Adenosine Triphosphate-Linked Control of
            <i>Pseudomonas aeruginosa</i>
            Glucose-6-Phosphate Dehydrogenase

Lessie, T G; Neidhardt, Frederick C.

doi:10.1128/jb.93.4.1337-1345.1967

Cited by 103 publications

(57 citation statements)

References 14 publications

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“…32H1 possesses a functional tricarboxylic acid cycle and nonoxidative PP pathway (transketolase and transaldolase) [26] indicating the capability of this organism to make necessary hexoses from pentoses in a manner similar to that seen in Pseudomonas sp. [13,27]. Hexoses as sole carbon and energy sources did not affect enzymes of the ED pathway or G3P dehydrogenase ( Table 1).…”

Section: Resultsmentioning

confidence: 99%

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Regulation of hexose catabolism in Rhizobium sp. 32H1

Stowers

1985

FEMS Microbiology Letters

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In this communication, results support the conclusion that succinate can repress hexose-catabolizing enzymes in Rhizobium sp. 32H1 in a manner similar to catabolite repression, such as that seen in Pseudomonas aeruginosa [9,27]. Enzymes of the Embden-Meyerhof-Parnas and Entner-Doudoroff pathways were only detected in cells cultured on hexoses and were not present in succinate-grown cells. Initial enzymes of fructose and mannitol metabolism were present in cells gorwn on fructose and mannitol, respectively. NADP-linked 6phosphogluconate dehydrogenase was not detected in cell-free extracts regardless of the carbon source. INTRODUCTIONlupini, cowpea Rhizobia) [10,17,18,26].Little attention has been directed toward elucidating mechanisms which regulate the metabolism of carbohydrate in Rhizobium. Inducible enzymes in Rhizobium have been reported in pathways of carbohydrate metabolism [5,11,16,23,29] and in other metabolic sequences [1,25]. The regulation of inducible carbohydrate catabolizing enzymes in Rhizobium has only recently been investigated. Glucose mediation of polyol metabolism in R. trifolii has been documented [23]. Dicarboxylic acids, succinate and malate repress glucose transport [4,26], fructose uptake [8], fl-galactosidase [29], and hydrogenase [15]. To date, no report has demonstrated the repression of hexose-catabolizing enzymes by succinate in Rhizobia. The central carbohydrate catabolic pathways in Rhizobium species are becoming well characterized. Rhizobium uses the Entner-Doudoroff (ED) and tricarboxylic acid cycle as the primary routes of carbohydrate dissimilation [6]. The pentose phosphate (PP) pathway is present only in fast-growing Rhizobium species ( R. trifoliL R. meliloti, R. phaseoli, R. leguminosarum) [17,22] while not in the slow-growers (R. japonicum, R. MATERIALS AND METHODSRhizobium sp. 32H1 was obtained from the Nitragin Co. (Milwaukee, WI) and was grown in culture medium as described by Cole and Elkan [3] with 10 mM or 20 mM carbon source, 7.5 mM NH 4 C1 and 0.0001% vitamin stock [2]. The presence of Hepes (N-2-hydroxyethyl-piperazine-N-2ethanesulfonic acid) and Mes (2-N-mor-0378-1097/85/$03.30

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Section: Resultsmentioning

confidence: 99%

“…Other gluconeogenic pathways for hexose formation have been shown to exist in Pseudomonas sp. [13,27]. Hexoses may be derived via pentoses through the nonoxidative PP pathway in these bacteria, and pentoses can be formed from the tricarboxylic acid intermediates.…”

Section: Resultsmentioning

confidence: 99%

Regulation of hexose catabolism in Rhizobium sp. 32H1

Stowers

1985

FEMS Microbiology Letters

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“…Triparental bacterial conjugation and assay of catechol 2,3 dioxygenase were described previously (8). Glucose 6-phosphate dehydrogenase was assayed according to the published procedure (17). Recombinant DNA techniques and RNA isolation.…”

Section: Materials and Methods Materialsmentioning

confidence: 99%

Pseudomonas aeruginosainfection in cystic fibrosis: nucleotide sequence and transcriptional regulation of thealgDgene

1987

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Pulmonary infection by mucoid, alginate producing, Pseudomonas aeruginosa is a major complication in patients suffering from cystic fibrosis (CF). To analyze the mechanisms leading to the emergence of mucoid P. aeruginosa in CF lungs, control of the algD gene coding for GDPmannose dehydrogenase was studied. Transcriptional activation of algD was shown to be necessary for alginate production. Sequencing of algD and its promoter revealed multiple direct repeats upstream of the transcription start and throughout the promoter region. Using the algD-xy1E transcriptional fusion the algD promoter was demonstrated to be under positive control by the algR gene. This gene has previously been shown to undergo antibiotic promoted chromosomal amplification resulting in the emergence of the mucoid phenotype. These findings provide a basis for better understanding the control of mucoidy in P. aeruginosa.

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“…Pseudomonas fluorescens was cultivated in a Bioflo Model C30 continuous fermentor (New Brunswick Scientific Co. Inc., New Brunswick, New Jersey) set at a dilution rate of 0.08 in order to minimize the effects of varying growth rate on enzyme activity (Lessie & Neidhardt 1967;Dean 1972). The medium was as described above or sodium pyruvate (2 g/l) was substituted for glucose in order to determine the basal enzyme levels.…”

Section: Continuous Culture Experimentsmentioning

confidence: 99%

Water Relations of Glucose‐catabolizing Enzymes in Pseudomonas fluorescens

Prior

Kenyon

1980

Journal of Applied Bacteriology

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Examination of the catabolism of glucose via the Entner‐Doudoroff pathway by standard enzyme assays showed that the activity of glucose‐6‐phosphate dehydrogenase, glucokinase and 2‐ketoglu‐conokinase plus phosphoketogluconate reductase was completely inhibited at aw values less than 0.965, 0.98 and 0.96 respectively when NaCl was used to adjust the aw. The other glucose‐catabolizing enzymes were inhibited to a lesser degree. When sucrose was used to control aw, glucokinase and glucose‐6‐phosphate dehydrogenase were inhibited at 0.92 aw but the other enzymes remained active below 0.86 aw. Enzymes were relatively active at reduced aw when adjusted with glycerol and most remained active even at 0.80 aw. When aw was controlled by potassium glutamate, the activity of glucokinase and glucose‐6‐phosphate dehydrogenase was markedly less inhibited than by NaCl at similar aw. Possible reasons for the variation in activity by glucose‐catabolizing enzymes in response to aw controlled by various solutes could be location of the enzyme in the cell, ability of the solute to penetrate the cell and ability to withstand high salt and sucrose concentrations. When the aw of the growth medium was reduced to 0.98 by glycerol, NaCl and polyethylene glycol 400, levels of glucokinase were significantly reduced while higher levels of glucose dehydrogenase and gluconate dehydrogenase were induced. This suggests that reduction in aw could regulate the routes of catabolism in the Entner‐Doudoroff pathway. When sucrose was used to control aw of the growth medium high levels of most enzymes were induced, suggesting catabolism of the sucrose by the organism.

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Adenosine Triphosphate-Linked Control of Pseudomonas aeruginosa Glucose-6-Phosphate Dehydrogenase

Cited by 103 publications

References 14 publications

Regulation of hexose catabolism in Rhizobium sp. 32H1

Regulation of hexose catabolism in Rhizobium sp. 32H1

Pseudomonas aeruginosainfection in cystic fibrosis: nucleotide sequence and transcriptional regulation of thealgDgene

Water Relations of Glucose‐catabolizing Enzymes in Pseudomonas fluorescens

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