Skip to content
1887

Microbiology Society logo Microbiology

Volume 76, Issue 1

Asparaginase and Glutaminase Activities of Micro-organisms Free

Abstract

Summary: -Asparaginase and -glutaminase activities were detected in many microorganisms and the distribution of these activities was found to be related to the classification of micro-organisms.

Among 464 bacteria, the activities occurred in many Gram-negative bacteria and in a few Gram-positive bacteria. Most members of the family Enterobacteri-aceae possessed -asparaginase. -Asparaginase and -glutaminase occurred together in a large proportion of pseudomonads. Among Gram-positive bacteria many strains of showed strong -asparaginase activity. Amidase activities were also observed in several strains in other families.

-Asparaginase activity was not detected in culture filtrates of 261 strains of species of the genera and , but -asparaginase and -glutaminase were detected when these organisms were sonicated.

The amidase activities in culture filtrates of 4158 fungal strains were tested. All the strains of Fusarium species formed -asparaginase. Organisms of the genera and , which are regarded as the perfect stage of the genus , also formed -asparaginase. Several Penicillium species formed -asparaginase. Two organisms of the family Moniliaceae formed -glutaminase together with -asparaginase, and a fewascomycetous fungi formed -asparaginase or -glutaminase.

Among 1326 yeasts, -asparaginase or -glutaminase occurred frequently in certain serological groups of yeasts: VI (Hansenula) group, Cryptococcus group and Rhodotorula group. Many strains of Sporobolomyces species also showed -asparaginase activity. Several strains of Cryptococcus and Rhodotorula group possessed -glutaminase and -asparaginase. -Glutaminase alone was formed in many strains of and , both of which are related to Basidiomycetes.

  • Received:
  • Revised:
  • Published Online:
© Society for General Microbiology, 1973
Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-76-1-85
1973-05-01
2025-01-21
Loading full text...

Full text loading...

/deliver/fulltext/micro/76/1/mic-76-1-85.html?itemId=/content/journal/micro/10.1099/00221287-76-1-85&mimeType=html&fmt=ahah

