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Titolo:
Purification, characterization and cloning of isovaleryl-CoA dehydrogenasefrom higher plant mitochondria
Autore:
Faivre-Nitschke, SE; Couee, I; Vermel, M; Grienenberger, JM; Gualberto, JM;
Indirizzi:
CNRS, Inst Biol Mol Plantes, F-67084 Strasbourg, France CNRS Strasbourg France F-67084 l Mol Plantes, F-67084 Strasbourg, France
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 5, volume: 268, anno: 2001,
pagine: 1332 - 1339
SICI:
0014-2956(200103)268:5<1332:PCACOI>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACYL-COENZYME-A; RAT-LIVER MITOCHONDRIA; PEROXISOMAL-BETA-OXIDATION; POTATO SEED-TUBERS; SUBSTRATE-SPECIFICITY; OXIDASE; STARVATION; METABOLISM; ENZYMES; CELLS;
Keywords:
plant mitochondria; isovaleryl-CoA dehydrogenase; leucine catabolism;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Gualberto, JM CNRS, Inst Biol Mol Plantes, 12 Rue Gen Zimmer, F-67084 Strasbourg, France CNRS 12 Rue Gen Zimmer Strasbourg France F-67084 rg, France
Citazione:
S.E. Faivre-Nitschke et al., "Purification, characterization and cloning of isovaleryl-CoA dehydrogenasefrom higher plant mitochondria", EUR J BIOCH, 268(5), 2001, pp. 1332-1339

Abstract

Between the different types of Acyl-CoA dehydrogenases (ACADs), those specific for branched chain acyl-CoA derivatives are involved in the catabolismof amino acids. In mammals, isovaleryl-CoA dehydrogenase (IVD), an enzyme of the leucine catabolic pathway, is a mitochondrial protein, as other acyl-CoA dehydrogenases involved in fatty acid beta -oxidation. In plants, fatty acid beta -oxidation takes place mainly in peroxisomes, and the cellular location of the enzymes involved in the catabolism of branched-chain amino acids had not been definitely assigned. Here, we describe that highly purified potato mitochondria have important IVD activity. The enzyme was partially purified and cDNAs from two different genes were obtained. The partially purified enzyme has enzymatic constantvalues with respect to isovaleryl-CoA comparable to those of the mammalianenzyme. It is not active towards straight-chain acyl-CoA substrates tested, but significant activity was also found with isobutyryl-CoA, implying an additional role of the enzyme in the catabolism of valine. The present study confirms recent reports that in plants IVD activity resides in mitochondria and opens the way to a more detailed study of amino-acid catabolism in plant development.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 16/07/20 alle ore 18:28:17