Skip to main content
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1969 Apr;98(1):109–115. doi: 10.1128/jb.98.1.109-115.1969

Enzymes of Tryptophan Biosynthesis in Serratia marcescens

M A Hutchinson 1, W L Belser 1
PMCID: PMC249911  PMID: 4891805

Abstract

In Serratia marcescens, the tryptophan biosynthetic enzymes were formed coordinately. A number of tryptophan auxotrophs showed single biochemical lesions; several mutants showed pleiotropic effects. Sucrose density gradient centrifugation revealed an unique pattern of migration of the tryptophan biosynthetic enzymes. The repression response of the Serratia enzymes to exogenous tryptophan was fivefold more sensitive than that found in Escherichia coli. When this information is contrasted with the available information on the other Enterobacteriaceae, one is compelled to conclude that S. marcescens enjoys a rather marked evolutionary divergence from the other enteric organisms.

Full text

PDF
109

Selected References

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

  1. AMES B. N., GARRY B., HERZENBERG L. A. The genetic control of the enzymes of histidine biosynthesis in Salmonella typhimurium. J Gen Microbiol. 1960 Apr;22:369–378. doi: 10.1099/00221287-22-2-369. [DOI] [PubMed] [Google Scholar]
  2. Ames B. N., Garry B. COORDINATE REPRESSION OF THE SYNTHESIS OF FOUR HISTIDINE BIOSYNTHETIC ENZYMES BY HISTIDINE. Proc Natl Acad Sci U S A. 1959 Oct;45(10):1453–1461. doi: 10.1073/pnas.45.10.1453. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bauerle R. H., Margolin P. A multifunctional enzyme complex in the tryptophan pathway of Salmonella typhimurium: comparison of polarity and pseudopolarity mutations. Cold Spring Harb Symp Quant Biol. 1966;31:203–214. doi: 10.1101/sqb.1966.031.01.028. [DOI] [PubMed] [Google Scholar]
  4. Belser W. L. BIOASSAY OF ORGANIC MICRONUTRIENTS IN THE SEA. Proc Natl Acad Sci U S A. 1959 Oct;45(10):1533–1542. doi: 10.1073/pnas.45.10.1533. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. 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]
  6. 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]
  7. Creighton T. E., Yanofsky C. Association of the alpha and beta-2 subunits of the tryptophan synthetase of Escherichia coli. J Biol Chem. 1966 Feb 25;241(4):980–990. [PubMed] [Google Scholar]
  8. 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]
  9. DeMoss J. A., Jackson R. W., Chalmers J. H., Jr Genetic control of the structure and activity of an enzyme aggregate in the tryptophan pathway of Neurospora crassa. Genetics. 1967 Jul;56(3):413–424. doi: 10.1093/genetics/56.3.413. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Enatsu T., Crawford I. P. Enzymes of the tryptophan synthetic pathway in Pseudomonas putida. J Bacteriol. 1968 Jan;95(1):107–112. doi: 10.1128/jb.95.1.107-112.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Gibson F. Chorismic acid: purification and some chemical and physical studies. Biochem J. 1964 Feb;90(2):256–261. doi: 10.1042/bj0900256. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Hütter R., DeMoss J. A. Organization of the tryptophan pathway: a phylogenetic study of the fungi. J Bacteriol. 1967 Dec;94(6):1896–1907. doi: 10.1128/jb.94.6.1896-1907.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. 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]
  14. 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]
  15. LABRUM E. L., BUNTING M. I. Spontaneous and induced color-variation of the HY strain of Serratia marcescens. J Bacteriol. 1953 Apr;65(4):394–404. doi: 10.1128/jb.65.4.394-404.1953. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. 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]
  17. Wegman J., Crawford I. P. Tryptophan synthetic pathway and its regulation in Chromobacterium violaceum. J Bacteriol. 1968 Jun;95(6):2325–2335. doi: 10.1128/jb.95.6.2325-2335.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Whitt D. D., Carlton B. C. Characterization of mutants with single and multiple defects in the tryptophan biosynthetic pathway in Bacillus subtilis. J Bacteriol. 1968 Oct;96(4):1273–1280. doi: 10.1128/jb.96.4.1273-1280.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. YANOFSKY C. The tryptophan synthetase system. Bacteriol Rev. 1960 Jun;24(2):221–245. doi: 10.1128/br.24.2.221-245.1960. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES