Regulatory properties of pyridine-nucleotide transhydrogenase from pseudomonas-aeruginosa - Active enzyme ultracentrifugation studies

Détails

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Etat: Public
Version: de l'auteur
ID Serval
serval:BIB_F6311A53CBC5
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Regulatory properties of pyridine-nucleotide transhydrogenase from pseudomonas-aeruginosa - Active enzyme ultracentrifugation studies
Périodique
Biochemistry
Auteur(s)
Widmer F., Kaplan N.O.
ISSN
0006-2960
Statut éditorial
Publié
Date de publication
1976
Peer-reviewed
Oui
Volume
15
Numéro
21
Pages
4699-4703
Langue
anglais
Résumé
Active enzyme ultracentrifugation studies of the pyridine nucleotide transhydrogenase from Pseudomonas aeruginosa (EC 1.6.1.1.) show that the enzymatic reaction is catalyzed by a molecular species characterized by an S20,W value of about 34 S, whatever the reduced substrate may be (tri- or diphosphopyridine nucleotide). The filamentous aggregated form of the enzyme (S20,W = 121 S and higher), identified by previous investigations (Cohen, P. T., and Kaplan, N. O. (1970), J. Biol. Chem. 245, 2825-2836; Louie, D. D., Kaplan, N. O., and Mc Lean, J. D. (1972), J. Mol. Biol. 70, 651-664), appears, therefore, to be an inactive species. The physiological implications of the enzyme are discussed. Several lines of evidence lead to the conclusion that the transhydrogenase might act as an essential link between carbohydrate catabolism and the respiratory chain.
Mots-clé
Macromolecular Substances, Molecular Weight, Nad, NADH, NADPH Oxidoreductases/*metabolism, Nadp, Pseudomonas aeruginosa/*enzymology, Ultracentrifugation
Pubmed
Web of science
Création de la notice
13/08/2015 7:53
Dernière modification de la notice
20/08/2019 16:22
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