Department of Biotechnology, School of Life Sciences, Central University of Rajasthan Bandar sindri, India.
Front Cell Dev Biol. 2016 Apr 26;4:32. doi: 10.3389/fcell.2016.00032. eCollection 2016.
During protein synthesis, there are several checkpoints in the cell to ensure that the information encoded within genetic material is decoded correctly. Charging of tRNA with its cognate amino acid is one of the important steps in protein synthesis and is carried out by aminoacyl-tRNA synthetase (aaRS) with great accuracy. However, due to presence of D-amino acids in the cell, sometimes aaRS charges tRNA with D-amino acids resulting in the hampering of protein translational process, which is lethal to the cell. Every species has some mechanism in order to prevent the formation of D-amino acid-tRNA complex, for instance DTD (D-Tyr-tRNA deacylase) is an enzyme responsible for the cleavage of ester bond formed between D-amino acid and tRNA leading to error free translation process. In this review, structure, function, and enzymatic mechanism of DTD are discussed. The role of DTD as a drug target is also considered.
在蛋白质合成过程中，细胞中有几个检查点以确保遗传物质中编码的信息被正确解码。tRNA 与其对应的氨基酸的加载是蛋白质合成的重要步骤之一，由氨酰-tRNA 合成酶（aaRS）高度准确地完成。然而，由于细胞中存在 D-氨基酸，有时 aaRS 会将 tRNA 与 D-氨基酸结合，从而阻碍蛋白质翻译过程，这对细胞是致命的。为了防止 D-氨基酸-tRNA 复合物的形成，每种生物都有一些机制，例如 DTD（D-Tyr-tRNA 脱氨酶）是一种负责切割 D-氨基酸和 tRNA 之间形成的酯键的酶，从而导致无错误的翻译过程。本文讨论了 DTD 的结构、功能和酶促机制。还考虑了 DTD 作为药物靶点的作用。
