Skip to main content
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1971 Oct;68(10):2484–2487. doi: 10.1073/pnas.68.10.2484

Mutant Strains of Escherichia coli K12 That Use D-Amino Acids

Jonathan Kuhn 1, Ronald L Somerville 1
PMCID: PMC389449  PMID: 4400212

Abstract

A series of mutations has been isolated that confer upon amino-acid auxotrophs of Escherichia coli K-12 the ability to grow when fed various D-amino acids. Several distinct systems, mediating cellular use of the D-isomers of leucine, histidine, phenylalanine, tyrosine, tryptophan, isoleucine, and valine, can be mutationally activated. Mutations leading to D-tryptophan use (dadR) all map near purB. They result in high activities of an enzyme that deaminates D-amino acids. Neither the enzymes of the tryptophan biosynthetic pathway nor tryptophanase (EC 4.2.1.e) are involved in D-tryptophan utilization.

Keywords: histidine, phenyalanine, tryptophan, keto acid, deamination, membrane transport

Full text

PDF
2487

Selected References

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

  1. Ames G. F., Lever J. Components of histidine transport: histidine-binding proteins and hisP protein. Proc Natl Acad Sci U S A. 1970 Aug;66(4):1096–1103. doi: 10.1073/pnas.66.4.1096. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Cooper S. Utilization of d-Methionine by Escherichia coli. J Bacteriol. 1966 Aug;92(2):328–332. doi: 10.1128/jb.92.2.328-332.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Guest J. R. Biochemical and genetic studies with nitrate reductase C-gene mutants of Escherichia coli. Mol Gen Genet. 1969;105(4):285–297. doi: 10.1007/BF00277583. [DOI] [PubMed] [Google Scholar]
  4. Igarashi K., Hiraga S., Yura T. A deoxythymidine kinase deficient mutant of Escherichia coli. II. Mapping and transduction studies with phage phi 80. Genetics. 1967 Nov;57(3):643–654. doi: 10.1093/genetics/57.3.643. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Krajewska-Grynkiewicz K., Walczak W., Klopotowski T. Mutants of Salmonella typhimurium able to utilize D-histidine as a source of L-histidine. J Bacteriol. 1971 Jan;105(1):28–37. doi: 10.1128/jb.105.1.28-37.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. 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]
  7. NEWTON W. A., MORINO Y., SNELL E. E. PROPERTIES OF CRYSTALLINE TRYPTOPHANASE. J Biol Chem. 1965 Mar;240:1211–1218. [PubMed] [Google Scholar]
  8. RUDMAN D., MEISTER A. Transamination in Escherichia coli. J Biol Chem. 1953 Feb;200(2):591–604. [PubMed] [Google Scholar]
  9. Signer E. R., Beckwith J. R., Brenner S. Mapping of suppressor loci in Escherichia coli. J Mol Biol. 1965 Nov;14(1):153–166. doi: 10.1016/s0022-2836(65)80237-6. [DOI] [PubMed] [Google Scholar]
  10. Taylor A. L., Trotter C. D. Revised linkage map of Escherichia coli. Bacteriol Rev. 1967 Dec;31(4):332–353. doi: 10.1128/br.31.4.332-353.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. VOGEL H. J., BONNER D. M. Acetylornithinase of Escherichia coli: partial purification and some properties. J Biol Chem. 1956 Jan;218(1):97–106. [PubMed] [Google Scholar]
  12. WEIDEL W., PELZER H. BAGSHAPED MACROMOLECULES--A NEW OUTLOOK ON BACTERIAL CELL WALLS. Adv Enzymol Relat Areas Mol Biol. 1964;26:193–232. doi: 10.1002/9780470122716.ch5. [DOI] [PubMed] [Google Scholar]
  13. WOOD W. A., GUNSALUS I. C. D-Alanine formation; a racemase in Streptococcus faecalis. J Biol Chem. 1951 May;190(1):403–416. [PubMed] [Google Scholar]
  14. 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]
  15. Yanofsky C. Gene structure and protein structure. Harvey Lect. 1967;61:145–168. [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES