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. 1973 Jan;131(1):83–89. doi: 10.1042/bj1310083

The effect of substitution at C-2 of d-glucose 6-phosphate on the rate of dehydrogenation by glucose 6-phosphate dehydrogenase (from yeast and from rat liver)

Eric M Bessell 1, Peter Thomas 1
PMCID: PMC1177441  PMID: 4578852

Abstract

1. The deoxyfluoro-d-glucopyranose 6-phosphates are substrates for both yeast and rat liver glucose 6-phosphate dehydrogenase. 2. The Vmax. values (relative to d-glucose 6-phosphate) were determined for a series of d-glucose 6-phosphate derivatives substituted at C-2. The Vmax. values decreased with increasing electronegativity of the C-2 substituent. This is consistent with a mechanism involving hydride-ion transfer. 3. 2-Deoxy-d-arabino-hexose 6-phosphate (2-deoxy-d-glucose 6-phosphate) showed substrate inhibition with the yeast enzyme but not with the rat liver enzyme. 4. 2-Amino-2-deoxy-d-glucose 6-phosphate (d-glucosamine 6-phosphate) was a substrate for the yeast enzyme but a competitive inhibitor for the rat liver enzyme. 5. Lineweaver–Burk plots for the d-glucose 6-phosphate derivatives with yeast glucose 6-phosphate dehydrogenase were biphasic.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Anderson W. B., Horne R. N., Nordlie R. C. Glucose dehydrogenase activity of yeast glucose 6-phosphate dehydrogenase. II. Kinetic studies of the mode of activation by bicarbonate, phosphate, and sulfate. Biochemistry. 1968 Nov;7(11):3997–4004. doi: 10.1021/bi00851a029. [DOI] [PubMed] [Google Scholar]
  2. Bessell E. M., Foster A. B., Westwood J. H. Fluorinated carbohydrates. XI. 6-Deoxy-6-fluoro-D-glucose: an improved synthesis and the glycosyl fluoride derivatives. Carbohydr Res. 1971 Aug;19(1):39–48. doi: 10.1016/s0008-6215(00)80310-9. [DOI] [PubMed] [Google Scholar]
  3. Bessell E. M., Foster A. B., Westwood J. H. The use of deoxyfluoro-D-glucopyranoses and related compounds in a study of yeast hexokinase specificity. Biochem J. 1972 Jun;128(2):199–204. doi: 10.1042/bj1280199. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bessell E. M., Thomas P. The deoxyfluoro-D-glucopyranose 6-phosphates and their effect on yeast glucose phosphate isomerase. Biochem J. 1973 Jan;131(1):77–82. doi: 10.1042/bj1310077. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Blomquist C. H. Electronic effects in horse liver alcohol dehydrogenase catalysis. Acta Chem Scand. 1966;20(7):1747–1757. doi: 10.3891/acta.chem.scand.20-1747. [DOI] [PubMed] [Google Scholar]
  6. CLARKE H. B., DATTA S. P., RABIN B. R. Thermodynamic quantities for the dissociation equilibria of biologically important compounds. 5. The second and dissociation of 2-aminoethanol 1-phosphoric acid. Biochem J. 1955 Feb;59(2):209–218. doi: 10.1042/bj0590209. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. CLELAND W. W. Computer programmes for processing enzyme kinetic data. Nature. 1963 May 4;198:463–465. doi: 10.1038/198463a0. [DOI] [PubMed] [Google Scholar]
  8. Cleland W. W. The statistical analysis of enzyme kinetic data. Adv Enzymol Relat Areas Mol Biol. 1967;29:1–32. doi: 10.1002/9780470122747.ch1. [DOI] [PubMed] [Google Scholar]
  9. Conway A., Koshland D. E., Jr Negative cooperativity in enzyme action. The binding of diphosphopyridine nucleotide to glyceraldehyde 3-phosphate dehydrogenase. Biochemistry. 1968 Nov;7(11):4011–4023. doi: 10.1021/bi00851a031. [DOI] [PubMed] [Google Scholar]
  10. DICKENS F., GLOCK G. E. Direct oxidation of glucose-6-phosphate, 6-phosphogluconate and pentose-5-phosphates by enzymes of animal origin. Biochem J. 1951 Nov;50(1):81–95. doi: 10.1042/bj0500081. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Dalziel Keith, Engel Paul C. Antagonistic homotropic interactions as a possible explanation of coenzyme activation of glutamate dehydrogenase. FEBS Lett. 1968 Oct;1(5):349–352. doi: 10.1016/0014-5793(68)80153-x. [DOI] [PubMed] [Google Scholar]
  12. Greiling H., Kisters R. Untersuchungen über die Substratspezifität der Glucose-6-phosphat-Dehydrogenase. Hoppe Seylers Z Physiol Chem. 1965;341(4):172–184. [PubMed] [Google Scholar]
  13. HERS H. G. alpha-Glucosidase deficiency in generalized glycogenstorage disease (Pompe's disease). Biochem J. 1963 Jan;86:11–16. doi: 10.1042/bj0860011. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Koshland D. E., Jr, Neet K. E. The catalytic and regulatory properties of enzymes. Annu Rev Biochem. 1968;37:359–410. doi: 10.1146/annurev.bi.37.070168.002043. [DOI] [PubMed] [Google Scholar]
  15. Matsuda T., Yugari Y. Glucose-6-phosphate dehydrogenase from rat liver. I. Crystallization and properties. J Biochem. 1967 May;61(5):535–540. doi: 10.1093/oxfordjournals.jbchem.a128583. [DOI] [PubMed] [Google Scholar]
  16. SALAS M., VINUELA E., SOLS A. SPONTANEOUS AND ENZYMATICALLY CATALYZED ANOMERIZATION OF GLUCOSE 6-PHOSPHATE AND ANOMERIC SPECIFICITY OF RELATED ENZYMES. J Biol Chem. 1965 Feb;240:561–568. [PubMed] [Google Scholar]
  17. Tsai C. S. Relative reactivities of primary alcohols as substrates of liver alcohol dehydrogenase. Can J Biochem. 1968 Apr;46(4):381–385. doi: 10.1139/o68-056. [DOI] [PubMed] [Google Scholar]
  18. Yue R. H., Noltmann E. A., Kuby S. A. Glucose 6-phosphate dehydrogenase from brewers' yeast (Zwischenferment). 3. Studies on the subunit structure and on the molecular association phenomenon induced by triphosphopyridine nucleotide. J Biol Chem. 1969 Mar 10;244(5):1353–1364. [PubMed] [Google Scholar]

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