Production of glycopeptide derivatives for exploring substrate specificity of human OGA toward sugar moiety

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

Research output: Contribution to journalArticle

1 Scopus citations

Abstract

O-GlcNAcase (OGA) is the only enzyme responsible for removing N-acetyl glucosamine (GlcNAc) attached to serine and threonine residues on proteins. This enzyme plays a key role in O-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 O-GlcNAc modification, as well as a better understanding of the roles of O-GlcNAc in cellular physiology.

Original languageEnglish (US)
Article number646
JournalFrontiers in Chemistry
Volume7
Issue numberJAN
DOIs
StatePublished - Jan 1 2019

Keywords

  • GlcNAc derivatives
  • O-GlcNAcase
  • O-GlcNAcylation
  • Substrate specificity
  • Sugar moiety

ASJC Scopus subject areas

  • Chemistry(all)

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  • Cite this

    Li, S., Wang, J., Zang, L., Zhu, H., Guo, J., Zhang, J., Wen, L., Chen, Y., Li, Y., Chen, X., Wang, P. G., & Li, J. (2019). Production of glycopeptide derivatives for exploring substrate specificity of human OGA toward sugar moiety. Frontiers in Chemistry, 7(JAN), [646]. https://doi.org/10.3389/fchem.2018.00646