Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1965 Oct;90(4):837–842. doi: 10.1128/jb.90.4.837-842.1965

Fructose-1,6-Diphosphatase and Acid Hexose Phosphatase of Escherichia coli1

D G Fraenkel a, B L Horecker a
PMCID: PMC315746  PMID: 4284917

Abstract

Fraenkel, D. G. (Albert Einstein College of Medicine, New York, N.Y.), and B. L. Horecker. Fructose-1,6-diphosphatase and acid hexose phosphatase of Escherichia coli. J. Bacteriol. 90:837–842. 1965.—The conversion of fructose-1,6-diphosphate to fructose-6-phosphate (fructose-1,6-diphosphatase activity) is essential for growth of Escherichia coli on glycerol, acetate, or succinate, but is unnecessary for growth on hexoses or pentoses. It has sometimes been assumed that fructose-1,6-diphosphatase activity is due to a nonspecific acid hexose phosphatase. We have now obtained a number of one-step mutants which have lost the ability to grow on glycerol, succinate, or acetate, but which grow normally on hexoses; these mutants are deficient in a fructose-1,6-diphosphatase which can be assayed spectrophotometrically in the presence of Mg++ and low concentrations of substrate. These mutants still possess the nonspecific acid hexose phosphatase, which does not require Mg++ and is active only at much higher concentrations of fructose-1,6-diphosphate. Evidence is presented to support the hypothesis that the newly described activity is the physiological fructose-1,6-diphosphatase. The acid hexose phosphatase is a different enzyme whose function remains unknown.

