1887

Abstract

synthesized an inducible extracellular collagenase in a peptone medium during the stationary growth phase. These cultures also possessed extracellular alkaline serine protease activity. The alkaline protease activity did not require a specific inducer and it was produced in tryptone or minimal media. The collagenase was not produced in either the tryptone or minimal media. The alkaline protease activity was sensitive to catabolite repression by a number of carbon sources, including glucose, and by amino acids and ammonium ions. Cyclic AMP, dibutyryl cyclic AMP and cyclic GMP did not relieve catabolite repression. Histidine and urocanic acid stimulated the production of alkaline protease activity in tryptone and minimal media. Other compounds associated with the histidine utilization () pathway did not increase alkaline protease activity. Histidine reversed the repression of alkaline protease activity by glucose or (NH)SO in minimal medium. Histidine and the compounds associated with the pathway inhibited collagenase production.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-127-1-193
1981-11-01
2021-10-26
Loading full text...

Full text loading...

/deliver/fulltext/micro/127/1/mic-127-1-193.html?itemId=/content/journal/micro/10.1099/00221287-127-1-193&mimeType=html&fmt=ahah

References

  1. Boethling R. S. 1975; Regulation of extracellular protease secretion in Pseudomonas maltophilia. Journal of Bacteriology 123:954–961
    [Google Scholar]
  2. Florkin M., Stotz E. M. 1973 Comprehensive Biochemistry 13, 3rd edn.. Amsterdam: Elsevier.;
    [Google Scholar]
  3. Glenn A. R. 1976; Production of extracellular proteins by bacteria. Annual Review of Microbiology 30:41–62
    [Google Scholar]
  4. Hagen D. C., Magasanik B. 1973; Isolation of the self regulated repressor protein hut operons of Salmonella typhimurium. Proceedings of the National Academy of Sciences of the United States of America 70:808–812
    [Google Scholar]
  5. Keil-Dlouha V., Misrahi R., Keil B. 1976; The induction of collagenase and a neutral proteinase by their high molecular weight substrates in Achromobacter iophagus. Journal of Molecular Biology 107:293–305
    [Google Scholar]
  6. Lecroisey A., Keil-Dlouha V., Woods D. R., Perrin D., Keil B. 1975; Purification, stability and inhibition of the collagenase from Achromobacter iophagus. FEBS Letters 59:167–172
    [Google Scholar]
  7. Lilley G., Rowley B. I., Bull A. T. 1974; Extracellular β-l,3-glucanase synthesis by continuous flow cultures of a thermophilic streptomycete. Journal of Applied Chemistry and Biotechnology 24:677–686
    [Google Scholar]
  8. Priest F. G. 1977; Extracellular enzyme synthesis in the genus Bacillus. Bacteriological Reviews 41:711–753
    [Google Scholar]
  9. Reid G. C., Robb F. T., Woods D. R. 1978; Regulation of extracellular collagenase production in Achromobacter iophagus. Journal of General Microbiology 109:149–154
    [Google Scholar]
  10. Reid G. C., Woods D. R., Robb F. T. 1980; Peptone induction and rifampicin insensitive collagenase production by Vibrio alginolyticus. Journal of Bacteriology 142:447–454
    [Google Scholar]
  11. Robbertse P. J., Woods D. R., Reay A. M., Robb F. T. 1978; Simple and sensitive procedure for screening collagenolytic bacteria and the isolation of collagenase mutants. Journal of General Microbiology 106:373–376
    [Google Scholar]
  12. Smith G. R., Magasanik B. 1971; The two operons of the histidine utilisation system in Salmonella typhimurium. Journal of Biological Chemistry 246:3330–3341
    [Google Scholar]
  13. Smith G. R., Halpern J. S., Magasanik B. 1971; Genetic and metabolic control of enzymes responsible for histidine degradation in Salmonella typhimurium. Journal of Biological Chemistry 246:3320–3329
    [Google Scholar]
  14. Stinson M. W., Merrick J. M. 1974; Extracellular enzyme secretion by Pseudomonas lemoignei. Journal of Bacteriology 119:152–161
    [Google Scholar]
  15. Tanaka S., Iuchi S. 1971; Induction and repression of an extracellular proteinase in Vibrio parahaemolyticus. Biken Journal 14:81–96
    [Google Scholar]
  16. Welton R. L., Woods D. R. 1973; Halotolerant collagenolytic activity of Achromobacter iophagus. Journal of General Microbiology 75:191–196
    [Google Scholar]
  17. Welton R. L., Woods D. R. 1975; Collagenase production by Achromobacter iophagus. Biochimica et biophysica acta 384:228–234
    [Google Scholar]
  18. Wünsch E., Heidrich H. G. 1963; Zur quantitativen Bestimmung der Kollagenase. Hoppe-Seyler’s Zeitschrift für physiologische Chemie 333:149–151
    [Google Scholar]
  19. Yosmikawa M., Matsuda F., Naka M., Murofishi E., Tsunematus J. 1974; Pleiotropic alterations of activities of several toxins and enzymes in mutant Staphylococcus aureus. Journal of Bacteriology 119:117–122
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-127-1-193
Loading
/content/journal/micro/10.1099/00221287-127-1-193
Loading

Data & Media loading...

Most cited this month 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