Exact emitted record, retrieved 2026-09-10T14:34:29.656476+00:00.
An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. 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
NPI (CS 0) for the composite assertion that this selected protein executes the complete DTD editing mechanism. The family mechanism, D-aminoacyl-tRNA hydrolysis and chiral rejection are real, but its conserved Gly-cisPro element is deleted here. Gly-tRNA(Ala) hydrolysis and an in vivo protection phenotype have not been demonstrated for this truncated product. This does not challenge the full-length human DTD1 activity measured in PMID:17264083 or infer an ATD-like alternative specificity. PMID:17264083(https://pubmed.ncbi.nlm.nih.gov/17264083/); PMID:24302572(https://pubmed.ncbi.nlm.nih.gov/24302572/).
The assessment concerns the selected accession A0A2R8YCT7. Other emitted outputs and evidence context.