Skip to main content
PMC home page
Plant Physiology logoLink to Plant Physiology
. 1973 May;51(5):960–966. doi: 10.1104/pp.51.5.960

Hexokinase from Maize Endosperm and Scutellum 1

Edward L Cox a, David B Dickinson a
PMCID: PMC366382  PMID: 16658446

Abstract

Hexokinase (EC 2.7.1.1) was isolated from endosperm and scutellum of developing and germinating maize (Zea mays) seeds. With fructose as the variable substate, Michaelis constant values for the scutellum enzyme were about onethird those of the endosperm enzyme (0.05 versus 0.15 mm), and no developmental differences were observed. With glucose as the variable substrate, Michaelis constant values were all in the range 0.1 to 0.2 mm. The enzyme preparation from germinating scutellum was studied further; when glucose was varied over a wide range, a Michaelis constant of 3.4 mm was observed in addition to the much lower Michaelis constant noted above. This low affinity binding of glucose may have regulatory significance and may indicate the presence of a glucokinase in addition to hexokinase.

Full text

PDF
962

Selected References

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

  1. BALLARD F. J. GLUCOSE UTILIZATION IN MAMMALIAN LIVER. Comp Biochem Physiol. 1965 Mar;14:437–443. doi: 10.1016/0010-406x(65)90218-5. [DOI] [PubMed] [Google Scholar]
  2. Bachelard H. S. Glucose-phosphorylating enzyme with high Km in human brain. Nature. 1967 Aug 26;215(5104):959–960. doi: 10.1038/215959a0. [DOI] [PubMed] [Google Scholar]
  3. DIPIETRO D. L., SHARMA C., WEINHOUSE S. Studies on glucose phosphorylation in rat liver. Biochemistry. 1962 May 25;1:455–462. doi: 10.1021/bi00909a014. [DOI] [PubMed] [Google Scholar]
  4. DOWD J. E., RIGGS D. S. A COMPARISON OF ESTIMATES OF MICHAELIS-MENTEN KINETIC CONSTANTS FROM VARIOUS LINEAR TRANSFORMATIONS. J Biol Chem. 1965 Feb;240:863–869. [PubMed] [Google Scholar]
  5. Gazith J., Schulze I. T., Gooding R. H., Womack F. C., Colowick S. P. Multiple forms and subunits of yeast hexokinase. Ann N Y Acad Sci. 1968 Jun 14;151(1):307–331. doi: 10.1111/j.1749-6632.1968.tb11898.x. [DOI] [PubMed] [Google Scholar]
  6. Hopper J. E., Dickinson D. B. Partial purification and sugar nucleotide inhibition of UDP-glucose pyrophosphorylase from Lilium longiflorum pollen. Arch Biochem Biophys. 1972 Feb;148(2):523–535. doi: 10.1016/0003-9861(72)90171-3. [DOI] [PubMed] [Google Scholar]
  7. Ingle J., Beevers L., Hageman R. H. Metabolic Changes Associated with the Germination of Corn. I. Changes in Weight and Metabolites and their Redistribution in the Embryo Axis, Scutellum, and Endosperm. Plant Physiol. 1964 Sep;39(5):735–740. doi: 10.1104/pp.39.5.735. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. KATZEN H. M., SODERMAN D. D., NITOWSKY H. M. KINETIC AND ELECTROPHORETIC EVIDENCE FOR MULTIPLE FORMS OF GLUCOSE-ATP PHOSPHOTRANSFERASE ACTIVITY FROM HUMAN CELL CULTURES AND RAT LIVER. Biochem Biophys Res Commun. 1965 Apr 23;19:377–382. doi: 10.1016/0006-291x(65)90472-9. [DOI] [PubMed] [Google Scholar]
  9. Katzen H. M. The multiple forms of mammalian hexokinase and their significance to the action of insulin. Adv Enzyme Regul. 1967;5:335–356. doi: 10.1016/0065-2571(67)90025-8. [DOI] [PubMed] [Google Scholar]
