An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs (Probable). Hydrolyzes D-tyrosyl-tRNA(Tyr) into D-tyrosine and free tRNA(Tyr) (PubMed:10766779). May also deacylate mischarged D-leucyl-tRNA(Leu) (PubMed:10918062). Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS (By similarity). Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site (By similarity). 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 (By similarity). 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) 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. 10-fold decrease in D-tyrosyl-tRNA(Tyr) deacylase activity, growth becomes more sensitive to D-tyrosine and is inhibited at 0.1 mM D-Tyr (PubMed:10766779, PubMed:10918062). Growth is also inhibited in the presence of 0.3 mM D-leucine; wild-type cells grow well in up to 0.3 mM D-Tyr and 10 mM D-Leu (PubMed:10918062). No growth differences observed in the presence of the other D-amino acids (PubMed:10918062). Present with 4610 molecules/cell in log phase SD medium. Belongs to the DTD family.