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. 1968 Jan;95(1):107–112. doi: 10.1128/jb.95.1.107-112.1968

Enzymes of the Tryptophan Synthetic Pathway in Pseudomonas putida

Toshio Enatsu a,1, Irving P Crawford a
PMCID: PMC251978  PMID: 5636809

Abstract

The first four enzymatic activities of the tryptophan synthetic pathway in Pseudomonas putida were found on separate molecules. Gel filtration and density gradient centrifugation experiments did not disclose any associations or aggregations among them. These findings contrast with the situation found in the enteric bacteria, where the first two activities are found in an aggregate and the third and fourth are catalyzed by a single enzyme. Tryptophan synthetase, the last enzyme of the pathway, consists of two dissociable components. The affinity of these components is less in P. putida than is the case in Escherichia coli.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Anagnostopoulos C., Crawford I. P. Le groupe des gènes régissant la biosynthèse du tryptophane chez Bacillus subtilis. C R Acad Sci Hebd Seances Acad Sci D. 1967 Jul 3;265(1):93–96. [PubMed] [Google Scholar]
  2. Carlton B. C. Transformation mapping of the genes controlling tryptophan biosynthesis in Bacillus subtilis. J Bacteriol. 1967 Sep;94(3):660–665. doi: 10.1128/jb.94.3.660-665.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Crawford I. P., Gunsalus I. C. Inducibility of tryptophan synthetase in Pseudomonas putida. Proc Natl Acad Sci U S A. 1966 Aug;56(2):717–724. doi: 10.1073/pnas.56.2.717. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Crawford I. P., Sikes S., Melhorn D. K. The natural relationships of Aeromonas formicans. Arch Mikrobiol. 1967;59(1):72–81. doi: 10.1007/BF00406318. [DOI] [PubMed] [Google Scholar]
  5. Creighton T. E., Yanofsky C. Indole-3-glycerol phosphate synthetase of Escherichia coli, an enzyme of the tryptophan operon. J Biol Chem. 1966 Oct 25;241(20):4616–4624. [PubMed] [Google Scholar]
  6. FARGIE B., HOLLOWAY B. W. ABSENCE OF CLUSTERING OF FUNCTIONALLY RELATED GENES IN PSEUDOMONAS AERUGINOSA. Genet Res. 1965 Jul;6:284–299. doi: 10.1017/s0016672300004158. [DOI] [PubMed] [Google Scholar]
  7. Ito J., Crawford I. P. Regulation of the enzymes of the tryptophan pathway in Escherichia coli. Genetics. 1965 Dec;52(6):1303–1316. doi: 10.1093/genetics/52.6.1303. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Ito J., Yanofsky C. The nature of the anthranilic acid synthetase complex of Escherichia coli. J Biol Chem. 1966 Sep 10;241(17):4112–4114. [PubMed] [Google Scholar]
  9. LENNOX E. S. Transduction of linked genetic characters of the host by bacteriophage P1. Virology. 1955 Jul;1(2):190–206. doi: 10.1016/0042-6822(55)90016-7. [DOI] [PubMed] [Google Scholar]
  10. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  11. MATSUSHIRO A., SATO K., ITO J., KIDA S., IMAMOTO F. ON THE TRANSCRIPTION OF THE TRYTOPHAN OPERON IN ESCHERICHIA COLI. I. THE TRYPTOPHAN OPERATOR. J Mol Biol. 1965 Jan;11:54–63. doi: 10.1016/s0022-2836(65)80170-x. [DOI] [PubMed] [Google Scholar]
  12. Waltho J. A., Holloway B. W. Suppression of fluorophenylalanine resistance by mutation to streptomycin resistance in Pseudomonas aeruginosa. J Bacteriol. 1966 Jul;92(1):35–42. doi: 10.1128/jb.92.1.35-42.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. YANOFSKY C., LENNOX E. S. Transduction and recombination study of linkage relationships among the genes controlling tryptophan synthesis in Escherichia coli. Virology. 1959 Aug;8:425–447. doi: 10.1016/0042-6822(59)90046-7. [DOI] [PubMed] [Google Scholar]

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