Publication date: Available online 29 July 2017
Source:Trends in Biochemical Sciences
Author(s): Richard Calendar
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 tRNAAla.
http://ift.tt/2hbrpRw
Σάββατο 29 Ιουλίου 2017
d-Tyrosyl-tRNA Deacylase: A New Function
Εγγραφή σε:
Σχόλια ανάρτησης (Atom)
-
Publication date: September 2017 Source: Free Radical Biology and Medicine, Volume 110 Author(s): Lucía Fernández-del-Río, Anish Nag, Elen...
-
Abstract Noise pollution is a major factor of environmental complaints in many cities, which has significant impacts on human health. As a...
Δεν υπάρχουν σχόλια:
Δημοσίευση σχολίου