Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1976 Mar 1;153(3):551–560. doi: 10.1042/bj1530551

Metal-replacement studies in Bacillus stearothermophilus aldolase and a comparison of the mechanisms of class I and class II aldolases.

H A Hill, R R Lobb, S L Sharp, A M Stokes, J I Harris, R S Jack
PMCID: PMC1172621  PMID: 942370

Abstract

A comparison of the product-inhibition patterns during cleavage of D-fructose 1,6-diphosphate by aldolases from yeast, rabbit muscle and Bacillus stearothermophilus shows an ordered reaction sequence for all three enzymes, with dihydroxyacetone phosphate the last-leaving product. Addition of Zn2+, Co2+, Fe2+, Mn2+ or Cd2+ ions to the inactive apo-(Bacillus stearothermophilus aldolase) restores activity to different extents, whereas Ni2+, Mg2+ or Cu2+ ions have no effect. The cleavage activity of this aldolase is not enhanced by added K+ ion. The effects of metal replacement on thermal stability, Km and Vmax. are given and the possible role of the metal is discussed in the light of these results.

Full text

PDF
551

Selected References

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

  1. Biellmann J. F., O'Connell E. L., Rose I. A. Secondary isotope effects in reactions catalyzed by yeast and muscle aldolase. J Am Chem Soc. 1969 Nov 5;91(23):6484–6488. doi: 10.1021/ja01051a053. [DOI] [PubMed] [Google Scholar]
  2. De la Mare S., Coulson A. F., Knowles J. R., Priddle J. D., Offord R. E. Active-site labelling of triose phosphate isomerase. The reaction of bromohydroxyacetone phosphate with a unique glutamic acid residue and the migration of the label to tyrosine. Biochem J. 1972 Sep;129(2):321–331. doi: 10.1042/bj1290321. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. HORECKER B. L., ROWLEY P. T., GRAZI E., CHENG T., TCHOLA O. THE MECHANISM OF ACTION OF ALDOLASES. IV. LYSINE AS THE SUBSTRATE-BINDING SITE. Biochem Z. 1963;338:36–51. [PubMed] [Google Scholar]
  4. Harris C. E., Kobes R. D., Teller D. C., Rutter W. J. The molecular characteristics of yeast aldolase. Biochemistry. 1969 Jun;8(6):2442–2454. doi: 10.1021/bi00834a029. [DOI] [PubMed] [Google Scholar]
  5. Heron E. J., Caprioli R. M. 18O studies of the mechanisms of yeast and muscle aldolases. Biochemistry. 1974 Oct 8;13(21):4371–4375. doi: 10.1021/bi00718a020. [DOI] [PubMed] [Google Scholar]
  6. Ingram J. M. Fructose diphosphate aldolase from Fusarium oxysporum f. lycopersici. 3. Studies on the mechanism of reaction. Can J Biochem. 1967 Dec;45(12):1909–1917. doi: 10.1139/o67-224. [DOI] [PubMed] [Google Scholar]
  7. Ingram J. M., Hochster R. M. Purification and properties of fructose diphosphate aldolase from Fusarium oxysporum F. lycopersici. Can J Biochem. 1967 Jun;45(6):929–936. doi: 10.1139/o67-103. [DOI] [PubMed] [Google Scholar]
  8. Kobes R. D., Simpson R. T., Vallee R. L., Rutter W. J. A functional role of metal ions in a class II aldolase. Biochemistry. 1969 Feb;8(2):585–588. doi: 10.1021/bi00830a018. [DOI] [PubMed] [Google Scholar]
  9. Lai C. Y., Horecker B. L. Aldolase: a model for enzyme structure-function relationships. Essays Biochem. 1972;8:149–178. [PubMed] [Google Scholar]
  10. MEHLER A. H., BLOOM B. Interaction between rabbit muscle aldolase and dihydroxyacetone phosphate. J Biol Chem. 1963 Jan;238:105–107. [PubMed] [Google Scholar]
  11. Mehler A. H., Cusic M. E., Jr Aldolase reaction with sugar diphosphates. Science. 1967 Mar 3;155(3766):1101–1103. doi: 10.1126/science.155.3766.1101. [DOI] [PubMed] [Google Scholar]
  12. Mildvan A. S., Kobes R. D., Rutter W. J. Magnetic resonance studies of the role of the divalent cation in the mechanism of yeast aldolase. Biochemistry. 1971 Mar 30;10(7):1191–1204. doi: 10.1021/bi00783a016. [DOI] [PubMed] [Google Scholar]
  13. Model P., Ponticorvo L., Rittenberg D. Catalysis of an oxygen-exchange reaction of fructose 1,6-diphosphate and fructose 1-phosphate with water by rabbit muscle aldolase. Biochemistry. 1968 Apr;7(4):1339–1347. doi: 10.1021/bi00844a014. [DOI] [PubMed] [Google Scholar]
  14. Morse D. E., Horecker B. L. The mechanism of action of aldolases. Adv Enzymol Relat Areas Mol Biol. 1968;31:125–181. doi: 10.1002/9780470122761.ch4. [DOI] [PubMed] [Google Scholar]
  15. Quiocho F. A., Lipscomb W. N. Carboxypeptidase A: a protein and an enzyme. Adv Protein Chem. 1971;25:1–78. doi: 10.1016/s0065-3233(08)60278-8. [DOI] [PubMed] [Google Scholar]
  16. RICHARDS O. C., RUTTER W. J. Comparative properties of yeast and muscle aldolase. J Biol Chem. 1961 Dec;236:3185–3192. [PubMed] [Google Scholar]
  17. ROSE I. A., O'CONNELL E. L., MEHLER A. H. MECHANISM OF THE ALDOLASE REACTION. J Biol Chem. 1965 Apr;240:1758–1765. [PubMed] [Google Scholar]
  18. ROSE I. A., RIEDER S. V. Studies on the mechanism on the aldolase reaction; isotope exchange reactions of muscle and yeast aldolase. J Biol Chem. 1958 Mar;231(1):315–329. [PubMed] [Google Scholar]
  19. RUTTER W. J. EVOLUTION OF ALDOLASE. Fed Proc. 1964 Nov-Dec;23:1248–1257. [PubMed] [Google Scholar]
  20. Riordan J. F., Christen P. Carbanion intermediates in the reaction of yeast and muscle aldolase. Biochemistry. 1969 Jun;8(6):2381–2386. doi: 10.1021/bi00834a019. [DOI] [PubMed] [Google Scholar]
  21. Rose I. A., O'Connell E. L. Studies on the interaction of aldolase with substrate analogues. J Biol Chem. 1969 Jan 10;244(1):126–134. [PubMed] [Google Scholar]
  22. SPOLTER P. D., ADELMAN R. C., WEINHOUSE S. DISTINCTIVE PROPERTIES OF NATIVE AND CARBOXYPEPTIDASE-TREATED ALDOLASES OF RABBIT MUSCLE AND LIVER. J Biol Chem. 1965 Mar;240:1327–1337. [PubMed] [Google Scholar]
  23. Sugimoto S., Noso Y. Thermal properties of fructose-I,6-diphosphate aldolase from thermophilic bacteria. Biochim Biophys Acta. 1971 Apr 14;235(1):210–221. doi: 10.1016/0005-2744(71)90049-0. [DOI] [PubMed] [Google Scholar]
  24. THIERS R. E. Contamination in trace element analysis and its control. Methods Biochem Anal. 1957;5:273–335. doi: 10.1002/9780470110218.ch6. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES