DTD2 Human

DTD2 is a recombinant protein that is often expressed in Escherichia coli for research purposes. The recombinant form typically includes a His-tag at the N-terminus to facilitate purification. The protein consists of 168 amino acids and has a molecular weight of approximately 21 kDa .

The primary function of DTD2 is to hydrolyze D-tyrosyl-tRNA(Tyr) into D-tyrosine and free tRNA(Tyr). This activity is essential as it serves as a defense mechanism against the harmful effects of D-tyrosine. The presence of D-tyrosine in proteins can lead to dysfunctional proteins and potentially harmful cellular consequences .

DTD2 belongs to the DTD family of enzymes, which are known for their role in maintaining the accuracy of protein synthesis. By hydrolyzing misacylated tRNAs, DTD2 ensures that only correctly acylated tRNAs are used in protein synthesis, thereby maintaining the integrity of the proteome .

Recombinant DTD2 is widely used in biochemical and structural studies to understand its function and mechanism. It is also used in studies aimed at developing inhibitors that could modulate its activity for therapeutic purposes. The recombinant protein is typically purified using conventional chromatography techniques and is available in various formulations for research use .

Recombinant DTD2 should be stored at 4°C for short-term use and at -20°C for long-term storage. It is important to avoid repeated freeze-thaw cycles to maintain its stability and activity. The protein is usually supplied in a buffer containing Tris-HCl, NaCl, glycerol, and DTT to ensure its stability .