Effect of temperature on the uptake of glucose, gluconate, and 2-ketogluconate by Pseudomonas fluorescens

1978 ◽  
Vol 24 (1) ◽  
pp. 56-62 ◽  
Author(s):  
William H. Lynch ◽  
Mervyn Franklin
Keyword(s):  
Glucose Uptake ◽  
Pseudomonas Fluorescens ◽  
Differential Effect ◽  
Effect Of Temperature ◽  
Lower Growth ◽  
Major Function ◽  
Glucose Catabolism ◽  
Uptake Activity ◽  
Psychrotrophic Strain ◽  
In Cells

The effect of temperature on the uptake systems involved with glucose catabolism was studied in a psychrotrophic strain of Pseudomonas fluorescens. The Km values for glucose and gluconate uptake were approximately 1 and 30 μM respectively whether uptake was assayed at 30 or 5 °C. The Km for 2-ketogluconate (2-KG) uptake was approximately 40 μM assayed at 30 °C and 20 μM assayed at 5 °C. Little or no induction of 2-KG uptake was detected in cells grown at 30 °C with glucose or gluconate. High induced levels of 2-KG uptake were observed in cells grown at 5 °C. The induced level of glucose uptake in cells grown at 5 °C with glucose was only one-half the induced level in cells grown at 30 °C with glucose (when activities were compared at the same assay temperature). The effect of low-assay temperature on the activities of these uptake systems was most pronounced for gluconate. When the assay temperature was decreased from 30 to 5 °C, uptake activity decreased 12-fold, 6-fold, and 5-fold for gluconate, glucose, and 2-KG, respectively. Because of the differential effect of temperature on the induction of glucose uptake and on the activity of glucose, gluconate, and 2-KG uptake, the major uptake activity measured in cells grown at 5 °C with glucose or gluconate was through 2-KG. Glucose and 2-KG appeared to inhibit significantly gluconate uptake and (or) catabolism which might promote the continued oxidation of gluconate to 2-KG at low growth temperatures. The results confirm the lack of glucose or gluconate catabolism by the direct oxidative non-phosphorylated pathway through 2-KG at higher growth temperatures and the major function of this pathway at lower growth temperatures.

Effect of temperature on the activity and synthesis of glucose-catabolizing enzymes in Pseudomonas fluorescens

1975 ◽  
Vol 21 (10) ◽  
pp. 1560-1572 ◽  
Author(s):  
William H. Lynch ◽  
Janet MacLeod ◽  
Mervyn Franklin
Keyword(s):  
Pseudomonas Fluorescens ◽  
Growth Temperature ◽  
Differential Effect ◽  
Glucose Dehydrogenase ◽  
Oxidation Products ◽  
Effect Of Temperature ◽  
Direct Oxidation ◽  
Induction Of Enzymes ◽  
Low Levels ◽  
Similar Decrease

