Inproceedings: an article in a conference proceedings.
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Nonallosteric transhydrogenase from Pseudomonas-aeruginosa
Title of the conference
12th Annual Meeting of the Union of Swiss Societies of Experimental Biology
Basel, Switzerland, March 13-14, 1980
The allosteric transhydrogenase from P. aeruginosa (EC 184.108.40.206) 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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