An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs, has no observable editing activity on tRNAs charged with cognate L-amino acid (PubMed:10383414, PubMed:4292198, PubMed:10918062, PubMed:24302572, PubMed:27224426). Edits mischarged glycyl-tRNA(Ala) more efficiently than AlaRS (PubMed:28362257). Acts via tRNA-based rather than protein-based catalysis (PubMed:24302572, PubMed:27224426, PubMed:28362257). Rejects correctly charged L-amino acid-tRNAs from its binding site rather than specifically recognizing incorrectly charged D-amino acid-tRNAs (PubMed:27224426). Hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly); GTP-bound EF-Tu (tested with T.thermophilus EF-Tu AC Q5SHN6) protects charged glycyl-tRNA(Gly) from hydrolysis, while increasing Dtd levels or inactivating EF-Tu decreases protection (PubMed:27224426). Hydrolyzes mischarged glycyl-tRNA(Ala) (but not seryl-tRNA(Ala)) even in the presence of EF-Tu, edits about 4-fold better than the editing domain of AlaRS (PubMed:28362257). Has greater activity on glycyl-tRNA(Ala) than glycyl-tRNA(Gly) due in part to its recognition of the conserved tRNA(Ala) G3.U70 wobble base pair (PubMed:28362257). Binds D-amino acids but not L-amino acids (PubMed:16902403). Overexpression of E.coli or P.falciparum Dtd is toxic in E.coli, toxicity can be rescued by supplementation with Gly (PubMed:27224426). By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality (PubMed:15292242). Hydrolyzes D-tyrosyl-tRNA(Tyr) (PubMed:4292198, PubMed:10383414, PubMed:24302572, PubMed:27224426). Hydrolyzes D-phenylalanyl-tRNA(Phe) (PubMed:4292198, PubMed:24302572). Hydrolyzes D-aspartyl-tRNA(Asp) (PubMed:10918062). Hydrolyzes D-tryptophanyl-tRNA(Trp) (PubMed:10918062). Hydrolyzes glycyl-tRNA(Gly) (PubMed:27224426). Hydrolyzes glycyl-tRNA(Ala) (PubMed:28362257). glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala) a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+) D-tyrosyl-tRNA(Tyr) + H2O = D-tyrosine + tRNA(Tyr) kcat/KM is 6 uM(-1)sec(-1) for D-tyrosyl-tRNA(Tyr) (PubMed:10383414). kcat/KM is 2.8 uM(-1)sec(-1) for D-tryptophanyl-tRNA(Trp) (PubMed:10918062). kcat/KM is 12 uM(-1)sec(-1) for D-aspartyl-tRNA(Asp) (PubMed:10918062). kcat/KM is 10 uM (-1)sec(-1) for glycyl-tRNA(Gly) (PubMed:27224426). Homodimer. A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids (PubMed:24302572, PubMed:27224426). No phenotype in rich or minimal medium, decreased growth rate in the presence of excess D-tyrosine (PubMed:10383414). A double dtd-dadA deletion mutant has a more pronounced growth defect in the presence of D-Tyr (in strain K12 / EC989) (PubMed:10383414). In a dtd deletion mutant about 40% of tRNA(Tyr) is D-tyrosyl-tRNA(Tyr); overexpressing the gene for tRNA(Tyr) suppresses the toxicity of D-Tyr by increasing the levels of L-tyrosyl-tRNA(Tyr) available for translation (PubMed:15292242). Decreased growth in the presence of D-Asp, D-Ser, D-Gln and D-Trp (PubMed:10918062). Poor growth on 20 mg/ml D-Tyr, no growth on 500 mg/ml D-Tyr or 20 mg/ml D-Trp (PubMed:25441601). Overexpression of genes for tRNA(Asp) or tRNA(Trp) suppresses the toxicity of their respective D-amino acids (PubMed:15292242). No effect seen when grown in 3 or 10 mM Gly; in a mutant that no longer edits mischarged glycyl-tRNA(Ala) or seryl-tRNA(Ala) (triple mutation in alaS) Gly becomes toxic, but excess Ala restores growth (PubMed:28362257). Belongs to the DTD family. Initially the conserved reside Thr-80 was thought to be a nucleophile; mutagenesis in this organism and P.falciparum indicates it is not.