References

  1. Altenbern R. A., Housewright R. D. 1954; Stereospecific asparaginases in smooth Brucella abortus, strain 19. Archives of Biochemistry and Biophysics 49:130–137
     [Google Scholar]
  2. Arima K., Sakamoto T., Araki C., Tamura G. 1972; Production of extracellular l-asparaginases by microorganisms. Agricultural and Biological Chemistry 36:356–361
     [Google Scholar]
  3. Bach D. 1928; Les conditions d’action de l’asparaginase de VAspergillus niger . Comptes rendus 187:955–956
     [Google Scholar]
  4. Boyd J. W., Phillips A. W. 1971; Inhibition of lymphoma 6C3HED by l-asparaginase from Serratia marcescens . Journal of National Cancer Institute 46:1271–1276
     [Google Scholar]
  5. Broome J. D. 1961; Evidence that the l-asparaginase activity of guinea pig serum is responsible for its antilymphoma effects. Nature, London 191:1114–1115
     [Google Scholar]
  6. Broome J. D. 1963a; Evidence that the l-asparaginase of guinea pig serum is responsible for its antilymphoma effects. I. Properties of the l-asparaginase of guinea pig serum in relation to those of the antilymphoma substance. Journal of Experimental Medicine 118:99–120
     [Google Scholar]
  7. Broome J. D. 1963b; Evidence that the L-asparaginase of guinea pig serum is responsible for its antilymphoma effects. II. Lymphoma 6C3HED cells cultured in a medium devoid of l-asparagine lose their susceptibility to the effects of guinea pig serum in vivo . Journal of Experimental Medicine 118:121–148
     [Google Scholar]
  8. Campbell H. A., Mashburn L. T. 1969; l-Asparaginase EC-2 from Escherichia coli. Some substrate specificity characteristics. Biochemistry 8:3768–3775
     [Google Scholar]
  9. De-Angeli L. C., Pocciari F., Russi S., Tonolo A., Zurita V. E., Ciaranfi E., Perin A. 1970; Effect of L-asparaginase from Aspergillus terreus on ascites sarcoma in the rat. Nature, London 225:549–550
     [Google Scholar]
  10. Dox A. W. 1909; The intracellular enzymes of lower fungi, especially those of Penicillium camemberti . Journal of Biological Chemistry 6:461–467
     [Google Scholar]
  11. El-Asmar F. A., Greenberg D. M. 1966; Studies on the mechanism of inhibition of tumor growth by the enzyme glutaminase. Cancer Research 26:116–122
     [Google Scholar]
  12. Eremenco V. V., Evseev L. P., Nikolaev A. Ya. 1968; Asparaginase of Bacterium cadaveris . Mikro-biologiya 37:207–212
     [Google Scholar]
  13. Fell J. W., Statzell A. C., Hunter I. L., Phaff H. J. 1969; Leucosporidium gen.n., the heterobasidiomycetous stage of several yeasts of the genus Candida . Antonie van Leeuwenhoek 35:433–462
     [Google Scholar]
  14. Gorr G., Wagner J. 1932; Über das Amidspaltungsvermögen der Hefen. Biochemische Zeitschrift 254:1–4
     [Google Scholar]
  15. Grassmann W., Mayr O. 1933; Zur Kenntnis der Hefeasparaginase. Zeitschrift fur physiologische Chemie 214:185–210
     [Google Scholar]
  16. Greenberg D. M., Blumenthal G., Ramadan M-E. A. 1964; Effect of administration of the enzyme glutaminase on the growth of cancer cells. Cancer Research 24:957–963
     [Google Scholar]
  17. De Groot N., Lichtenstein N. 1960; The action of Pseudomonas fluorescens extracts on asparagine and asparagine derivatives. Biochimica et biophysica acta 40:99–110
     [Google Scholar]
  18. Haskel C. M., Canellos G. P., Leventhal B. G., Carbone P. P., Block J. B., Serpick A. A., Selawry O. S. 1969; l-Asparaginase. Therapeutic and toxic effects in patients with neoplastic disease. New England Journal of Medicine 281:1028–1034
     [Google Scholar]
  19. Hill J. M., Roberts J., Loeb E., Khan A., MacLellan A., Hill R. W. 1967; l-Asparaginase therapy for leukemia and other malignant neoplasms. Remission in human leukemia. Journal of American Medical Association 202:882–888
     [Google Scholar]
  20. Imada A., Igarasi S. 1967; Ribosyl and deoxyribosyl transfer by bacterial enzyme systems. Journal of Bacteriology 94:1551–1559
     [Google Scholar]
  21. Kidd J. G. 1953; Regression of transplanted lymphomas induced in vivo by means of normal guinea pig serum. I. Course of transplanted cancers of various kinds in mice and rats given guinea pig serum, horse serum, or rabbit serum. Journal of Experimental Medicine 98:565–581
     [Google Scholar]
  22. Law A. S., Wriston J. C. Jun 1971; Purification and properties of Bacillus coagulans l-asparaginase. Archives of Biochemistry and Biophysics 147:744–752
     [Google Scholar]
  23. Manning G. B., Campbell L. L. Jun 1957; The asparagine deamidase of Bacillus coagulans and Bacillus stearothermophilus . Canadian Journal of Microbiology 3:1001–1009
     [Google Scholar]
  24. Mashburn L. T., Wriston J. C. Jun 1964; Tumor inhibitory effect of l-asparaginase from Escherichia coli . Archives of Biochemistry and Biophysics 105:450–452
     [Google Scholar]
