1887

Abstract

SUMMARY: -Norvaline inhibits growth of wild-type A number of mutants resistant to growth inhibition by this analogue were isolated and studied. Cross-feeding experiments and paper chromatography of culture supernatants indicated that the mutants excreted leucine and possibly valine and glutamate. Enzymic analysis indicated that the mutants were derepressed for acetohydroxy-acid synthetase and α-isopropylmalate synthetase; however, no derepression of threonine deaminase, dihydroxyacid dehydrase or transaminase B was observed.

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/content/journal/micro/10.1099/00221287-88-2-289
1975-06-01
2021-10-22
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References

  1. Bauerle R. H., Freundlich M., Störmer F. C., Umbarger H. E. 1964; Control of isoleucine, valine and leucine biosynthesis. II. Endproduct inhibition by valine of acetohydroxyacid synthetase in Salmonella typhimurium. Biochimica et biophysica acta 92:142–149
    [Google Scholar]
  2. Calvo J. M., Freundlich M., Umbarger H. E. 1969; Regulation of branched-chain amino acid biosynthesis in Salmonella typhimurium: isolation of regulatory mutants. Journal of Bacteriology 97:1272–1282
    [Google Scholar]
  3. Calvo T. M., Bartholomew J. C., Stieglitz B. I. 1969; Fluorometric assay of enzymatic reactions involving acetyl coenzyme A in aldol condensations. Analytical Biochemistry 28:164–181
    [Google Scholar]
  4. Chapman L. F. 1972; Regulation of acetohydroxyacid synthetase in Bacillus subtilis. Molecular and General Genetics 117:14–18
    [Google Scholar]
  5. Chapman L. F., Hull C. J. 1974; Strains of Bacillus subtilis synthesizing elevated levels of isoleucine- valine biosynthetic enzymes. Molecular and General Genetics 129:87–95
    [Google Scholar]
  6. Duggan D. E., Wechsler J. A. 1973; An assay for transaminase B activity in Escherichia coli K12. Analytical Biochemistry 51:67–79
    [Google Scholar]
  7. Hatfield G. W., Umbarger H. E. 1971; l-Threonine deaminase, biosynthetic (Bacillus subtilis). In Methods in Enzymology 17B561–566 Tabor H., Tabor C. W. Edited by New York and London:: Academic Press;
    [Google Scholar]
  8. Kiritani K., Wagner R. P. 1970; α,β-Dihydroxyacid dehydrase (Neurospora crassa and spinach). In Methods in Enzymology 17A755–764 Tabor H., Tabor C. W. Edited by New York and London:: Academic Press;
    [Google Scholar]
  9. Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. 1951; Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193:265–275
    [Google Scholar]
  10. Mueller G. C., Bowman G., Herranen A. 1955; Desalting amino acid solutions by ion exchange. Analytical Chemistry 27:1357–1358
    [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. Ward J. B., Zahler S. A. 1973a; Genetic studies of leucine biosynthesis in Bacillus subtilis. Journal of Bacteriology 116:719–726
    [Google Scholar]
  13. Ward J. B., Zahler S. A. 1973b; Regulation of leucine biosynthesis in Bacillus subtilis. Journal of Bacteriology 116:727–735
    [Google Scholar]
  14. Westerfield W. W. 1945; A colorimetric determination of blood acetoin. Journal of Biological Chemistry 161:495–500
    [Google Scholar]
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