D-aminoacyl-tRNA deacylase 2 (DTD2)

D-aminoacyl-tRNA deacylase 2 (DTD2) is an enzyme that plays a critical proofreading role during protein translation by hydrolyzing and removing D-amino acids that have been mischarged onto tRNA molecules, thereby preventing the incorporation of D-amino acids into proteins and maintaining translational fidelity[1][2][3][4]. In humans and many other eukaryotes, DTD2 counteracts the toxicity associated with D-aminoacyl-tRNA formation, recycles D-aminoacyl-tRNA to D-amino acids and free tRNA, and may also act on certain mischarged glycyl- and alanyl-tRNA species depending on its substrate specificity[4]. DTD2 is catalytically distinct from DTD1 and has adaptations that allow it to deacylate specific aldehyde-modified D-aa-tRNA adducts, which may be relevant in responding to stresses from endogenous or environmental aldehyde exposure[5]. Deficiency or mutation in the gene encoding DTD2 has been genetically linked to the rare disorder Frontometaphyseal dysplasia, though its primary molecular function is conserved and translational quality control is its key biological function[4]. There are currently no known drugs targeting DTD2, nor are there established roles as a clinical biomarker or specific safety concerns reported in a therapeutic context.

Other names

DTD2C14orf126ATDMGC9912Animalia-specific tRNA deacylaseD-tyrosyl-tRNA(Tyr) deacylase 2L-alanyl-tRNA deacylaseD-aminoacyl-tRNA deacylase 2D-tyrosyl-tRNA deacylase 2 (putative)probable D-tyrosyl-tRNA(Tyr) deacylase 2putative D-tyrosyl-tRNA deacylase 2animalia-specific tRNA deacylase