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.
Article PDF
Similar content being viewed by others
Avoid common mistakes on your manuscript.
References
Becke F., Fleig H., Pasler P.: Eine allgemeine methode zur Herstellung von Carbonsaureamides aus den entsprechenden Nitrilen.Liebigs Ann. Chem. 749, 198 (1971).
Betz J. L., Brown P. R., Smyth M. J., Clarke P. H.: Evolution in action.Nature 247, 261 (1974).
Clarke P. H.: The aliphatic amidases ofPseudomonas aeruginosa.Adv. Microbial Physiol. 4, 179 (1970).
Clarke P. H.: Amidases ofPseudomonas species.Biochem. Soc. Trans. 2, 831 (1974).
Draper P.: The aliphatic acylamide amidohydrolase ofMycobacterium smegmatis its inducible nature and relation to aeyl-transfer to hydroxylamine.J. Gen. Microbiol. 46, 111 (1967).
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).
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).
Fukumura T.: Splitting of ε-caprolactam and other lactams by bacteria.Plant and Cell Physiol. 7, 105 (1966).
Georges J. C., Dailloux M.: Activités amidasiques quantitatives des mycobactéries atypiques.Ann. Biol. Clin. 31, 217 (1973).
Gorr G., Wagner J.: Amide splitting ability ofTorula utilis.Bot. Ztg. 266, 96 (1933).
Grant D. J. W., Wilson J. V.: Degradation and hydrolysis of amides byCorynebacterium pseudodiphtherilicum NC1B 10803.Microbios. 8, 15 (1973-.
Grant D. J. W.: Degradative versatility ofCorynebacterium pseudodiphtheriticum NC1B 10803 which uses amides as carbon sources.Ant. van Leeuwenhoek 39, 273 (1973).
Halpern Y. S., Grossowiez N.: Hydrolysis of amides by extracts from Mycobacteria.Biochem. J. 65, 716 (1957-.
Hughes D. E., Williamson D. H.: The deamidation of nieotinamide by bacteria.Biochem. J. 55, 851 (1953).
Hynes M. J., Pateman J. H. J.: Use of amides as nitrogen sources byAspergillus nidulans.J. Gen. Microbiol. 63, 317 (1970).
Hynes M. J.: Induction and repression of amidase enzymes inAspergillus nidulans.J. Bacteriol. 103, 482 (1970).
Hynes M. J.: A cis-dominant regulatory mutation affecting enzyme: Induction in the eukaryoteAspergillus nidulans.Nature 253, 210, 1975.
Jakoby W. B., Fredericks J.: Reactions catalyzed by amidases. Acetamidase.J. Biol. Chem. 239, 1978 (1964).
Joshi J. G., Handler P.: Puribcation and properties of nicotinamidase fromTorula cremoris.J. Biol. Chem. 237, 929 (1962).
Kelly M., Kornberg H. L.: Purification and properties of acyltransferases fromPseudomonas aeruginosa Biochem. J. 93, 557 (1964).
Kimura T.: Metabolism of amides in Mycobacteriaceae I. Purification and properties of nicotinamidase fromMycobacterium avium.J. Biochem. 46, 973 (1959a).
Kimura T.: Metabolism of amides in Mycobacteriaceae. II. Enzymatic transfer of nicotinyl group of nicotinamide to hydroxylamine inMycobacterium aviurn.J. Biochem. 46, 1133 (1959b).
Kimura T.: Metabolism of amides in Mycobacteriaceae. III. Amidases and transferases in the extracts from Mycobacteriaceae.J. Biochem. 46, 1271 (1959c).
Kimura T.: Metabolism of amides in Mycobacteriaceae. IV. Formation and hydrolysis of hydroxamate.J. Biochem. 46, 1399 (1959d).
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).
Tosa T., Chibata I.: Utilization of cyclic amides and formation of ω-amino acids by microorganisms.J. Bacteriol. 89, 919 (1965).
Viallier J., Viallier G.: L’activité amidasique des mycobactéries atypiques.Rev. Inst. Pasteur, Lyon 4, 167 (1971-.
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).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Arnaud, A., Galzy, P. & Jallageas, J.C. Amidase activity of some bacteria. Folia Microbiol 21, 178–184 (1976). https://doi.org/10.1007/BF02883153
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF02883153