  10. Kosow D. P., Rose I. A. Activators of yeast hexokinase. J Biol Chem. 1971 Apr 25;246(8):2618–2625. [PubMed] [Google Scholar]
  11. Kosow D. P., Rose I. A. Product inhibition of the hexokinases. J Biol Chem. 1970 Jan 10;245(1):198–204. [PubMed] [Google Scholar]
  12. MEDINA A., SOLS A. A specific fructokinase in peas. Biochim Biophys Acta. 1956 Feb;19(2):378–379. doi: 10.1016/0006-3002(56)90445-0. [DOI] [PubMed] [Google Scholar]
  13. Meunier J. C., Buc J., Ricard J. Purification and characterization of wheat germ hexokinases. FEBS Lett. 1971 Apr 12;14(1):25–28. doi: 10.1016/0014-5793(71)80266-1. [DOI] [PubMed] [Google Scholar]
  14. Newsholme E. A., Robinson J., Taylor K. A radiochemical enzymatic activity assay for glycerol kinase and hexokinase. Biochim Biophys Acta. 1967 Mar 15;132(2):338–346. doi: 10.1016/0005-2744(67)90153-2. [DOI] [PubMed] [Google Scholar]
  15. Purich D. L., Fromm H. J. The kinetics and regulation of rat brain hexokinase. J Biol Chem. 1971 Jun 10;246(11):3456–3463. [PubMed] [Google Scholar]
  16. Ramel A. H., Rustum Y. M., Jones J. G., Barnard E. A. Yeast Hexokinase. IV. Multiple forms of hexokinase in the yeast cell. Biochemistry. 1971 Sep 14;10(19):3499–3508. doi: 10.1021/bi00795a003. [DOI] [PubMed] [Google Scholar]
  17. SALAS J., SALAS M., VINUELA E., SOLS A. GLUCOKINASE OF RABBIT LIVER. J Biol Chem. 1965 Mar;240:1014–1018. [PubMed] [Google Scholar]
  18. SALTMAN P. Hexokinase in higher plants. J Biol Chem. 1953 Jan;200(1):145–154. [PubMed] [Google Scholar]
  19. SLEIN M. W., CORI G. T., CORI C. F. A comparative study of hexokinase from yeast and animal tissues. J Biol Chem. 1950 Oct;186(2):763–780. [PubMed] [Google Scholar]
  20. Sapag-Hagar M., Marco R., Sols A. Distribution of hexokinase and glucokinase between parenchymal and non-parenchymal cells of rat liver. FEBS Lett. 1969 Apr;3(1):68–71. doi: 10.1016/0014-5793(69)80099-2. [DOI] [PubMed] [Google Scholar]
  21. Schimke R. T., Grossbard L. Studies on isozymes of hexokinase in animal tissues. Ann N Y Acad Sci. 1968 Jun 14;151(1):332–350. doi: 10.1111/j.1749-6632.1968.tb11899.x. [DOI] [PubMed] [Google Scholar]
  22. Shannon J. C. Carbon-14 Distribution in Carbohydrates of Immature Zea mays. Kernels Following CO(2) Treatment of Intact Plants. Plant Physiol. 1968 Aug;43(8):1215–1220. doi: 10.1104/pp.43.8.1215. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Tsai C. Y., Salamini F., Nelson O. E. Enzymes of carbohydrate metabolism in the developing endosperm of maize. Plant Physiol. 1970 Aug;46(2):299–306. doi: 10.1104/pp.46.2.299. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Ureta T., González C., Niemeyer H. Comparative studies on glucose phosphorylating isoenzymes of vertebrates. II. Chromatographic patterns of glucokinase and hexokinases in the liver of rodents. Comp Biochem Physiol B. 1971 Sep 15;40(1):81–91. doi: 10.1016/0305-0491(71)90064-2. [DOI] [PubMed] [Google Scholar]
  25. WALKER D. G. ON THE PRESENCE OF TWO SOLUBLE GLUCOSE-PHOSPHORYLATING ENZYMES IN ADULT LIVER AND THE DEVELOPMENT OF ONE OF THESE AFTER BIRTH. Biochim Biophys Acta. 1963 Oct 1;77:209–226. doi: 10.1016/0006-3002(63)90494-3. [DOI] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES