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.