Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1986 Jul 15;237(2):469–476. doi: 10.1042/bj2370469

Hydrolysis of a naturally occurring beta-glucoside by a broad-specificity beta-glucosidase from liver.

K L LaMarco, R H Glew
PMCID: PMC1147008  PMID: 3099756

Abstract

We have isolated from guinea-pig liver a broad-specificity beta-glucosidase of unknown function that utilizes as its substrate non-physiological aryl glycosides (e.g. 4-methylumbelliferyl beta-D-glucopyranoside, p-nitrophenyl beta-D-glucopyranoside). The present paper documents that this enzyme can be inhibited by various naturally occurring glycosides, including L-picein, dhurrin and glucocheirolin. In addition, L-picein, which acts as a competitive inhibitor of the broad-specificity beta-glucosidase (Ki 0.65 mM), is also a substrate for this enzyme (Km 0.63 mM; Vmax. 277,000 units/mg). Heat-denaturation, kinetic competition studies, chromatographic properties and pH optima all argue strongly that the broad-specificity beta-glucosidase is responsible for the hydrolysis of both the non-physiological aryl glycosides and L-picein. This paper demonstrates that beta-glucosidase can catalyse the hydrolysis of a natural glycoside, and may provide a key to understanding the function of this enigmatic enzyme. A possible role in the metabolism of xenobiotic compounds is discussed.

Full text

PDF
469

Selected References

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

  1. BRADY R. O., KANFER J. N., SHAPIRO D. METABOLISM OF GLUCOCEREBROSIDES. II. EVIDENCE OF AN ENZYMATIC DEFICIENCY IN GAUCHER'S DISEASE. Biochem Biophys Res Commun. 1965 Jan 18;18:221–225. doi: 10.1016/0006-291x(65)90743-6. [DOI] [PubMed] [Google Scholar]
  2. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  3. Cleland W. W. Statistical analysis of enzyme kinetic data. Methods Enzymol. 1979;63:103–138. doi: 10.1016/0076-6879(79)63008-2. [DOI] [PubMed] [Google Scholar]
  4. Dance N., Price R. G., Robinson D., Stirling J. L. Beta-galactosidase, beta-glucosidase and N-acetyl-beta-glucosaminidase in human kidney. Clin Chim Acta. 1969 May;24(2):189–197. doi: 10.1016/0009-8981(69)90311-8. [DOI] [PubMed] [Google Scholar]
  5. Daniels L. B., Coyle P. J., Chiao Y. B., Glew R. H., Labow R. S. Purification and characterization of a cytosolic broad specificity beta-glucosidase from human liver. J Biol Chem. 1981 Dec 25;256(24):13004–13013. [PubMed] [Google Scholar]
  6. Dorling P. R., Huxtable C. R., Vogel P. Lysosomal storage in Swainsona spp. toxicosis: an induced mannosidosis. Neuropathol Appl Neurobiol. 1978 Jul-Aug;4(4):285–295. doi: 10.1111/j.1365-2990.1978.tb00547.x. [DOI] [PubMed] [Google Scholar]
  7. Glew R. H., Peters S. P., Christopher A. R. Isolation and characterization of beta-glucosidase from the cytosol of rat kidney cortex. Biochim Biophys Acta. 1976 Jan 23;422(1):179–199. doi: 10.1016/0005-2744(76)90018-8. [DOI] [PubMed] [Google Scholar]
  8. LOWRY O. H., PASSONNEAU J. V., HASSELBERGER F. X., SCHULZ D. W. EFFECT OF ISCHEMIA ON KNOWN SUBSTRATES AND COFACTORS OF THE GLYCOLYTIC PATHWAY IN BRAIN. J Biol Chem. 1964 Jan;239:18–30. [PubMed] [Google Scholar]
  9. LaMarco K. L., Glew R. H. Galactosylsphingosine inhibition of the broad-specificity cytosolic beta-glucosidase of human liver. Arch Biochem Biophys. 1985 Feb 1;236(2):669–676. doi: 10.1016/0003-9861(85)90672-1. [DOI] [PubMed] [Google Scholar]
  10. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  11. Ockerman P. A. Mannosidosis: isolation of oligosaccharide storage material from brain. J Pediatr. 1969 Sep;75(3):360–365. doi: 10.1016/s0022-3476(69)80259-3. [DOI] [PubMed] [Google Scholar]
  12. Peters S. P., Coyle P., Glew R. H. Differentiation of beta-glucocerebrosidase from beta-glucosidase in human tissues using sodium taurocholate. Arch Biochem Biophys. 1976 Aug;175(2):569–582. doi: 10.1016/0003-9861(76)90547-6. [DOI] [PubMed] [Google Scholar]
  13. Peters S. P., Lee R. E., Glew R. H. A microassay for Gaucher's disease. Clin Chim Acta. 1975 May 1;60(3):391–396. doi: 10.1016/0009-8981(75)90083-2. [DOI] [PubMed] [Google Scholar]
  14. Saul R., Chambers J. P., Molyneux R. J., Elbein A. D. Castanospermine, a tetrahydroxylated alkaloid that inhibits beta-glucosidase and beta-glucocerebrosidase. Arch Biochem Biophys. 1983 Mar;221(2):593–597. doi: 10.1016/0003-9861(83)90181-9. [DOI] [PubMed] [Google Scholar]
  15. Umoh I. B., Ogunkoya F. O., Maduagwu E. N., Oke O. L. Effect of thiamin status on the metabolism of linamarin in rats. Ann Nutr Metab. 1985;29(5):319–324. doi: 10.1159/000176987. [DOI] [PubMed] [Google Scholar]

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

RESOURCES