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.
MeSH Terms
Amino Acids/metabolism
Arginine/metabolism
Chromosome Mapping
Coliphages
D-Amino-Acid Oxidase/analysis
Escherichia coli/enzymology,metabolism
Genetic Linkage
Genotype
Histidine/metabolism
Isoleucine/metabolism
Isomerism
Leucine/metabolism
Lysine/metabolism
Mutation
Phenylalanine/metabolism
Proline/metabolism
Serine/metabolism
Threonine/metabolism
Transduction, Genetic
Tryptophan/metabolism
Tyrosine/metabolism
Valine/metabolism
Chemicals
Amino Acids
Isoleucine
Threonine
Tyrosine
Serine
Phenylalanine
Histidine
Tryptophan
Arginine
Proline
D-Amino-Acid Oxidase
Leucine
Valine
Lysine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Kuhn J
Somerville R L
References (15)
15 references, click to expand
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