyacyl Dehydratases,Crotonase,Enoyl Hydrase,beta-Hydroxyacyl Dehydratases,Enoyl CoA Hydratases,beta-Hydroxyacyl-CoA Dehydrases,trans-2-Enoyl-Coenzyme A Hydratase,3 Hydroxyacyl CoA Hydrolyases,3 Hydroxyacyl Dehydratases,CoA Hydratases, Enoyl,CoA Hydrolyases, 3-Hydroxyacyl,Dehydrases, beta-Hydroxyacyl-CoA,Dehydratases, 3-Hydroxyacyl,Dehydratases, beta-Hydroxyacyl,Enoyl CoA Hydratase,Hydrase, Enoyl,Hydratase, Enoyl-CoA,Hydratase, trans-2-Enoyl-Coenzyme A,Hydratases, Enoyl CoA,Hydrolyases, 3-Hydroxyacyl CoA,beta Hydroxyacyl CoA Dehydrases,beta Hydroxyacyl Dehydratases,trans 2 Enoyl Coenzyme A Hydratase
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D013379 Substrate Specificity A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts. Specificities, Substrate,Specificity, Substrate,Substrate Specificities
D015094 3-Hydroxyacyl CoA Dehydrogenases Enzymes that reversibly catalyze the oxidation of a 3-hydroxyacyl CoA to 3-ketoacyl CoA in the presence of NAD. They are key enzymes in the oxidation of fatty acids and in mitochondrial fatty acid synthesis. beta-Hydroxyacyl Dehydrogenases,3 Hydroxyacyl CoA Dehydrogenases,CoA Dehydrogenases, 3-Hydroxyacyl,Dehydrogenases, 3-Hydroxyacyl CoA,Dehydrogenases, beta-Hydroxyacyl,beta Hydroxyacyl Dehydrogenases
D051381 Rats The common name for the genus Rattus. Rattus,Rats, Laboratory,Rats, Norway,Rattus norvegicus,Laboratory Rat,Laboratory Rats,Norway Rat,Norway Rats,Rat,Rat, Laboratory,Rat, Norway,norvegicus, Rattus
D063994 Peroxisomal Bifunctional Enzyme A monomeric protein found in liver peroxisomes that contains two enzymatically active domains; an enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase domain, and an (S)-3-hydroxyacyl-CoA dehydrogenase domain. The enzyme is stereospecific with regards to how cis and trans double bonds are metabolized. It is complemented by PEROXISOMAL MULTIFUNCTIONAL PROTEIN-2, which has the opposite stereospecificity. Peroxisomal-Bifunctional Enzymes,2-Enoyl-CoA Hydratase, 3-Hydroxyacyl-CoA Dehydrogenase-delta 3, delta 2-Enoyl-CoA Isomerase,Enoyl-CoA Hydratase-3-Hydroxyacyl-CoA Dehydrogenase,L-Bifunctional Enzyme,L-Peroxisomal Bifunctional Enzyme,Peroxisomal Hydratase-Dehydrogenase-Epimerase,Peroxisomal Multifunctional beta-Oxidation Protein,Peroxisomal Trifunctional Enzyme,Bifunctional Enzyme, L-Peroxisomal,Bifunctional Enzyme, Peroxisomal,Dehydrogenase, Enoyl-CoA Hydratase-3-Hydroxyacyl-CoA,Enoyl CoA Hydratase 3 Hydroxyacyl CoA Dehydrogenase,Hydratase-3-Hydroxyacyl-CoA Dehydrogenase, Enoyl-CoA,Hydratase-Dehydrogenase-Epimerase, Peroxisomal,L Bifunctional Enzyme,L Peroxisomal Bifunctional Enzyme,Peroxisomal Bifunctional Enzymes,Peroxisomal Hydratase Dehydrogenase Epimerase,Peroxisomal Multifunctional beta Oxidation Protein

Related Publications

M Dieuaide, and D K Novikov, and H Carchon, and P P Van Veldhoven, and G P Mannaerts
Peroxisomal beta-oxidation. Purification of four novel 3-hydroxyacyl-CoA dehydrogenases from rat liver peroxisomes.
October 1994, The Journal of biological chemistry,
M Dieuaide, and D K Novikov, and H Carchon, and P P Van Veldhoven, and G P Mannaerts
Occurrence of two 3-hydroxyacyl-CoA dehydrogenases in rat liver.
August 1979, Biochimica et biophysica acta,
M Dieuaide, and D K Novikov, and H Carchon, and P P Van Veldhoven, and G P Mannaerts
Two mitochondrial 3-hydroxyacyl-CoA dehydrogenases in bovine liver.
April 1996, Journal of biochemistry,
M Dieuaide, and D K Novikov, and H Carchon, and P P Van Veldhoven, and G P Mannaerts
Purification and properties of mitochondrial and peroxisomal 3-hydroxyacyl-CoA dehydrogenase from rat liver.
August 1980, Archives of biochemistry and biophysics,
M Dieuaide, and D K Novikov, and H Carchon, and P P Van Veldhoven, and G P Mannaerts
Peroxisomal beta oxidation system of rat liver. Copurification of enoyl-CoA hydratase and 3-hydroxyacyl-CoA dehydrogenase.
July 1979, Biochemical and biophysical research communications,
M Dieuaide, and D K Novikov, and H Carchon, and P P Van Veldhoven, and G P Mannaerts
Enzymes converting D-3-hydroxyacyl-CoA to trans-2-enoyl-CoA. Microsomal and peroxisomal isoenzymes in rat liver.
October 1993, The Journal of biological chemistry,
M Dieuaide, and D K Novikov, and H Carchon, and P P Van Veldhoven, and G P Mannaerts
Prenatal diagnosis of peroxisomal D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein deficiency.
January 1999, Journal of human genetics,
M Dieuaide, and D K Novikov, and H Carchon, and P P Van Veldhoven, and G P Mannaerts
Purification, properties, and immunocytochemical localization of human liver peroxisomal enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase.
May 1987, Proceedings of the National Academy of Sciences of the United States of America,
M Dieuaide, and D K Novikov, and H Carchon, and P P Van Veldhoven, and G P Mannaerts
Transcription regulation of peroxisomal fatty acyl-CoA oxidase and enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase in rat liver by peroxisome proliferators.
March 1986, Proceedings of the National Academy of Sciences of the United States of America,
M Dieuaide, and D K Novikov, and H Carchon, and P P Van Veldhoven, and G P Mannaerts
D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein deficiency: a newly identified peroxisomal disorder.
November 1997, American journal of human genetics,
Copied contents to your clipboard!