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Titolo:
The mitochondrial isovaleryl-coenzyme A dehydrogenase of Arabidopsis oxidizes intermediates of leucine and valine catabolism
Autore:
Daschner, K; Couee, I; Binder, S;
Indirizzi:
Univ Ulm, D-89069 Ulm, Germany Univ Ulm Ulm Germany D-89069Univ Ulm, D-89069 Ulm, Germany Univ Rennes 1, CNRS, UMR 6553, F-35042 Rennes, France Univ Rennes 1 Rennes France F-35042 RS, UMR 6553, F-35042 Rennes, France
Titolo Testata:
PLANT PHYSIOLOGY
fascicolo: 2, volume: 126, anno: 2001,
pagine: 601 - 612
SICI:
0032-0889(200106)126:2<601:TMIADO>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
RAT-LIVER MITOCHONDRIA; BIOTIN-CONTAINING SUBUNIT; CHAIN ACYL-COA; BETA-OXIDATION; MOLECULAR-CLONING; A DEHYDROGENASE; HIGHER-PLANTS; 3-METHYLCROTONYL-COENZYME-A CARBOXYLASE; FATTY-ACIDS; PURIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Binder, S Univ Ulm, Albert Einstein Allee 11, D-89069 Ulm, Germany Univ Ulm Albert Einstein Allee 11 Ulm Germany D-89069 , Germany
Citazione:
K. Daschner et al., "The mitochondrial isovaleryl-coenzyme A dehydrogenase of Arabidopsis oxidizes intermediates of leucine and valine catabolism", PLANT PHYSL, 126(2), 2001, pp. 601-612

Abstract

We recently identified a cDNA encoding a putative isovaleryl-coenzyme A (CoA) dehydrogenase in Arabidopsis (AtIVD). In animals, this homotetrameric enzyme is located in mitochondria and catalyzes the conversion of isovaleryl-CoA to 3-methylcrotonyl-CoA as an intermediate step in the leucine (Leu) catabolic pathway. Expression of AtIVD:smGFP4 fusion proteins in tobacco (Nicotiana tabacum) protoplasts and biochemical studies now demonstrate the invivo import of the plant isovaleryl-CoA dehydrogenase (IVD) into mitochondria and the enzyme in the matrix of these organelles. Two-dimensional separation of mitochondrial proteins by blue native and SDS-PAGE and size determination of the native and overexpressed proteins suggest homodimers to be the dominant form of the plant ND. Northern-blot hybridization and studies in transgenic Arabidopsis plants expressing Ativd promoter:gus constructs reveal strong expression of this gene in seedlings and young plants grown in the absence of sucrose, whereas promoter activity in almost all tissues is strongly inhibited by exogeneously added sucrose. Substrate specificity; tests with AtIVD expressed in Escherichia coli indicate a strong preference toward isovaleryl-CoA but surprisingly also show considerable activity with isobutyryl-CoA. This strongly indicates a commitment of the enzyme in Leu catabolism, but the activity observed with isobutyryl-CoA also suggests a parallel involvement of the enzyme in the dehydrogenation of intermediates ofthe valine degradation pathway. Such a dual activity has not been observedwith the animal IVD and may suggest a novel connection of the Leu and valine catabolism in plants.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/07/20 alle ore 09:42:44