THE ENZYMES OF THE TRICARBOXYLIC ACID CYCLE OF PSEUDOMONAS AERUGINOSA
- 1 June 1956
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Microbiology
- Vol. 2 (4), 433-440
- https://doi.org/10.1139/m56-051
Abstract
It was demonstrated that Pseudomonas aeruginosa possesses all the enzymes necessary for the oxidation of pyruvate to CO2 and water without passing through the conventional intermediates oxalosuccinate and α-ketoglutarate. These intermediates are bypassed by the action of the enzyme isocitratase which splits d-isocitrate to succinate plus glyoxylate. This reaction was shown to be readily reversible. The malic acid dehydrogenase content was low and in addition this enzyme required a high pH for optimum activity. In fresh cell extracts at pH 7.4 its activity was only 10% that of the other enzymes of the cycle. The malic and isocitric dehydrogenases were TPN specific. The organism was also shown to possess all the enzymes necessary for the operation of the conventional tricarboxylic acid cycle.Keywords
This publication has 6 references indexed in Scilit:
- Distribution and Formation of IsocitritaseNature, 1955
- TRACER EXPERIMENTS ON THE MECHANISM OF CITRIC ACID FORMATION BY ASPERGILLUS NIGERJournal of Biological Chemistry, 1954
- A deviation from the conventional tricarboxylic acid cycle in Pseudomonas AeruginosaBiochimica et Biophysica Acta, 1953
- A Simplified Photometric Method for the Determination of Citric Acid in Biological FluidsJournal of Biological Chemistry, 1952
- TRICARBOXYLIC ACID CYCLE IN PSEUDOMONAS AERUGINOSAJournal of Biological Chemistry, 1951
- Spectrophotometric measurements of the enzymatic formation of fumaric and cis-aconitic acidsBiochimica et Biophysica Acta, 1950