Nonallosteric transhydrogenase from Pseudomonas-aeruginosa

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State: Serval
Version: author
Serval ID
serval:BIB_8FBF36192814
Type
Inproceedings: an article in a conference proceedings.
Publication sub-type
Abstract (Abstract): shot summary in a article that contain essentials elements presented during a scientific conference, lecture or from a poster.
Collection
Publications
Title
Nonallosteric transhydrogenase from Pseudomonas-aeruginosa
Title of the conference
12th Annual Meeting of the Union of Swiss Societies of Experimental Biology
Author(s)
Widmer F., Meyer I.
Address
Basel, Switzerland, March 13-14, 1980
ISBN
0014-4754
Publication state
Published
Issued date
1980
Peer-reviewed
Oui
Volume
36
Series
Experientia
Pages
736
Language
english
Abstract
The allosteric transhydrogenase from P. aeruginosa (EC 1.6.1.1) acts as an essential link between carbohydrate catabolism and respiratory chain (Widmer and Kaplan, Biochemistry 15, 4693, 4699, 1976). The enzyme is a unidirectional catalyst which brings about the reduction of NAD+ by NADPH + H+. The potential substrate NADP+ acts as an allosteric inhibitor, whereas other 2'-P nucleotides are allosteric activators. There are 1 catalytic site and 1 regulatory site per protomer. We now report the identification of a nonallosteric transhydrogenase isolated from a P. aeruginosa strain obtained from a hospital patient. No functional effector site appears to be present, and the catalytic site does not accommodate 2'-P nucleotides. Therefore, this enzyme form only catalyzes hydrogen transfers between NAD(H) and coenzyme analogs lacking the 2'-P group. It never constitutes the totality of the transhydrogenase activity detected in the bacterium, and its physiological role is still unclear. Its occurrence might be due to mutation and/or nutritional constraints.
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03/03/2018 19:22
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