1887

Abstract

SUMMARY: A strain of was obtained which was able to grow on acetamide or propionamide as sole source of carbon and nitrogen. When grown on these amides, whole bacteria and cell-free extracts rapidly hydrolysed acetamide, glycollamide, acrylamide and propionamide and slowly hydrolysed formamide and butyramide. -Methylformamide, -methylacetamide, -ethylacetamide, -acetylacetamide, -methylpropionamide, -ethylpropionamide, lactamide and methyl carbamate were found to be non-substrate inducers of the amidase when the organism was grown in succinate + ammonium chloride medium. -Methylformamide, -methylacetamide, lactamide and methyl carbamate did not inhibit propionamide hydrolysis by whole bacteria, but under the same conditions glycine amide, iodoacetamide and urea were effective inhibitors of amidase activity. -Phenylacetamide, cyanoacetamide, glycine amide, sarcosine amide, β-hydroxy-propionamide and thioacetamide were neither substrates nor inducers of the amidase in this strain, but inhibited amidase induction by -methylacetamide in succinate + ammonium chloride medium. Formamide also inhibited amidase induction under the same conditions.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-27-2-305
1962-02-01
2024-04-19
Loading full text...

Full text loading...

/deliver/fulltext/micro/27/2/mic-27-2-305.html?itemId=/content/journal/micro/10.1099/00221287-27-2-305&mimeType=html&fmt=ahah

References

  1. Anker H. S. 1948; Synthesis of carbonyl-labelled pyruvic acid. J. biol. Chem 176:1333
    [Google Scholar]
  2. Attenbern R. A., Housewright R. D. 1954; Stereospecific asparaginases in smooth Brucella abortus, strain 19. Arch. Biochem. Biophys 49:130
    [Google Scholar]
  3. Clarke P. H., Meadow P. M. 1959; Evidence for the occurrence of permeases for tricarboxylic acid cycle intermediates in Pseudomonas aeruginosa . J. gen. Microbiol 20:144
    [Google Scholar]
  4. Conway E. J. 1957 Microdiffusion Analysis and Volumetric Error, 4th ed.. p. 98 London: Crosby Lockwood and Son Ltd;
    [Google Scholar]
  5. Den Dooren de Jong L. E. 1926 Bijdrage tot de kennis van het mineralsatiesproces Dissertation Rotterdam;
    [Google Scholar]
  6. Galat A., Elion G. 1943; The interaction of amides with amines: A general method of acylation. J. Amer. chem. Soc 65:1566
    [Google Scholar]
  7. Gorr G., Wagner J. 1932; Über das Amidspaltungsvermögen der Hefen. Biochem. Z 254:1
    [Google Scholar]
  8. Gorr G., Wagner J. 1933; Über das Amidspaltungsvermögen der Torula utilis, eine Untersuchung über die Abhangigkeit pflantzlicher Enzymausbildung von der Stick-stoffernährung. Biochem. Z 266:96
    [Google Scholar]
  9. Gresham T. L., Jansen J. E., Shaver F. W., Bankert R. A., Fiedorec F. T. 1951; β-Propiolactone. XI. Reactions with ammonia and amines. J. Amer. chem. Soc 73:3168
    [Google Scholar]
  10. Halpern Y. S., Grossowicz N. 1957; Hydrolysis of amides by extracts from Mycobacteria. Biochem. J 65:716
    [Google Scholar]
  11. Hellström N. 1932; Das Reaktionsvermögen der Mercaptidogruppe. II. Z. phys. Chem 163:33
    [Google Scholar]
  12. Hughes D. E., Williamson D. H. 1952; Some properties of the glutaminase of Clostridium welchii . Biochem. J 51:45
    [Google Scholar]
  13. Kimura T. 1959; Studies on metabolism of amides in Mycobacteriaeeae. III. Amidases and transferases in extracts from Mycobacteriaceae. J. Biochem., Tokyo 46:1271
    [Google Scholar]
  14. Kogut M., Podoski E. P. 1953; Oxidative pathways in a fluorescent Pseudomonas. Biochem. J 55:800
    [Google Scholar]
  15. Lamaire Y., Brunel A. 1951; Un nouvel enzyme d’adaptation: La cyanamidase. C.R. Acad. Sci., Paris 232:872
    [Google Scholar]
  16. Lowry H. O., Rosebrough N. J., Farr A. L., Randall R. J. 1951; Protein measurements with the Folin Phenol reagent. J. Mol. Chem 193:265
    [Google Scholar]
  17. McIlwain H. 1948; Synthesis and breakdown of glutamine by micro-organisms. J. gen. Microbiol 2:186
    [Google Scholar]
  18. Milner H. W., Lawrence N. S., French C. S. 1950; Colloidal dispersion of chloroplast material. Science 111:633
    [Google Scholar]
  19. Monod J. 1956 In Enzymes: Units of Biological Structure and Function p. 7 Ed. Gaebler O. New York: Academic Press Inc;
    [Google Scholar]
  20. Oka Y. 1954; Studies on hydrolytic enzyme of nicotinamide. J. Biochem. Japan 41:89
    [Google Scholar]
  21. Pershin G. N., Nesvad’ba V. V. 1960; A study of the amidase activity of bacteria and the effect on it of some chemotherapeutic substances. Biochemistry 25:258 (Transl. from Biokhimiya, Acad. Science U.S.S.R.)
    [Google Scholar]
  22. Rickenberg H. V., Cohen G. N., Buttin G., Monod J. 1956; La galactoside-permease A’Escherichia coli . Ann. Inst. Pasteur 91:829
    [Google Scholar]
  23. Shilo M., Stanier R. Y. 1957; The utilisation of tartaric acids by Pseudomonads. J. gen. Microbiol 16:482
    [Google Scholar]
  24. Snell F. P., Snell C. T. 1954 Colorimetric methods of analysis Vol. 4 p. 31 New York: D. Van Nostrand Company, Inc;
    [Google Scholar]
  25. Steiner M. 1959; The utilization of amino and amide nitrogen by Endomycopsis vernalis and other yeasts (with special reference to metabolic reactions at the surface of the cells). Symp. Soc. exp. Biol 13:177
    [Google Scholar]
  26. Titherley A. W. 1901; A new method of preparing diacetamide. J. chem. Soc 79:411
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-27-2-305
Loading
/content/journal/micro/10.1099/00221287-27-2-305
Loading

Data & Media loading...

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