Recombinant DTD1 protein (His tag)

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Recombinant Human D-aminoacyl-tRNA deacylase 1 (DTD) Fragment (1-172) is a high-quality protein product designed for structural and biochemical studies. This 172-amino acid fragment, derived from the full-length DTD1 enzyme, is computationally optimized for stability and solubility, enabling reliable investigation into its roles in tRNA editing and DNA replication processes.

D-aminoacyl-tRNA deacylase 1 (DTD) is a multifunctional enzyme with critical roles in maintaining translational fidelity and supporting DNA replication. As an aminoacyl-tRNA editing enzyme, it deacylates mischarged D-aminoacyl-tRNAs and specifically deacylates mischarged glycyl-tRNA(Ala), thereby protecting cells against glycine mischarging by AlaRS. This activity helps enforce protein L-homochirality by recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, counteracting the toxicity of D-aminoacyl-tRNA formation. Additionally, DTD functions as a possible ATPase involved in DNA replication, where it may facilitate loading of CDC45 onto pre-replication complexes. The enzyme localizes to both the nucleus, where it associates with chromatin at replication origins containing functional DNA-unwinding elements, and the cytoplasm, reflecting its dual functional roles in nucleic acid metabolism and protein synthesis quality control.