AUTHOR=Li Shanshan , Wang Jiajia , Zang Lanlan , Zhu Hailiang , Guo Jianshuang , Zhang Jiabin , Wen Liuqing , Chen Yi , Li Yanhong , Chen Xi , Wang Peng George , Li Jing 

TITLE=Production of Glycopeptide Derivatives for Exploring Substrate Specificity of Human OGA Toward Sugar Moiety

JOURNAL=Frontiers in Chemistry

VOLUME=6

YEAR=2019

URL=https://www.frontiersin.org/journals/chemistry/articles/10.3389/fchem.2018.00646

DOI=10.3389/fchem.2018.00646

ISSN=2296-2646

ABSTRACT=<p><italic>O</italic>-GlcNAcase (OGA) is the only enzyme responsible for removing <italic>N</italic>-acetyl glucosamine (GlcNAc) attached to serine and threonine residues on proteins. This enzyme plays a key role in <italic>O</italic>-GlcNAc metabolism. However, the structural features of the sugar moiety recognized by human OGA (hOGA) remain unclear. In this study, a set of glycopeptides with modifications on the GlcNAc residue, were prepared in a recombinant full-length human OGT-catalyzed reaction, using chemoenzymatically synthesized UDP-GlcNAc derivatives. The resulting glycopeptides were used to evaluate the substrate specificity of hOGA toward the sugar moiety. This study will provide insights into the exploration of probes for <italic>O</italic>-GlcNAc modification, as well as a better understanding of the roles of O-GlcNAc in cellular physiology.</p>