| Function | Deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Probably acts by rejecting L-amino acids from its binding site rather than specific recognition of D-amino acids. Catalyzes the hydrolysis of D-tyrosyl-tRNA(Tyr), has no activity on correctly charged L-tyrosyl-tRNA(Tyr). 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. In contrast to DTD1, deacylates L-Ala mischarged on tRNA(Thr)(G4.U69) by alanine-tRNA ligase AARS. Can deacylate L-Ala due to a relaxed specificity for substrate chirality caused by the trans conformation of the Gly-Pro motif in the active site. Also hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly) in vitro, although in vivo EEF1A1/EF-Tu may protect cognate achiral glycyl-tRNA(Gly) from DTD2-mediated deacetylation. |
| Protein Name | D-Aminoacyl-Trna Deacylase 2Animalia-Specific Trna DeacylaseAtdD-Tyrosyl-Trna(Tyr Deacylase 2L-Alanyl-Trna Deacylase |
| Database Links | |
| Cellular Localisation | Cytoplasm |
| Alternative Protein Names | D-Aminoacyl-Trna Deacylase 2 proteinAnimalia-Specific Trna Deacylase proteinAtd proteinD-Tyrosyl-Trna(Tyr Deacylase 2 proteinL-Alanyl-Trna Deacylase proteinDTD2 proteinC14orf126 protein |
Information sourced from Uniprot.org