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Comparative Arrhenius plots of enzyme activity from penicillium

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Abstract

Comparison of the Arrhenius plots of three enzymes, formyltetrahydrofolate synthetase, glutathione reductase (GSSGR) and chorismate mutase (CM) from a thermophilic (Penicillium duponti) and a mesophilic (Penicillium chrysogenum) fungus reveals a fairly consistent pattern. In general, those enzymes extracted from mesophiles had lower activation energies than similar enzymes extracted from thermophiles. One enzyme studied, mesophilic glutathione reductase, exhibited a break in its Arrhenius plot. The allosteric enzyme studied showed slightly different sensitivities in the thermophilic versus the mesophilic extracts.

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References

  1. Abd-el-al, A. &Ingraham, J. L. (1969) Cold Sensitivity and Other Phenotypes Resulting from Mutation in Pyr A Gene.J. Biol. Chem. 244:4039–4045.

    PubMed  Google Scholar 

  2. Benko, P., Wood, T. &Segel, I. H. (1967) Specificity and Regulation of Methionine Transport in Filamentous Fungi.Arch. Biochem. Biophys. 122:783–804.

    Google Scholar 

  3. Broad, T. E. &Shepard, M. G. (1970) Purification and Properties of Glucose-6-Phosphate Dehydrogenase from the Thermophilic FungusPenicillium duponti Biochim.et Biophys. Acta 198:407–414.

    Google Scholar 

  4. Cazzulo, J. J., Sundaram, T. K. &Kornberg, H. L. (1970) Properties and Regulation of Pyruvate Carboxylase fromBacillus stearothermophilus.Proc. Roy Soc. Lond. B. 176:1–19.

    Google Scholar 

  5. Gerhart, J. C. &Pardee, A. B. (1962) The Enzymology of Control by Feedback Inhibition.J. Biol. Chem. 237:891–896.

    PubMed  Google Scholar 

  6. Gilchrist, D. G., Woodin, T. S., Johnson, M. L. &Kosuge, T. (1972) Regulation of Aromatic Amino Acid Biosynthesis in Higher Plants.Plant Physiol. 49:52–57.

    Google Scholar 

  7. Gornall, A. G., Bardawill, C. J. &David, M. M. (1949) Determination of Serum Proteins by Means of the Biuret Reaction.J. Biol. Chem. 177:751–766.

    Google Scholar 

  8. Hachimori, A., Namiko, M. &Nosoh, Y. (1970) Studies on an ATPase of Thermophilic Bacteria I. Purification and Properties.Biochim. et Biophys. Acta 206:426–437.

    Google Scholar 

  9. Himes, R. H. &Wilder, T. (1968) Formyltetrahydrofolate Synthetase: Effect of pH and Temperature on the Reaction.Arch. Biochem. Biophys. 124:230–237.

    PubMed  Google Scholar 

  10. Hochachka, P. W., Freed, J. M., Somero, G. M. &Prosser, C. L. (1971) Control Sites in Glycolysis of Crustacean Muscle.Int. J. Biochem. 2:125–130.

    Google Scholar 

  11. Kuramitsu, H. K. (1970) Concerted Feedback Inhibition of Aspartokinase fromBacillus stearothermophilus.J. Biol. Chem. 245:2991–2997.

    PubMed  Google Scholar 

  12. Nishioka, L. &Woodin, T. (1972) Assay for Phenylpyruvic Acid.Anal. Biochem. 45:617–623.

    PubMed  Google Scholar 

  13. Lyons, J. M. &Raison, J. K. (1970a) Oxidative Activity of Mitochondria Isolated from Plant Tissues Sensitive and Resistant to Chilling Injury.Plant Physiol. 45:386–389.

    PubMed  Google Scholar 

  14. Lyons, J. M. &Raison, J. K. (1970b) A Temperature Induced Transition in Mitochondrial Oxidation: Contrasts Between Cold and Warm Blooded Animals.Comp. Biochem. and Physiol. 37:405–411.

    Google Scholar 

  15. O'Brien, W. E., Ljungdahl, L. G. &Brewer, J. M. (1971) Properties of Methylenetetrahydrofolate Dehydrogenases fromClostridium thermoaceticum andClostridium formicoaceticum.Fed. Proc. 30:#873.

  16. Paule, M. R. &Preiss, J. (1971) Biosynthesis of Bacterial Glycogen X. The Kinetic Mechanism of Adenosine Diphosphoglucose Pyrophosphorylase fromRhodospirillum rubrum.J. Biol. Chem. 246:4602–4609.

    Google Scholar 

  17. Rabinowitz, J. C. &Pricer, W. E., Jr. (1962) Formyltetrahydrofolate Synthetase I. Isolation and Crystallization of the Enzyme.J. Biol. Chem. 237:2898–2902.

    PubMed  Google Scholar 

  18. Raison, J. K., Lyons, J. M. &Thomson, W. W. (1971) The Influence of Membranes on the Temperature — Induced Changes in the Kinetics of Some Respiratory Enzymes of Mitochondria.Arch. Biochem. Biophys. 142:83–90.

    PubMed  Google Scholar 

  19. Somero, G. N. (1969) Enzymic Mechanisms of Temperature Compensation: Immediate and Evolutionary Effects of Temperature on Enzymes of Aquatic Poikilotherms.The American Naturalist. 103:517–530.

    Google Scholar 

  20. Sprossler, B. &Lingens, F. (1970) Eigenschaften der Chorismat-Mutase aus verschiedenenClaviceps- Stammen.Hoppe-Seyler's Z. Physiol. Chem. 351:448–458.

    PubMed  Google Scholar 

  21. Thomas, D. A. &Kuramitsu, H. K. (1971) Biosynthetic L-Threonine Deaminase fromBacillus stearothermophilus I. Catalytic and Regulatory Properties.Arch. Biochem. Biophys. 145:96–104.

    PubMed  Google Scholar 

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Authors and Affiliations

  1. Division of Biochemistry, University of Nevada, 89507, Reno, Nevada

    Leo Nishioka

Authors
  1. Terry Woodin
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  2. William Welch Jr.
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  3. Leo Nishioka
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Woodin, T., Welch, W. & Nishioka, L. Comparative Arrhenius plots of enzyme activity from penicillium. Mycopathologia et Mycologia Applicata 50, 167–178 (1973). https://doi.org/10.1007/BF02049955

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  • DOI: https://doi.org/10.1007/BF02049955

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