D-aminoacyl-tRNA deacylase 1 (DTD1)

D-aminoacyl-tRNA deacylase 1 (DTD1) is an essential enzyme responsible for maintaining the fidelity of protein translation by hydrolyzing D-aminoacyl-tRNAs that are mistakenly charged by aminoacyl-tRNA synthetases[2][3][4]. It recognizes and deacylates tRNAs charged with D-amino acids, preventing their incorporation into proteins, which would be lethal or deleterious for cells[2]. DTD1 shows specificity for D-amino acids and also removes glycine mischarged onto tRNA(Ala), further ensuring accurate translation[1][4]. Structurally, it operates as a dimer with catalytic and chiral selection motifs that discriminate D- from L-amino acids[1][3]. Besides its role in translation quality control, DTD1 is implicated in DNA replication initiation via its DNA unwinding element-binding activity and possesses similarity to histidyl-tRNA synthetase[4]. Although targeted therapies or drugs are not yet associated with DTD1, its crucial role in translation fidelity makes it an attractive candidate for drug development against pathogens that rely on error-prone protein synthesis[2].

Other names

D-aminoacyl-tRNA deacylase 1DTD1C20orf88DUEBDUE-BHARS2DTDMGC119131MGC41905bA379J5.3bA555E18.1pqn-68DNA-unwinding element-binding protein BGly-tRNA(Ala) deacylaseHistidyl-tRNA synthase-relatedD-tyrosyl-tRNA deacylase 1 homologD-tyrosyl-tRNA(Tyr) deacylase 1Histidyl-tRNA synthetase 2

*Not applicable* (no known drugs)—the enzyme itself catalyzes hydrolysis of D-aminoacyl-tRNA ester bonds, thus rescuing cells from translation errors