| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10588346 | Bioorganic & Medicinal Chemistry Letters | 2012 | 5 Pages |
Abstract
Nucleotide sugars are essential glycosyl donors for Leloir-type glycosyltransferases. The UDP-N-acetylgalactosamine pyrophosphorylase (UDP-GalNAc PP; AGX1) from Homo sapiens catalyzes the synthesis of UDP-N-acetylgalactosamine from N-acetylgalactosamine 1-phosphate and UTP. In this Letter, we systematically studied nucleotide substrate specificity of AGX1 during its uridyltransfer reaction, and described the capability of AGX1 to catalyze dUTP and dTTP to their corresponding nucleotide sugars for the first time. Furthermore, using such a eukaryotic enzyme, we synthesized dUDP-GalNAc and dTDP-GalNAc in multiple mg scale in vitro efficiently and rapidly.
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Authors
Mengyang Xue, Wanyi Guan, Yang Zou, Junqiang Fang, Xian-wei Liu, Peng George Wang, Fengshan Wang,