Folia Microbiologica

, Volume 21, Issue 3, pp 178–184 | Cite as

Amidase activity of some bacteria

  • A. Arnaud
  • P. Galzy
  • J. C. Jallageas
Article
Received:

Abstract

The amidase activity of bacteria possessing a high nitrilase activity was found to display the same spectrum although the bacteria may belong to different taxonomic groups,Bacillus, Bacteridium, Micrococcus, Brevibacterium. The spectrum of amidase activity, although very broad, is more restricted than that of nitrilase activity. Internal amides as well as vinyl-bound amides are not hydrolyzed.

Keywords

Amide Mycobacterium Avium Amidase Activity Nitrilase Activity Tertiary Butyl Alcohol 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
This is a preview of subscription content, log in to check access.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Becke F., Fleig H., Pasler P.: Eine allgemeine methode zur Herstellung von Carbonsaureamides aus den entsprechenden Nitrilen.Liebigs Ann. Chem. 749, 198 (1971).CrossRefGoogle Scholar
  2. Betz J. L., Brown P. R., Smyth M. J., Clarke P. H.: Evolution in action.Nature 247, 261 (1974).PubMedCrossRefGoogle Scholar
  3. Clarke P. H.: The aliphatic amidases ofPseudomonas aeruginosa.Adv. Microbial Physiol. 4, 179 (1970).CrossRefGoogle Scholar
  4. Clarke P. H.: Amidases ofPseudomonas species.Biochem. Soc. Trans. 2, 831 (1974).Google Scholar
  5. Draper P.: The aliphatic acylamide amidohydrolase ofMycobacterium smegmatis its inducible nature and relation to aeyl-transfer to hydroxylamine.J. Gen. Microbiol. 46, 111 (1967).PubMedGoogle Scholar
  6. Engelhardt G., Wallnofer P. R., Plapf R.: Purification and properties of an arylacylamidase ofBacillus sphaericus, catalyzing hydrolysis of various phenylamides, herbicides and fungicides.Appl. Microbiol. 26, 709 (1973).PubMedGoogle Scholar
  7. Francis W. C., Thornton J. R., Werner J. C., Hopkins T. R.: The preparation and ammonolysis of α-halogen derivatives of ε-caprolactam. A new synthesis of lysine.J. Amer. Chem. Soc. 80, 6238 (1958).CrossRefGoogle Scholar
  8. Fukumura T.: Splitting of ε-caprolactam and other lactams by bacteria.Plant and Cell Physiol. 7, 105 (1966).Google Scholar
  9. Georges J. C., Dailloux M.: Activités amidasiques quantitatives des mycobactéries atypiques.Ann. Biol. Clin. 31, 217 (1973).Google Scholar
  10. Gorr G., Wagner J.: Amide splitting ability ofTorula utilis.Bot. Ztg. 266, 96 (1933).Google Scholar
  11. Grant D. J. W., Wilson J. V.: Degradation and hydrolysis of amides byCorynebacterium pseudodiphtherilicum NC1B 10803.Microbios. 8, 15 (1973-.PubMedGoogle Scholar
  12. Grant D. J. W.: Degradative versatility ofCorynebacterium pseudodiphtheriticum NC1B 10803 which uses amides as carbon sources.Ant. van Leeuwenhoek 39, 273 (1973).CrossRefGoogle Scholar
  13. Halpern Y. S., Grossowiez N.: Hydrolysis of amides by extracts from Mycobacteria.Biochem. J. 65, 716 (1957-.PubMedGoogle Scholar
  14. Hughes D. E., Williamson D. H.: The deamidation of nieotinamide by bacteria.Biochem. J. 55, 851 (1953).PubMedGoogle Scholar
  15. Hynes M. J., Pateman J. H. J.: Use of amides as nitrogen sources byAspergillus nidulans.J. Gen. Microbiol. 63, 317 (1970).PubMedGoogle Scholar
  16. Hynes M. J.: Induction and repression of amidase enzymes inAspergillus nidulans.J. Bacteriol. 103, 482 (1970).PubMedGoogle Scholar
  17. Hynes M. J.: A cis-dominant regulatory mutation affecting enzyme: Induction in the eukaryoteAspergillus nidulans.Nature 253, 210, 1975.PubMedCrossRefGoogle Scholar
  18. Jakoby W. B., Fredericks J.: Reactions catalyzed by amidases. Acetamidase.J. Biol. Chem. 239, 1978 (1964).PubMedGoogle Scholar
  19. Joshi J. G., Handler P.: Puribcation and properties of nicotinamidase fromTorula cremoris.J. Biol. Chem. 237, 929 (1962).PubMedGoogle Scholar
  20. Kelly M., Kornberg H. L.: Purification and properties of acyltransferases fromPseudomonas aeruginosa Biochem. J. 93, 557 (1964).PubMedGoogle Scholar
  21. Kimura T.: Metabolism of amides in Mycobacteriaceae I. Purification and properties of nicotinamidase fromMycobacterium avium.J. Biochem. 46, 973 (1959a).Google Scholar
  22. Kimura T.: Metabolism of amides in Mycobacteriaceae. II. Enzymatic transfer of nicotinyl group of nicotinamide to hydroxylamine inMycobacterium aviurn.J. Biochem. 46, 1133 (1959b).Google Scholar
  23. Kimura T.: Metabolism of amides in Mycobacteriaceae. III. Amidases and transferases in the extracts from Mycobacteriaceae.J. Biochem. 46, 1271 (1959c).Google Scholar
  24. Kimura T.: Metabolism of amides in Mycobacteriaceae. IV. Formation and hydrolysis of hydroxamate.J. Biochem. 46, 1399 (1959d).Google Scholar
  25. Tacqubt A., Tison F., Ross P., Devulder B.: Activité amidasique des mycobactéries. Technique qualitative nouvelle d’étude en milieu de culture solide.Ann. Inst. Pasteur 112, 378 (1967).Google Scholar
  26. Tosa T., Chibata I.: Utilization of cyclic amides and formation of ω-amino acids by microorganisms.J. Bacteriol. 89, 919 (1965).PubMedGoogle Scholar
  27. Viallier J., Viallier G.: L’activité amidasique des mycobactéries atypiques.Rev. Inst. Pasteur, Lyon 4, 167 (1971-.Google Scholar
  28. Wineman R. J., Eu-Phang T. Hsu, Anagnostopoulos A.: α-haloaenated products of ε-caprolactam and their transformation to DL-lysine.J. Amer. Chem. Soc. 80, 6233 (1958).CrossRefGoogle Scholar

Copyright information

© 1976 1976

Authors and Affiliations

  • A. Arnaud
    • 1
  • P. Galzy
    • 1
  • J. C. Jallageas
    • 2
  1. 1.Department of Genetics, École Nationale Supérieure AgronomiqueUniversité des Sciences et Techniques du LanguedocMontpellier, CedexFrance
  2. 2.Laboratory of Organic ChemistryUniversité des Sciences et Techniques du LanguedocMontpellier, CedexFrance

Personalised recommendations