The activity of the enzymes of the oxidative non-phosphorylated pathway, glucose and gluconate dehydrogenases, were not significantly affected by changes in the assay temperature. Both enzymes demonstrated only a threefold difference in activity when compared at assay temperatures of 30 °C and 5 °C. In contrast, the enzymes involved in the direct phosphorylation and catabolism of glucose or its oxidation products, gluconate and 2-ketogluconate, exhibited a more pronounced response to decreasing assay temperatures. At least one enzyme in each pathway, involved in the direct phosphorylation and catabolism of glucose or 2-ketogluconate (2KG), demonstrated an eightfold decrease in activity with a decrease in assay temperature from 30 °C to 5 °C. A similar decrease in assay temperature resulted in a fivefold decrease in activity of the enzymes involved in the direct phosphorylation and catabolism of gluconate. The observed differential effect of temperature on the activity of the enzymes of glucose catabolism and on the accumulation of direct oxidation products during growth with glucose in P. fluorescens E-20 is discussed.Growth with glucose at 5 or 20 °C resulted in high induced levels of all glucose-catabolizing enzymes examined when compared with the levels of these same enzymes in pyruvate-grown cells. However, only low levels of glucose dehydrogenase were detected during growth at 30 °C with glucose, gluconate, or 2-KG. Similarly, only low levels of gluconate dehydrogenase were detected during growth with glucose at 30 °C, although a weak induction was observed during growth with gluconate or 2-KG at 30 °C. The levels of 2-KG kinase plus KPG reductase during growth at 30 °C were undetectable with glucose, weakly induced with gluconate, and fully induced with 2-KG. High induced levels of glucose dehydrogenase, gluconate dehydrogenase, and 2-KG kinase plus KPG reductase were present during growth at 20 °C with glucose or 2-KG. The low levels of glucose and gluconate dehydrogenases present at a growth temperature of 30 °C was not due to heat lability of the enzymes at this temperature. The low amounts of these two enzymes during growth with glucose at 30 °C probably prevented sufficient inducer(s) formation from glucose to allow induction of enzymes of 2-KG catabolism. The results demonstrated that temperature may regulate the pathways of glucose dissimilation by regulating, either directly or indirectly, the activity and synthesis of the enzymes involved in these pathways.

Development of Novel Glitazones as Antidiabetic Agents: Molecular Design, Synthesis, Evaluation of Glucose Uptake Activity and SAR Studies

2020 ◽  
Vol 17 (7) ◽  
pp. 840-849
Author(s):  
Mahendra Gowdru Srinivas ◽  
Prabitha Prabhakaran ◽  
Subhankar Probhat Mandal ◽  
Yuvaraj Sivamani ◽  
Pranesh Guddur ◽  
...  
Keyword(s):  
Glucose Uptake ◽  
Molecular Design ◽  
Docking Studies ◽  
Antidiabetic Activity ◽  
Design Synthesis ◽  
In Silico Docking ◽  
Ppar Γ ◽  
Sar Studies ◽  
Structure Activity ◽  
Uptake Activity

Background: Thiazolidinediones and its bioisostere, namely, rhodanines have become ubiquitous class of heterocyclic compounds in drug design and discovery. In the present study, as part of molecular design, a series of novel glitazones that are feasible to synthesize in our laboratory were subjected to docking studies against PPAR-γ receptor for their selection. Methods and Results: As part of the synthesis of selected twelve glitazones, the core moiety, pyridine incorporated rhodanine was synthesized via dithiocarbamate. Later, a series of glitazones were prepared via Knovenageal condensation. In silico docking studies were performed against PPARγ protein (2PRG). The titled compounds were investigated for their cytotoxic activity against 3T3-L1 cells to identify the cytotoxicity window of the glitazones. Further, within the cytotoxicity window, glitazones were screened for glucose uptake activity against L6 cells to assess their possible antidiabetic activity. Conclusion: Based on the glucose uptake results, structure activity relationships are drawn for the title compounds.

In vitro glucose uptake activity of Aegles marmelos and Syzygium cumini by activation of Glut-4, PI3 kinase and PPARγ in L6 myotubes

Phytomedicine ◽  
2006 ◽  
Vol 13 (6) ◽  
pp. 434-441 ◽  
Author(s):  
R. Anandharajan ◽  
S. Jaiganesh ◽  
N.P. Shankernarayanan ◽  
R.A. Viswakarma ◽  
A. Balakrishnan
Keyword(s):  
Glucose Uptake ◽  
Pi3 Kinase ◽  
Syzygium Cumini ◽  
Glut 4 ◽  
L6 Myotubes ◽  
Uptake Activity

scholarly journals Structural and Functional Analysis of the Phosphonoacetate Hydrolase (phnA) Gene Region in Pseudomonas fluorescens 23F

