Pseudomonas aeruginosa transhydrogenase: Affinity of substrates for the regulatory site and possible hysteretic behavior

Détails

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Etat: Public
Version: de l'auteur
ID Serval
serval:BIB_1221D6285358
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Pseudomonas aeruginosa transhydrogenase: Affinity of substrates for the regulatory site and possible hysteretic behavior
Périodique
Biochemical and Biophysical Research Communications
Auteur(s)
Widmer F., Kaplan N.O.
ISSN
0006-291X
Statut éditorial
Publié
Date de publication
1977
Peer-reviewed
Oui
Volume
76
Numéro
4
Pages
1287-1292
Langue
anglais
Résumé
The polymeric enzyme transhydrogenase from Pseudomonas aeruginosa (NADPH:NAD+ oxidoreductase; EC 1.6.1.1) has been shown to possess distinct catalytic and regulatory sites, despite the close structural relationship between substrates and effectors. The present report substantiates the previous conclusions from kinetic and affinity chromatography studies, which have suggested that the substrates NADPH and oxidized thionicotinamide ademine dinucleotide phosphate could bind to both catalytic and regulatory sites. In addition, the allosteric R form of the enzyme appears now to be stabilized against high dilution inactivation.
The oxidized substrate thionicotinamide adenine dinucleotide forms a dead end complex on binding to the catalytic site in the T form. The process is slow, and can be termed hysteretic, as defined by Frieden (J. Biol. Chem. (1970), 245, 5788-5799).
Mots-clé
Binding Sites, Kinetics, Macromolecular Substances, NAD/analogs & derivatives, *NADH, NADPH Oxidoreductases/metabolism, NADP/analogs & derivatives, Oxidation-Reduction, Protein Binding, Pseudomonas aeruginosa/*enzymology, Time Factors
Pubmed
Web of science
Création de la notice
13/08/2015 7:53
Dernière modification de la notice
20/08/2019 12:40
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