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 Citation (Scopus)

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

Fingerprint

Glycopeptides
Sugars
Derivatives
Uridine Diphosphate
Glucosamine
Physiology
Substrates
Enzymes
Threonine
Metabolism
Serine
Proteins
hexosaminidase C

Keywords

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

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

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

In: Frontiers in Chemistry, Vol. 7, No. JAN, 646, 01.01.2019.

Research output: Contribution to journalArticle

Li, S, Wang, J, Zang, L, Zhu, H, Guo, J, Zhang, J, Wen, L, Chen, Y, Li, Y, Chen, X, Wang, PG & Li, J 2019, 'Production of glycopeptide derivatives for exploring substrate specificity of human OGA toward sugar moiety', Frontiers in Chemistry, vol. 7, no. JAN, 646. https://doi.org/10.3389/fchem.2018.00646
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. / Production of glycopeptide derivatives for exploring substrate specificity of human OGA toward sugar moiety. In: Frontiers in Chemistry. 2019 ; Vol. 7, No. JAN.
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AU - Zhang, Jiabin

AU - Wen, Liuqing

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AB - 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.

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