Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3202, USA.
Trends Biochem Sci. 2017 Sep;42(9):684-686. doi: 10.1016/j.tibs.2017.06.012. Epub 2017 Jul 29.
d-Aminoacyl-tRNA deacylase (DTD) hydrolyzes d-amino acids mistakenly attached to tRNAs and, thus, has been implicated in perpetuating protein homochirality. Fifty years after the discovery of DTD, it has now been shown that its function extends beyond 'chiral proofreading' because it also eliminates glycine that has been erroneously coupled to tRNA.
d-氨酰-tRNA 脱氨酶 (DTD) 水解错误连接到 tRNA 的 d-氨基酸,因此,它被认为与蛋白质的手性持久有关。在 DTD 发现 50 年后,现在已经表明其功能不仅仅是“手性校对”,因为它还消除了错误连接到 tRNA 的甘氨酸。