Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1966 Jan;98(1):94–99. doi: 10.1042/bj0980094

The inhibition of enzymes by beryllium

Molly Thomas 1, W N Aldridge 1
PMCID: PMC1264799  PMID: 4287187

Abstract

1. The action of beryllium on the following enzymes has been examined: alkaline phosphatase (Escherichia coli and kidney), acid phosphatase, phosphoprotein phosphatase, apyrase (potato), adenosine triphosphatase (liver nuclei, liver mitochondria, brain microsomes), glucose 6-phosphatase, polysaccharide phosphorylases a and b, phosphoglucomutase, hexokinase, phosphoglyceromutase, ribonuclease, A-esterase (rabbit serum), cholinesterase (horse serum), chymotrypsin. Alkaline phosphatase and phosphoglucomutase are inhibited by 1μm-beryllium sulphate whereas the other enzymes are largely unaffected by 1mm-beryllium sulphate. 2. Possible mechanisms for the inhibition of phosphoglucomutase and alkaline phosphatase are discussed.

Full text

PDF
96

Selected References

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

  1. ALDRIDGE W. N. Adenosine triphosphatase in the microsomal fraction from rat brain. Biochem J. 1962 Jun;83:527–533. doi: 10.1042/bj0830527. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. ALDRIDGE W. N., BARNES J. M., DENZ F. A. Experimental beryllium poisoning. Br J Exp Pathol. 1949 Oct;30(5):375–389. [PMC free article] [PubMed] [Google Scholar]
  3. ALDRIDGE W. N. Beryllium and alkaline phosphatase. Nature. 1950 May 13;165(4202):772–772. doi: 10.1038/165772a0. [DOI] [PubMed] [Google Scholar]
  4. ALDRIDGE W. N., EMERY R. C., STREET B. W. A tissue homogenizer. Biochem J. 1960 Nov;77:326–327. doi: 10.1042/bj0770326. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. ALDRIDGE W. N. Liver and brain mitochondria. Biochem J. 1957 Nov;67(3):423–431. doi: 10.1042/bj0670423. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. ALDRIDGE W. N., STONER H. B. The behaviour of liver mitochondria isolated from rats with different body temperatures after limb ischaemia or after injection of 3:5-dinitro-ocresol. Biochem J. 1960 Jan;74:148–154. doi: 10.1042/bj0740148. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. ALDRIDGE W. N. Serum esterases. I. Two types of esterase (A and B) hydrolysing p-nitrophenyl acetate, propionate and butyrate, and a method for their determination. Biochem J. 1953 Jan;53(1):110–117. doi: 10.1042/bj0530110. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. ALDRIDGE W. N., THRELFALL C. J. Trialkyltins and oxidative phosphorylation. The [32P]phosphate-adenosine triphosphate-exchange reaction. Biochem J. 1961 May;79:214–219. doi: 10.1042/bj0790214. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. ALDRIDGE W. N. The biochemistry of organotin compounds: trialkyltins and oxidative phosphorylation. Biochem J. 1958 Jul;69(3):367–376. doi: 10.1042/bj0690367. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. ALDRIDGE W. N. The differentiation of true and pseudo cholinesterase by organophosphorus compounds. Biochem J. 1953 Jan;53(1):62–67. doi: 10.1042/bj0530062. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. AXELROD B., SALTMAN P., BANDURSKI R. S., BAKER R. S. Phosphonexokinase in higher plants. J Biol Chem. 1952 May;197(1):89–96. [PubMed] [Google Scholar]
  12. Abul-Fadl M. A., King E. J. Purification of alkaline phosphatase. Biochem J. 1949;44(4):428–431. doi: 10.1042/bj0440428. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Ashmore J., Hastings A. B., Nesbett F. B. THE EFFECT OF DIABETES AND FASTING ON LIVER GLUCOSE-6-PHOSPHATASE. Proc Natl Acad Sci U S A. 1954 Aug;40(8):673–678. doi: 10.1073/pnas.40.8.673. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. BERTHET J., DE DUVE C. Tissue fractionation studies. I. The existence of a mitochondria-linked, enzymically inactive form of acid phosphatase in rat-liver tissue. Biochem J. 1951 Dec;50(2):174–181. doi: 10.1042/bj0500174. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Bailey K., Webb E. C. Purification and properties of yeast pyrophosphatase. Biochem J. 1944;38(5):394–398. doi: 10.1042/bj0380394. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. COCHRAN K. W., ZERWIC M. M., DUBOIS K. P. Studies on the mechanism of acute beryllium poisoning. J Pharmacol Exp Ther. 1951 Jul;102(3):165–178. [PubMed] [Google Scholar]
  17. COOPER R. THE BIOSYNTHESIS OF COPROPORPHYRINOGEN, MAGNESIUM PROTOPORPHYRIN MONOMETHYL ESTER AND BACTERIOCHLOROPHYLL BY RHODOPSEUDOMONAS CAPSULATA. Biochem J. 1963 Oct;89:100–108. doi: 10.1042/bj0890100. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. COWGILL R. W., PIZER L. I. Purification and some properties of phosphorylglyceric acid mutase from rabbit skeletal muscle. J Biol Chem. 1956 Dec;223(2):885–895. [PubMed] [Google Scholar]
  19. Dubois K. P., Cochran K. W., Mazur M. Inhibition of Phosphatases by Beryllium and Antagonism of the Inhibition by Manganese. Science. 1949 Oct 21;110(2860):420–422. doi: 10.1126/science.110.2860.420. [DOI] [PubMed] [Google Scholar]
  20. ENGSTROM L. Further studies on the incorporation of inorganic phosphate into calf-intestinal alkaline phosphatase. Biochim Biophys Acta. 1961 Nov 25;54:179–185. doi: 10.1016/0006-3002(61)90951-9. [DOI] [PubMed] [Google Scholar]
  21. FELDMAN I., HAVILL J. R., NEUMAN W. F. The state of beryllium in blood plasma. Arch Biochem Biophys. 1953 Oct;46(2):443–453. doi: 10.1016/0003-9861(53)90215-x. [DOI] [PubMed] [Google Scholar]
  22. GAREN A., LEVINTHAL C. A fine-structure genetic and chemical study of the enzyme alkaline phosphatase of E. coli. I. Purification and characterization of alkaline phosphatase. Biochim Biophys Acta. 1960 Mar 11;38:470–483. doi: 10.1016/0006-3002(60)91282-8. [DOI] [PubMed] [Google Scholar]
  23. GRISOLIA S., JOYCE B. K., FERNANDEZ M. Studies on the mechanism of action of phosphoglyceromutases. Biochim Biophys Acta. 1961 Jun 10;50:81–89. doi: 10.1016/0006-3002(61)91063-0. [DOI] [PubMed] [Google Scholar]
  24. GUTFREUND H., HAMMOND B. R. Records of pH changes during enzyme reactions and kinetic studies with yeast hexokinase. Nature. 1963 May 18;198:667–670. doi: 10.1038/198667a0. [DOI] [PubMed] [Google Scholar]
  25. HARDY H. L. Reaction to toxic beryllium compounds: terminology. J Occup Med. 1962 Oct;4:532–534. [PubMed] [Google Scholar]
  26. HASS L. F., BOYER P. D., REYNARD A. M. Studies on possible phosphoryl enzyme formation in catalysis by hexokinase, pyruvate kinase, and glucose 6-phosphatase. J Biol Chem. 1961 Aug;236:2284–2291. [PubMed] [Google Scholar]
  27. HOKIN L. E., HOKIN M. R., MATHISON D. Phosphatidic acid phosphatase in the erythrocyte membrane. Biochim Biophys Acta. 1963 Mar 12;67:485–497. doi: 10.1016/0006-3002(63)91853-5. [DOI] [PubMed] [Google Scholar]
  28. HURST R. O., LITTLE J. A., BUTLER G. C. The enzymatic degradation of thymonucleic acid. II. The hydrolysis of oligonucleotides. J Biol Chem. 1951 Feb;188(2):705–715. [PubMed] [Google Scholar]
  29. KLEMPERER F. W. The effect of beryllium on certain enzymes. J Biol Chem. 1950 Nov;187(1):189–196. [PubMed] [Google Scholar]
  30. KOSHLAND D. E., Jr, BUDENSTEIN Z., KOWALSKY A. Mechanism of hydrolysis of adenosinetriphosphate catalyzed by purified muscle proteins. J Biol Chem. 1954 Nov;211(1):279–287. [PubMed] [Google Scholar]
  31. KOSHLAND D. E., Jr CONFORMATION CHANGES AT THE ACTIVE SITE DURING ENZYME ACTION. Fed Proc. 1964 May-Jun;23:719–726. [PubMed] [Google Scholar]
  32. KREBS E. G., KENT A. B., FISCHER E. H. The muscle phosphorylase b kinase reaction. J Biol Chem. 1958 Mar;231(1):73–83. [PubMed] [Google Scholar]
  33. LEE K. H., EILER J. J. Temperature dependent characteristics of an adenylpyrophosphatase preparation from potatoes. Science. 1951 Oct 12;114(2963):393–395. doi: 10.1126/science.114.2963.393-a. [DOI] [PubMed] [Google Scholar]
  34. MALMSTROM B. G. Metal-ion specificity in the activation of enolase. Arch Biochem Biophys. 1955 Oct;58(2):381–397. doi: 10.1016/0003-9861(55)90138-7. [DOI] [PubMed] [Google Scholar]
