1887

Abstract

SUMMARY: Isoleucine hydroxamate-resistant mutants of have been isolated. Biochemical examination of the isoleucine-valine biosynthetic enzymes allowed the mutants to be grouped into three classes: I, mutants with increased enzyme levels; II, mutants with feedback inhibition-insensitive -threonine dehydratase; III, mutants without any alteration in either feedback inhibition or enzyme levels. Of these mutants, class II accumulated isoleucine outside the cells in medium containing -threonine. Strain IHr3i3, whose -threonine dehydratase was about 500-fold less sensitive to feedback inhibition when compared with wild-type enzyme, accumulated up to 7 mg. of isoleucine per ml. of medium.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-69-3-291
1971-12-01
2024-04-16
Loading full text...

Full text loading...

/deliver/fulltext/micro/69/3/mic-69-3-291.html?itemId=/content/journal/micro/10.1099/00221287-69-3-291&mimeType=html&fmt=ahah

References

  1. Adelberg E. A., Mandel M., Chen G. C. C. 1965; Optimal conditions for mutagenesis by N-methyl- N′-nitro-N-nitrosoguanidine in Escherichia coli K12. Biochemical and Biophysical Research Communications 18:788–795
    [Google Scholar]
  2. Davis B. D., Mingioli E. S. 1950; Mutants of Escherichia coli requiring methionine or vitamin B12. Journal of Bacteriology 60:17–28
    [Google Scholar]
  3. Kisumi M. 1962; Studies on the isoleucine fermentation. I. Screening of organisms and investigation of cultural conditions. Journal of Biochemistry 52:390–399
    [Google Scholar]
  4. Kisumi M., Kato J., Komatsubara S., Chibata I. 1971a; Increase in isoleucine accumulation by α-aminobutyric acid-resistant mutants of serratia marcescens. Applied Microbiology 21:569–574
    [Google Scholar]
  5. Kisumi M., Komatsubara S., Chibata I. 1971b; Valine accumulation by α-aminobutyric acid-resistant mutants of Serratia marcescens. Journal of Bacteriology 106:493–499
    [Google Scholar]
  6. Kisumi M., Komatsubara S., Chibata I. 1971c; Multivalent repression and genetic derepression of isoleucine-valine biosynthetic enzymes in Serratia marcescens. Journal of Bacteriology 107:824–827
    [Google Scholar]
  7. Kisumi M., Komatsubara S., Sugiura M., Chibata I. 1971d; Isoleucine hydroxamate, an isoleucine antagonist. Journal of Bacteriology 107:741–746
    [Google Scholar]
  8. Ramakrishnan T., Adelberg E. A. 1964; Regulatory mechanisms in the biosynthesis of isoleucine and valine. I. Genetic derepression of enzyme formation. Journal of Bacteriology 87:566–573
    [Google Scholar]
  9. Ramakrishnan T., Adelberg E. A. 1965; Regulatory mechanisms in the biosynthesis of isoleucine and valine. II. Identification of two operator genes. Journal of Bacteriology 89:654–660
    [Google Scholar]
  10. Roth J. R., Silbert D. F., Fink G. R., Voll M. J., Anton D., Hartman P. E., Ames B. N. 1965; Transfer RNA and the control of the histidine operon. Cold Spring Harbor Symposia on Quantitative Biology 31:383–392
    [Google Scholar]
  11. Szentirmai A., Szentirmai M., Umbarger H. E. 1968; Isoleucine and valine metabolism of Escherichia coli. XV. Biochemical properties of mutants resistant to thiaisoleucine. Journal of Bacteriology 95:1672–1679
    [Google Scholar]
  12. Tosa T., Pizer L. I. 1971; Biochemical bases for the antimetabolite action of l-serine hydroxamate. Journal of Bacteriology 106:972–982
    [Google Scholar]
  13. Umbarger H. E. 1969a; Regulation of amino acid metabolism. Annual Review of Biochemistry 38:323–370
    [Google Scholar]
  14. Umbarger H. E. 1969b; Regulation of the biosynthesis of the branched-chain amino acids. Current Topics in Cellular Regulation 1:57–76
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-69-3-291
Loading
/content/journal/micro/10.1099/00221287-69-3-291
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