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
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- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- NEWTON W. A., MORINO Y., SNELL E. E. PROPERTIES OF CRYSTALLINE TRYPTOPHANASE. J Biol Chem. 1965 Mar;240:1211–1218. [PubMed] [Google Scholar]
- RUDMAN D., MEISTER A. Transamination in Escherichia coli. J Biol Chem. 1953 Feb;200(2):591–604. [PubMed] [Google Scholar]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- Yanofsky C. Gene structure and protein structure. Harvey Lect. 1967;61:145–168. [PubMed] [Google Scholar]