  35. MILSTEIN C., SANGER F. An amino acid sequence in the active centre of phosphoglucomutase. Biochem J. 1961 Jun;79:456–469. doi: 10.1042/bj0790456. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. MORTON R. K. Some properties of alkaline phosphatase of cow's milk and calf intestinal mucosa. Biochem J. 1955 Aug;60(4):573–582. doi: 10.1042/bj0600573. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. NAJJAR V. A., PULLMAN M. E. The occurrence of a group transfer involving enzyme (phosphoglucomutase) and substrate. Science. 1954 May 7;119(3097):631–634. doi: 10.1126/science.119.3097.631. [DOI] [PubMed] [Google Scholar]
  38. PAIGEN K. The properties of particulate phosphoprotein phosphatase. J Biol Chem. 1958 Aug;233(2):388–394. [PubMed] [Google Scholar]
  39. PARKS R. E., Jr, PLAUT G. W. A manometric assay for chymotrypsin. J Biol Chem. 1953 Aug;203(2):755–761. [PubMed] [Google Scholar]
  40. PIZER L. I. Properties of the phosphoprotein-phosphoglyceric mutase. J Biol Chem. 1960 Apr;235:895–901. [PubMed] [Google Scholar]
  41. PLOCKE D. J., LEVINTHAL C., VALLEE B. L. Alkaline phosphatase of Escherichia coli: a zinc metalloenzyme. Biochemistry. 1962 May 25;1:373–378. doi: 10.1021/bi00909a001. [DOI] [PubMed] [Google Scholar]
  42. PLOCKE D. J., VALLEE B. L. Interaction of alkaline phosphatase of E. coli with metal ions and chelating agents. Biochemistry. 1962 Nov;1:1039–1043. doi: 10.1021/bi00912a014. [DOI] [PubMed] [Google Scholar]
  43. REEVES A. L., VORWALD A. J. The humoral transport of beryllium. J Occup Med. 1961 Dec;3:567–574. [PubMed] [Google Scholar]
  44. ROBINSON J. P., NAJJAR V. A. Time dependent activation of phospho-glucomutase by magnesium and imidazole. Fed Proc. 1961 Sep;2:90–94. [PubMed] [Google Scholar]
  45. ROCHE J., THOAI N. V. Phosphatase alkaline. Adv Enzymol Relat Subj Biochem. 1950;10:83–122. [PubMed] [Google Scholar]
  46. SCHUBERT J., LINDENBAUM A. Studies on the mechanism of protection by aurintricarboxylic acid in beryllium poisoning. II. Equilibria involving alkaline phosphatase. J Biol Chem. 1954 May;208(1):359–368. [PubMed] [Google Scholar]
  47. SCHWARTZ J. H., LIPMANN F. Phosphate incorporation into alkaline phosphatase of E. coli. Proc Natl Acad Sci U S A. 1961 Dec 15;47:1996–2005. doi: 10.1073/pnas.47.12.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. SIDBURY J. B., Jr, NAJJAR V. A. Further studies on the mechanism of phosphoglucomutase; the phosphoenzyme bond. J Biol Chem. 1957 Jul;227(1):517–522. [PubMed] [Google Scholar]
  49. SMITH J. D., MARKHAM R. Chromatographic studies on nucleic acids; the quantitative analysis of ribonucleic acids. Biochem J. 1950 May;46(5):509–513. doi: 10.1042/bj0460509. [DOI] [PMC free article] [PubMed] [Google Scholar]
  50. STERNER J. H., EISENBUD M. Epidemiology of beryllium intoxication. AMA Arch Ind Hyg Occup Med. 1951 Aug;4(2):123–151. [PubMed] [Google Scholar]
  51. SUTHERLAND E. W., POSTERNAK T., CORI C. F. Mechanism of the phosphoglyceric mutase reaction. J Biol Chem. 1949 Nov;181(1):153–159. [PubMed] [Google Scholar]
  52. Schwartz J. H., Crestfield A. M., Lipmann F. THE AMINO ACID SEQUENCE OF A TETRADECAPEPTIDE CONTAINING THE REACTIVE SERINE IN E. COLI ALKALINE PHOSPHATASE. Proc Natl Acad Sci U S A. 1963 May;49(5):722–729. doi: 10.1073/pnas.49.5.722. [DOI] [PMC free article] [PubMed] [Google Scholar]
  53. Stirpe F., Aldridge W. N. Diphosphopyridine nucleotide pyrophosphorylase in the nuclei isolated from poisoned and regenerating rat liver. Biochem J. 1961 Sep;80(3):481–487. doi: 10.1042/bj0800481. [DOI] [PMC free article] [PubMed] [Google Scholar]
  54. TRAYSER K. A., COLOWICK S. P. Properties of crystalline hexokinase from yeast. II. Studies on ATP-enzyme interaction. Arch Biochem Biophys. 1961 Jul;94:161–168. doi: 10.1016/0003-9861(61)90024-8. [DOI] [PubMed] [Google Scholar]
  55. ZWAIG N., MILSTEIN C. ON THE NATURE OF THE PHOSPHOENZYME INTERMEDIATE IN THE PHOSPHOGLYCEROMUTASE REACTION. Biochim Biophys Acta. 1963 Aug 6;73:676–679. doi: 10.1016/0006-3002(63)90347-0. [DOI] [PubMed] [Google Scholar]

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

RESOURCES