Full text

PDF
837

Selected References

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

  1. ANRAKU Y. A NEW CYCLIC PHOSPHODIESTERASE HAVING A 3'-NUCLEOTIDASE ACTIVITY FROM ESCHERICHIA COLI B. I. PURIFICATION AND SOME PROPERTIES OF THE ENZYME. J Biol Chem. 1964 Oct;239:3412–3419. [PubMed] [Google Scholar]
  2. ANRAKU Y. A NEW CYCLIC PHOSPHODIESTERASE HAVING A 3'-NUCLEOTIDASE ACTIVITY FROM ESCHERICHIA COLI B. II. FURTHER STUDIES ON SUBSTRATE SPECIFICITY AND MODE OF ACTION OF THE ENZYME. J Biol Chem. 1964 Oct;239:3420–3424. [PubMed] [Google Scholar]
  3. APP A. A., JAGENDORF A. T. PURIFICATION OF ALKALINE FRUCTOSE DIPHOSPHATASE FROM EUGLENA GRACILIS. Biochim Biophys Acta. 1964 Jun 1;85:427–434. doi: 10.1016/0926-6569(64)90306-2. [DOI] [PubMed] [Google Scholar]
  4. ENGLESBERG E., WATSON J. A., HOFFEE P. A. The glucose effect and the relationship between glucose permease, acid phosphatase, and glucose resistance. Cold Spring Harb Symp Quant Biol. 1961;26:261–276. doi: 10.1101/sqb.1961.026.01.033. [DOI] [PubMed] [Google Scholar]
  5. FOSSITT D. D., BERNSTEIN I. A. FRUCTOSE-1,6-DIPHOSPHATASE FROM PSEUDOMONAS SACCHAROPHILA. J Bacteriol. 1963 Sep;86:598–599. doi: 10.1128/jb.86.3.598-599.1963. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. FRAENKEL D. G., FALCOZ-KELLY F., HORECKER B. L. THE UTILIZATION OF GLUCOSE 6-PHOSPHATE BY GLUCOKINASELESS AND WILD-TYPE STRAINS OF ESCHERICHIA COLI. Proc Natl Acad Sci U S A. 1964 Nov;52:1207–1213. doi: 10.1073/pnas.52.5.1207. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. FRAENKEL D. G., HORECKER B. L. PATHWAYS OF D-GLUCOSE METABOLISM IN SALMONELLA TYPHINMURIUM. A STUDY OF A MUTANT LACKING PHOSPHOGLUCOSE ISOMERASE. J Biol Chem. 1964 Sep;239:2765–2771. [PubMed] [Google Scholar]
  8. FRAENKEL D., OSBORN M. J., HORECKER B. L., SMITH S. M. Metabolism and cell wall structure of a mutant of Salmonella typhimurium deficient in phosphoglucose isomerase. Biochem Biophys Res Commun. 1963 Jun 20;11:423–428. doi: 10.1016/0006-291x(63)90086-x. [DOI] [PubMed] [Google Scholar]
  9. GORINI L., KAUFMAN H. Selecting bacterial mutants by the penicillin method. Science. 1960 Feb 26;131(3400):604–605. doi: 10.1126/science.131.3400.604. [DOI] [PubMed] [Google Scholar]
  10. GOTTO A. M., POGELL B. M. Induction of fructose-1,6-diphosphatase activity in Escherichia coli. Biochem Biophys Res Commun. 1962 Nov 27;9:381–387. doi: 10.1016/0006-291x(62)90020-7. [DOI] [PubMed] [Google Scholar]
  11. HOFSTEN B. V. MUTATIONS AFFECTING THE GLYCONEOGENESIS OF ESCHERICHIA COLI. Biochim Biophys Acta. 1963 Sep 17;76:140–142. [PubMed] [Google Scholar]
  12. KLUNGSOEYR L., ENDRESEN A. INTRACELLULAR PH EFFECT UPON PHOSPHOGLUCOSE ISOMERASE IN ESCHERICHIA COLI. Biochim Biophys Acta. 1964 Nov 22;92:378–387. [PubMed] [Google Scholar]
  13. LEDERBERG J. The beta-d-galactosidase of Escherichia coli, strain K-12. J Bacteriol. 1950 Oct;60(4):381–392. doi: 10.1128/jb.60.4.381-392.1950. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  15. MAGASANIK B. Catabolite repression. Cold Spring Harb Symp Quant Biol. 1961;26:249–256. doi: 10.1101/sqb.1961.026.01.031. [DOI] [PubMed] [Google Scholar]
  16. MANDELL J. D., GREENBERG J. A new chemical mutagen for bacteria, 1-methyl-3-nitro-1-nitrosoguanidine. Biochem Biophys Res Commun. 1960 Dec;3:575–577. doi: 10.1016/0006-291x(60)90064-4. [DOI] [PubMed] [Google Scholar]
  17. MENDICINO J., VASARHELY F. RENAL D-FRUCTOSE 1,6-DIPHOSPHATASE. J Biol Chem. 1963 Nov;238:3528–3534. [PubMed] [Google Scholar]
  18. NEIDHARDT F. C. Mutant of Aerobacter aerogenes lacking glucose repression. J Bacteriol. 1960 Oct;80:536–543. doi: 10.1128/jb.80.4.536-543.1960. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Neu H. C., Heppel L. A. On the surface localization of enzymes in E. coli. Biochem Biophys Res Commun. 1964 Oct 14;17(3):215–219. doi: 10.1016/0006-291x(64)90386-9. [DOI] [PubMed] [Google Scholar]
  20. PASSONNEAU J. V., LOWRY O. H. Phosphofructokinase and the Pasteur effect. Biochem Biophys Res Commun. 1962 Feb 20;7:10–15. doi: 10.1016/0006-291x(62)90134-1. [DOI] [PubMed] [Google Scholar]
  21. POGELL B. M. Enzyme purification by selective elution with substrate from substituted cellulose columns. Biochem Biophys Res Commun. 1962 Apr 20;7:225–230. doi: 10.1016/0006-291x(62)90179-1. [DOI] [PubMed] [Google Scholar]
  22. RACKER E., SCHROEDER E. A. The reductive pentose phosphate cycle. II. Specific C-1 phosphatases for fructose 1,6-diphosphate and sedoheptulose 1,7-diphosphate. Arch Biochem Biophys. 1958 Apr;74(2):326–344. doi: 10.1016/0003-9861(58)90004-3. [DOI] [PubMed] [Google Scholar]
  23. ROBERTS I. Z., WOLFFE E. L. Utilization of labeled fructose-6-phosphate and fructose-1,6-diphosphate by Escherichia coli. Arch Biochem Biophys. 1951 Aug;33(1):165–166. doi: 10.1016/0003-9861(51)90090-2. [DOI] [PubMed] [Google Scholar]
  24. ROGERS D., REITHEL F. J. Acid phosphatases of Escherichia coli. Arch Biochem Biophys. 1960 Jul;89:97–104. doi: 10.1016/0003-9861(60)90018-7. [DOI] [PubMed] [Google Scholar]
  25. TAYLOR A. L., THOMAN M. S. THE GENETIC MAP OF ESCHERICHIA COLI K-12. Genetics. 1964 Oct;50:659–677. doi: 10.1093/genetics/50.4.659. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. TORRIANI A. Influence of inorganic phosphate in the formation of phosphatases by Escherichia coli. Biochim Biophys Acta. 1960 Mar 11;38:460–469. doi: 10.1016/0006-3002(60)91281-6. [DOI] [PubMed] [Google Scholar]
  27. Yu M. T., Kaney A. R., Atwood K. C. Genetic mapping off fructose-1,6-diphosphatase in Escherichia coli. J Bacteriol. 1965 Oct;90(4):1150–1152. doi: 10.1128/jb.90.4.1150-1152.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. von HOFSTEN Acid phosphatase and the growth of Escherichia coli. Biochim Biophys Acta. 1961 Mar 18;48:171–181. doi: 10.1016/0006-3002(61)90529-7. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES