scholarly journals Carbon Sources Tune Antibiotic Susceptibility in Pseudomonas aeruginosa via Tricarboxylic Acid Cycle Control

2017 ◽  
Vol 24 (2) ◽  
pp. 195-206 ◽  
Author(s):  
Sylvain Meylan ◽  
Caroline B.M. Porter ◽  
Jason H. Yang ◽  
Peter Belenky ◽  
Arnaud Gutierrez ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Antibiotic Susceptibility ◽  
Tricarboxylic Acid Cycle ◽  
Carbon Sources ◽  
Tricarboxylic Acid ◽  
Acid Cycle

scholarly journals TRICARBOXYLIC ACID CYCLE IN PSEUDOMONAS AERUGINOSA

1951 ◽  
Vol 190 (2) ◽  
pp. 853-858
Author(s):  
Jack J.R. Campbell ◽  
Flora.Norris. Stokes
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Tricarboxylic Acid Cycle ◽  
Tricarboxylic Acid ◽  
Acid Cycle

THE ENZYMES OF THE TRICARBOXYLIC ACID CYCLE OF PSEUDOMONAS AERUGINOSA

1956 ◽  
Vol 2 (4) ◽  
pp. 433-440 ◽  
Author(s):  
Jack J. R. Campbell ◽  
Roberts A. Smith
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Malic Acid ◽  
Tricarboxylic Acid Cycle ◽  
Tricarboxylic Acid ◽  
The Other ◽  
Acid Cycle ◽  
High Ph ◽  
Optimum Activity ◽  
Fresh Cell ◽  
Cell Extracts

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.

THE TRICARBOXYLIC ACID CYCLE, THE GLYOXYLATE CYCLE, AND THE ENZYMES OF GLUCOSE OXIDATION IN PSEUDOMONAS AERUGINOSA

1966 ◽  
Vol 12 (5) ◽  
pp. 1015-1022 ◽  
Author(s):  
Margaret von Tigerstrom ◽  
J. J. R. Campbell
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Glucose Oxidation ◽  
Nadh Oxidase ◽  
Specific Activity ◽  
Tricarboxylic Acid Cycle ◽  
Glyoxylate Cycle ◽  
Succinic Dehydrogenase ◽  
Tricarboxylic Acid ◽  
Acid Cycle ◽  
The Glyoxylate Cycle

The enzymes of the glyoxylate cycle, the tricarboxylic acid cycle, glucose oxidation, and hydrogen transport were measured in extracts of Pseudomonas aeruginosa grown with glucose, α-ketoglutarate, or acetate as sole carbon source. The specific activity of isocitritase was increased 25-fold by growth on acetate whereas malate synthetase was increased only 4-fold. All of the enzymes of glucose metabolism, operative at the hexose level, were inducible. The enzymes of the tricarboxylic acid cycle were present under all conditions of growth but extracts from acetate-grown cells contained only one-quarter of the fumarase and pyruvic oxidase activity and half the malate-oxidizing activity of the other extracts. Transhydrogenase, NADH oxidase, and NADPH oxidase activities were similar in each type of extracts. Most of the enzymes were present in the soluble cytoplasm, exceptions being glucose oxidase, succinic dehydrogenase, and NADH oxidase.

scholarly journals Identification of a multienzyme complex of the tricarboxylic acid cycle enzymes containing citrate synthase isoenzymes from Pseudomonas aeruginosa

1996 ◽  
Vol 313 (3) ◽  
pp. 769-774 ◽  
Author(s):  
Colin G. MITCHELL
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Citrate Synthase ◽  
Tricarboxylic Acid Cycle ◽  
Growth Cycle ◽  
Tricarboxylic Acid ◽  
Multienzyme Complex ◽  
Acid Cycle ◽  
Consecutive Reactions ◽  
Osmotic Lysis ◽  
The Individual

A multienzyme complex of tricarboxylic acid cycle enzymes, catalysing the consecutive reactions from fumarate to 2-oxoglutarate, has been identified in extracts of Pseudomonas aeruginosa prepared by gentle osmotic lysis of the cells. The individual enzyme activities of fumarase, malate dehydrogenase, citrate synthase, aconitase and isocitrate dehydrogenase can be used to reconstitute the complex. The citrate synthase isoenzymes, CSI and CSII, from this organism can be used either together or as the individual activities to reconstitute the complex. No complex can be reformed in the absence of CSI or CSII. Which CS isoenzyme predominates in the complex depends on the phase of growth at which the cells were harvested and the extract prepared. More CSI was found in the complex during exponential growth, whereas CSII predominated during the stationary phase. The results support the idea of a ‘metabolon’ in this organism, with the composition of the CS component varying during the growth cycle.

scholarly journals Control of the production of exo-β-N-acetylglucosaminidase by Bacillus subtilis B. Derepression during gluconeogenesis and initial stages of sporulation

1973 ◽  
Vol 134 (1) ◽  
pp. 271-281 ◽  
Author(s):  
Stephen J. Brewer ◽  
Roger C. W. Berkeley
Keyword(s):  
Bacillus Subtilis ◽  
Exponential Growth ◽  
Phosphoenolpyruvate Carboxylase ◽  
Metal Ion ◽  
Tricarboxylic Acid Cycle ◽  
Carbon Sources ◽  
Defined Medium ◽  
Tricarboxylic Acid ◽  
Carboxylase Activity ◽  
Acid Cycle

1. The control of exo-β-N-acetylglucosaminidase (EC 3.2.1.30) production by Bacillus subtilis B growing on a chemically defined medium was studied. 2. The enzyme was repressed during exponential growth by those carbon sources that enter the glycolytic pathway above the level of phosphoenolpyruvate. When exponential growth ceased as a result of low concentrations of the nitrogen, carbon or metal ion components of the medium, the enzyme was formed and its amount could be increased by the addition of cell-wall fragments as inducer. 3. The enzyme was de-repressed and could be induced during exponential growth on non-glycolytic compounds metabolized directly into pyruvate, acetyl-CoA or tricarboxylic acid cycle intermediates. 4. The major difference in the metabolism of the organism utilizing these two groups of compound was the existence of high activities of phosphoenolpyruvate carboxylase required for gluconeogenesis. 5. It is concluded that the de-repression of glucosaminidase occurs when the only principal change detected in the intermediary metabolism of the organism was the presence of high activities of phosphoenolpyruvate carboxylase. 6. When the organism was grown on media containing repressing compounds, the enzyme was only de-repressed on entry of the cells into the initial stages of sporulation, where phosphoenolpyruvate carboxylase activity, even in the presence of excess of glucose, increased in parallel with glucosaminidase, neutral proteinase and alkaline phosphatase activities. 7. These results suggest a strong link, at the level of the tricarboxylic acid cycle, between the control of phosphoenolpyruvate carboxylase and the control of the de-repression of glucosaminidase and sporulation.

scholarly journals The LysR-Type Transcriptional Regulator BsrA (PA2121) Controls Vital Metabolic Pathways in Pseudomonas aeruginosa

mSystems ◽  
2021 ◽  
Author(s):  
Magdalena Modrzejewska ◽  
Adam Kawalek ◽  
Aneta Agnieszka Bartosik
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Regulatory Network ◽  
Metabolic Pathways ◽  
Tricarboxylic Acid Cycle ◽  
Transcriptional Regulator ◽  
Tricarboxylic Acid ◽  
Content Type ◽  
Acid Cycle

This study shows that BsrA, a LysR-type transcriptional regulator from Pseudomonas aeruginosa , previously identified as a repressor of biofilm synthesis, is part of an intricate global regulatory network. BsrA acts directly and/or indirectly as the repressor and/or activator of genes from vital metabolic pathways (e.g., pyruvate, acetate, and tricarboxylic acid cycle) and is involved in control of transport functions and the formation of surface appendages.

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