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. 1963 Feb;85(2):468–475. doi: 10.1128/jb.85.2.468-475.1963

REGULATION OF EARLY REACTIONS IN THE BIOSYNTHESIS OF TRYPTOPHAN IN NEUROSPORA CRASSA

Gabriel Lester 1
PMCID: PMC278155  PMID: 13929917

Abstract

Lester, Gabriel (Reed College, Portland, Ore.). Regulation of early reactions in the biosynthesis of tryptophan in Neurospora crassa. J. Bacteriol. 85:468–475. 1963.—The regulation of the biosynthesis of tryptophan was examined in Neurospora crassa, strain ylo-tryp-la, which accumulates anthranil compounds. The block in this strain appeared to be in the conversion of 1-(o-carboxyphenylamino)-1-deoxyribulose-5-phosphate to indole-3-glycerol phosphate, since the dephosphorylated form of the former compound, the anthranilic ribonucleoside, and the anthranilic acid were found. Cells cultured on levels of l-tryptophan greater than 0.1 μmole per ml were almost devoid of anthranilate-synthesizing activity, whereas cells cultured on low levels of tryptophan (e.g., 0.025 μmole/ml) could produce anthranilate at a rate of 125 mμmoles per mg (dry wt) per hr. A repressive effect was also caused by d-, 5-methyl-dl-, and 6-methyl-dl-tryptophan, but none of these compounds was as effective a repressor as l-tryptophan. Neither 4-methyl-dl-tryptophan, tryptamine, nor indole-3-acetic acid repressed the formation of anthranilate-synthesizing activity. Preformed activity was strongly inhibited by l-tryptophan, and to a lesser extent by 4-, 5-, and 6-methyl-dl-tryptophan; d-tryptophan, tryptamine, or indole-3-acetic acid did not inhibit preformed anthranilate-synthesizing activity. These results are indicative of the operation of repression and feedback-inhibition mechanisms early in the biosynthetic sequence leading to tryptophan. The relation of these results to those concerned with other aspects of tryptophan biosynthesis is discussed.

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Selected References

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  1. BORENFREUND E., DISCHE Z. A new spray for spotting of sugars on paper chromatograms. Arch Biochem Biophys. 1957 Mar;67(1):239–240. doi: 10.1016/0003-9861(57)90262-x. [DOI] [PubMed] [Google Scholar]
  2. Bonner D. M., Yanofsky C., Partridge C. W. Incomplete Genetic Blocks in Biochemical Mutants of Neurospora. Proc Natl Acad Sci U S A. 1952 Jan;38(1):25–34. doi: 10.1073/pnas.38.1.25. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. COHEN G., JACOB F. Sur la répression de la synthèse des enzymes intervenant dans la formation du tryptophane chez Escherichia coll. C R Hebd Seances Acad Sci. 1959 Jun 15;248(24):3490–3492. [PubMed] [Google Scholar]
  4. DOY C. H., GIBSON F. 1-(o-Carboxyphenylamino)-1-deoxyribulose. A compound formed by mutant strains of Aerobacter aerogenes and Escherichia coli blocked in the biosynthesis of tryptophan. Biochem J. 1959 Aug;72:586–597. doi: 10.1042/bj0720586. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. DOY C. H., RIVERA A., Jr, SRINIVASAN P. R. Evidence for the enzymatic synthesis of N-(5'-phosphoribosyl) anthranilic acid, a new intermediate in tryptophan biosynthesis. Biochem Biophys Res Commun. 1961 Jan 25;4:83–88. doi: 10.1016/0006-291x(61)90261-3. [DOI] [PubMed] [Google Scholar]
  6. GIBSON F. W., DOY C. H., SEGALL S. B. A possible intermediate in the biosynthesis of tryptophan: 1-deoxy-1-N-o-carboxyphenyl-ribulose. Nature. 1958 Feb 22;181(4608):549–550. doi: 10.1038/181549a0. [DOI] [PubMed] [Google Scholar]
  7. GIBSON F., YANOFSKY C. The partial purification and properties of indole-3-glycerol phosphate synthetase from Escherichia coli. Biochim Biophys Acta. 1960 Oct 7;43:489–500. doi: 10.1016/0006-3002(60)90471-6. [DOI] [PubMed] [Google Scholar]
  8. LESTER G. Repression and inhibition of indole-synthesizing activity in Neurospora crassa. J Bacteriol. 1961 Aug;82:215–223. doi: 10.1128/jb.82.2.215-223.1961. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. LESTER G. Some aspects of tryptophan synthetase formation in Neurospora crassa. J Bacteriol. 1961 Jun;81:964–973. doi: 10.1128/jb.81.6.964-973.1961. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. LESTER G., YANOFSKY C. Influence of 3-methylanthranilic and anthranilic acids on the formation of tryptophan synthetase in Escherichia coli. J Bacteriol. 1961 Jan;81:81–90. doi: 10.1128/jb.81.1.81-90.1961. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. MATCHETT W. H., DEMOSS J. A. Factors affecting increased production of tryptophan synthetase by a TD mutant of Neurospora crassa. J Bacteriol. 1962 Jun;83:1294–1300. doi: 10.1128/jb.83.6.1294-1300.1962. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. MONOD J., COHEN-BAZIRE G. L'effet d'inhibition spécifique dans la biosynthèse de la tryptophane-desmase chez Aerobacter aerogenes. C R Hebd Seances Acad Sci. 1953 Feb 2;236(5):530–532. [PubMed] [Google Scholar]
  13. SMITH O. H., YANOFSKY C. 1-(o-Carboxyphenylamino)-1-deoxyribulose 5-phosphate, a new intermediate in the biosynthesis of tryptophan. J Biol Chem. 1960 Jul;235:2051–2057. [PubMed] [Google Scholar]
  14. YANOFSKY C. Indole-3-glycerol phosphate, an intermediate in the biosynthesis of indole. Biochim Biophys Acta. 1956 May;20(2):438–439. doi: 10.1016/0006-3002(56)90332-8. [DOI] [PubMed] [Google Scholar]
  15. YANOFSKY C., RACHMELER M. The exclusion of free indole as an intermediate in the biosynthesis of tryptophan in Neurospora crassa. Biochim Biophys Acta. 1958 Jun;28(3):640–641. doi: 10.1016/0006-3002(58)90533-x. [DOI] [PubMed] [Google Scholar]
  16. YANOFSKY C. The enzymatic conversion of anthranilic acid to indole. J Biol Chem. 1956 Nov;223(1):171–184. [PubMed] [Google Scholar]

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