  25. Nikolaev A. Ya., Evseev L. P., Tyul’panova E. S., Abdumalikov A. Kh. 1969; Isoenzymes of asparaginase in Pseudomonas sp. Biokhimiya 34:352–355
     [Google Scholar]
  26. Oettgen H. F., Old L. J., Boyse E. A., Campbell H. A., Phillips F. S., Clarkson B. D., Tallal L., Leeper R. D., Schwartz M. K., Kim J. H. 1967; Inhibition of leukemias in man by L-asparaginase. Cancer Research 27:2619–2631
     [Google Scholar]
  27. Old L. J., Boyse E. A., Campbell H. A., Daria G. M. 1963; Leukemia-inhibiting properties and l-asparaginase activity of sera from certain South American rodents. Nature, London 198:801
     [Google Scholar]
  28. Peterson R. E., Ciegler A. 1969a; l-Asparaginase production by Erwinia aroideae . Applied Microbiology 18:64–67
     [Google Scholar]
  29. Peterson R. E., Ciegler A. 1969b; l-Asparaginase production by various bacteria. Applied Microbiology 17:929–930
     [Google Scholar]
  30. Ramadan M. E-D. A., El-Asmar F., Greenberg D. M. 1964; Purification and properties of glutaminase and asparaginase from a pseudomonad. I. Purification and physical chemical properties. Archives of Biochemistry and Biophysics 108:143–149
     [Google Scholar]
  31. Reddy V. V. S., Jayaram H. N., Sirsi M., Ramakrishnan T. 1969; Inhibitory activity of L-asparaginase from Mycobacterium tuberculosis on Yoshida ascites sarcoma in rats. Archives of Biochemistry and Biophysics 132:262–267
     [Google Scholar]
  32. Roberts J., Burson G., Hill J. M. 1968; New procedures for purification of l-asparaginase with high yield from Escherichia coli . Journal of Bacteriology 95:2117–2123
     [Google Scholar]
  33. Roberts J., Holcenberg J. S., Dolowy W. C. 1970; Antineoplastic activity of highly purified bacterial glutaminases. Nature, London 227:1136–1137
     [Google Scholar]
  34. Roberts J., Holcenberg J. S., Dolowy W. C. 1972; Isolation, crystallization, and properties of Achromobacteraceae glutaminase-asparaginase with antitumour activity. Journal of Biological Chemistry 247:84–90
     [Google Scholar]
  35. Rowley B., Wriston J. C. Jun 1967; Partial purification and antilymphoma activity of Serratia marcescens l-asparaginase. Biochemical and Biophysical Research Communications 28:160–165
     [Google Scholar]
  36. Sakamoto T., Araki C., Tamura G., Arima K., Yamamoto T., Matsuzawa A., Hori S. 1970; On the extracellular asparaginases of microorganisms. Proceedings of the Society of Agricultural Chemistry p 159
     [Google Scholar]
  37. Scheetz R. W., Whelan H. A., Wriston J. C. Jun 1971; Purification and properties of an L-asparaginase from Fusarium tricinctum . Archives of Biochemistry and Biophysics 142:184–189
     [Google Scholar]
  38. Schmalfuss K., Mothes K. 1930; Über die fermentative Desamidierung durch Aspergillus niger . Biochemische Zeitschrift 221:134–153
     [Google Scholar]
  39. Schwartz J. H., Reeves J. Y., Broome J. D. 1966; Two l-asparaginases from E. coli and their action against tumors. Proceedings of the National Academy of Sciences of the United States of America 56:1516–1519
     [Google Scholar]
  40. Tchan Y. T., Asano J., Kobayashi M. 1971; Study of l-asparaginase production by Rhodopseudomonas capsulatus (1) A model for the induction of l-asparaginase. Journal of Fermentation Technology 49:733–739
     [Google Scholar]
  41. Tosa T., Sano R., Yamamoto K., Nakamura M., Ando K., Chibata I. 1971; l-Asparaginase from Proteus vulgaris . Applied Microbiology 22:387–392
     [Google Scholar]
  42. Tsuchiya T. 1967; Serological classification of yeasts. In Kobo-gaku (Yeast studies) pp 100–135 Edited by Hashitani Y. Tokyo: Iwanami Shoten;
     [Google Scholar]
  43. Tsuji Y. 1957; Amidase. Naika-Hokan 4:222
     [Google Scholar]
  44. Wade H. E., Elsworth R., Herbert D., Keppie J., Sargeant K. 1968; A new l-asparaginase with antitumour activity. Lancet ii:776–777
     [Google Scholar]
  45. Wade H. E., Robinson H. K., Phillips B. W. 1971; Asparaginase and glutaminase activities of bacteria. Journal of General Microbiology 69:299–312
     [Google Scholar]
  46. Yamada K. 1970; Antileukemia activity of l-asparaginase. Igaku no Ayumi 72:112–113
     [Google Scholar]
  47. Yellin T. O., Wriston J. C. Jun 1966a; Purification and properties of guinea pig serum asparaginase. Biochemistry 5:1605–1612
     [Google Scholar]
  48. Yellin T. O., Wriston J. C. Jun 1966b; Antagonism of purified asparaginase from guinea pig serum toward lymphoma. Science, New York 151:998–999
     [Google Scholar]
/content/journal/micro/10.1099/00221287-76-1-85
Loading
Asparaginase and Glutaminase Activities of Micro-organisms
Microbiology 76, 85 (1973); https://doi.org/10.1099/00221287-76-1-85
/content/journal/micro/10.1099/00221287-76-1-85
/content/journal/micro/10.1099/00221287-76-1-85
Loading

Data & Media loading...

Most cited Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error