C14orf126 (DTD2) (NM_080664) Human Recombinant Protein

Deacylates mischarged D-aminoacyl-tRNAs (By similarity) . Probably acts by rejecting L-amino acids from its binding site rather than specific recognition of D-amino acids (By similarity) . Catalyzes the hydrolysis of D-tyrosyl-tRNA (Tyr), has no activity on correctly charged L-tyrosyl-tRNA (Tyr) (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. In contrast to DTD1, deacylates L-Ala mischarged on tRNA (Thr) (G4.U69) by alanine-tRNA ligase AARS (PubMed:29410408) . 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 (PubMed:29410408) . 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 (By similarity) .[UniProtKB/Swiss-Prot Function]

Stable for 1 year at -20°C or below from date of shipment. For maximum recovery of product, centrifuge the original vial after thawing and opening the cap. For long-term storage, aliquot and store at -20°C or below. Avoid repeated freeze-thaw cycles.