2001 ◽  
Vol 183 (11) ◽  
pp. 3268-3275 ◽  
Author(s):  
Anna N. Kulakova ◽  
Leonid A. Kulakov ◽  
Natalya V. Akulenko ◽  
Vladimir N. Ksenzenko ◽  
John T. G. Hamilton ◽  
...  
Keyword(s):  
Pseudomonas Fluorescens ◽  
Bond Cleavage ◽  
Transcriptional Regulators ◽  
Open Reading Frames ◽  
Cell Analysis ◽  
Rna Analysis ◽  
Cleavage Enzyme ◽  
Reading Frames ◽  
Lysr Family ◽  
In Cells

ABSTRACT The Pseudomonas fluorescens 23F phosphonoacetate hydrolase gene (phnA) encodes a novel carbon-phosphorus bond cleavage enzyme whose expression is independent of the phosphate status of the cell. Analysis of the regions adjacent to the phosphonoacetate hydrolase structural gene (phnA) indicated the presence of five open reading frames (ORFs). These include one (phnR) whose putative product shows high levels of homology to the LysR family of positive transcriptional regulators. Its presence was shown to be necessary for induction of the hydrolase activity. 2-Phosphonopropionate was found to be an inducer (and poor substrate) for phosphonoacetate hydrolase. Unlike phosphonoacetate, which is also an inducer of phosphonoacetate hydrolase, entry of 2-phosphonopropionate into cells appeared to be dependent on the presence of a gene (phnB) that lies immediately downstream of phnA and whose putative product shows homology to the glycerol-3-phosphate transporter. RNA analysis revealed transcripts for the phnAB andphnR operons, which are transcribed divergently; the resulting mRNAs overlapped by 29 nucleotide bases at their 5′ ends. Transcripts of phnAB were detected only in cells grown in the presence of phosphonoacetate, whereas transcripts ofphnR were observed in cells grown under both induced and uninduced conditions. The expression of three additional genes found in the phnA region did not appear necessary for the degradation of phosphonoacetate and 2-phosphonopropionate by eitherPseudomonas putida or Escherichia colicells.

scholarly journals Insulinomimetic Zn(II) Complexes as Evaluated by Both Glucose-Uptake Activity and Inhibition of Free Fatty Acids Release in Isolated Rat Adipocytes

2008 ◽  
Vol 56 (8) ◽  
pp. 1181-1183 ◽  
Author(s):  
Midori Nishide ◽  
Yutaka Yoshikawa ◽  
Eriko U. Yoshikawa ◽  
Kinuyo Matsumoto ◽  
Hiromu Sakurai ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Free Fatty Acids ◽  
Glucose Uptake ◽  
Rat Adipocytes ◽  
Uptake Activity ◽  
Isolated Rat

The influence of temperature on the pathways of glucose catabolism in Pseudomonas fluorescens

1969 ◽  
Vol 15 (9) ◽  
pp. 995-1000 ◽  
Author(s):  
S. A. Palumbo ◽  
Lloyd D. Witter
Keyword(s):  
Continuous Culture ◽  
Pseudomonas Fluorescens ◽  
Enzyme Activities ◽  
Hexose Monophosphate ◽  
Influence Of Temperature ◽  
Glucose Catabolism ◽  
Hexose Monophosphate Pathway ◽  
Influence Of Temperature On ◽  
Major Shift

The influence of temperature on the pathways of glucose catabolism in Pseudomonas fluorescens has been investigated using the radiorespirometry method. When grown in continuous culture with limiting concentrations of glucose, the organism metabolized 86% of the glucose via the Entner–Doudoroff pathway at 30, 20, and 8 C. The remaining glucose, 14%, was metabolized via the hexose monophosphate pathway. When the organism was grown on non-limiting concentrations of glucose at 8 C, a major shift in pathways of glucose catabolism was observed. Fifty-seven percent of the glucose was degraded via the hexose monophosphate pathway and only 43% via the Entner–Doudoroff pathway. A change in temperature altered the pathways of glucose catabolism by regulating the growth limiting concentration of glucose rather than by directly affecting the respective enzyme activities of the pathways.

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