Deacylates mischarged D-aminoacyl-tRNAs (By similarity).
Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS (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).
Store at -20°C for 1 year. Avoid freeze/thaw cycle.
图片
Recombinant Human DTD2 Protein (rp189411) - SDS-PAGE 3 μg/lane of Recombinant Human DTD2 Protein was resolved with SDS-PAGE under reducing (R) and non-reducing (N) conditions and visualized by Coomassie® Blue staining, showing a band at 17.4 kDa under reducing conditions and 17.0 kDa under non-reducing conditions.
ZJ25F0218481
危险品化学品经营许可证（带存储）