Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1971 Feb;68(2):416–419. doi: 10.1073/pnas.68.2.416

Photoinactivation of Aldolases by Pyridoxal Phosphate and Its Analogues

L C Davis 1,*, G Ribereau-Gayon 1, B L Horecker 1
PMCID: PMC388951  PMID: 5277095

Abstract

Pyridoxal phosphate can act as a specific photosensitizer for amino acid residues in rabbit muscle and spinach leaf aldolases, but the residues affected depend on the pH of the reaction. Below pH 8 one histidine residue per enzyme subunit is destroyed; above pH 8.5 there is little loss of histidine, and photoinactivation is associated with the destruction of specific tyrosine residues, particularly the COOH-terminal residues. Pyridoxal and 4-pyridinecarboxaldehyde are much less effective than pyridoxal phosphate at neutral pH, but are similar to pyridoxal phosphate in their photosensitizing activity at the higher pH. Compounds lacking the aldehyde group or the pyridine ring show little or no activity. A number of other enzymes, including α-glycerophosphate dehydrogenase, glucose-6-phosphate dehydrogenase, and yeast hexokinase, were also photoinactivated in the presence of pyridoxal phosphate; however, rabbit liver aldolase and two isomerases tested were completely resistant. The results suggest that certain enzymes, including rabbit muscle and spinach aldolases, but not rabbit liver aldolase, contain a specific site which interacts with pyridoxal phosphate, and that the conformation of this site changes in the pH range between 8.0 and 8.5

Full text

PDF
416

Selected References

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

  1. CRESTFIELD A. M., MOORE S., STEIN W. H. The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins. J Biol Chem. 1963 Feb;238:622–627. [PubMed] [Google Scholar]
  2. DRECHSLER E. R., BOYER P. D., KOWALSKY A. G. The catalytic activity of carboxypeptidase-degraded aldolase. J Biol Chem. 1959 Oct;234:2627–2634. [PubMed] [Google Scholar]
  3. Davis L. C., Brox L. W., Gracy R. W., Ribereau-Gayon G., Horecker B. L. Photosensitization of specific histidine residues of rabbit muscle and spinach leaf aldolases by pyridoxal phosphate. Arch Biochem Biophys. 1970 Sep;140(1):215–222. doi: 10.1016/0003-9861(70)90025-1. [DOI] [PubMed] [Google Scholar]
  4. Domschke W., Domagk G. F. Proteinstruktur und Enzymaktivität, 3. Die Hemmbarkeit der Glucose-6-phosphat-dehydrogenase und anderer Enzyme des Zuckerstoffwechsels durch Pyridoxal-5-phosphat. Hoppe Seylers Z Physiol Chem. 1969 Sep;350(9):1111–1116. [PubMed] [Google Scholar]
  5. Gracy R. W., Lacko A. G., Horecker B. L. Subunit structure and chemical properties of rabbit liver aldolase. J Biol Chem. 1969 Jul 25;244(14):3913–3919. [PubMed] [Google Scholar]
  6. Hoffee P., Lai C. Y., Pugh E. L., Horecker B. L. The function of histidine residues in rabbit muscle aldolase. Proc Natl Acad Sci U S A. 1967 Jan;57(1):107–113. doi: 10.1073/pnas.57.1.107. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Koida M., Lai C. Y., Horecker B. L. Subunit structure of rabbit muscle aldolase: extent of homology of the alpha and beta subunits and age-dependent changes in their ratio. Arch Biochem Biophys. 1969 Nov;134(2):623–631. doi: 10.1016/0003-9861(69)90326-9. [DOI] [PubMed] [Google Scholar]
  8. 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]
  9. 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]
  10. RUTTER W. J., RICHARDS O. C., WOODFIN B. M. Comparative studies of liver and muscle aldolase. I. Effect of carboxypeptidase on catalytic activity. J Biol Chem. 1961 Dec;236:3193–3197. [PubMed] [Google Scholar]
  11. Rapoport G., Davis L., Horecker B. L. The subunit structure of the fructose diphosphate aldolase from spinach leaf. Arch Biochem Biophys. 1969 Jun;132(1):286–293. doi: 10.1016/0003-9861(69)90364-6. [DOI] [PubMed] [Google Scholar]
  12. Rippa M., Pontremoli S. Pyridoxal 5'-phosphate as a specific photosensitizer for histidine residue at the active site of 6-phosphogluconate dehydrogenase. Arch Biochem Biophys. 1969 Aug;133(1):112–118. doi: 10.1016/0003-9861(69)90494-9. [DOI] [PubMed] [Google Scholar]
  13. Shapiro S., Enser M., Pugh E., Horecker B. L. The effect of pyridoxal phosphate on rabbit muscle aldolase. Arch Biochem Biophys. 1968 Nov;128(2):554–562. doi: 10.1016/0003-9861(68)90062-3. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES