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

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

doi:10.3389/fchem.2018.00646

Frontiers in Chemistry (Jan 2019)

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

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

Affiliations

Shanshan Li: Department of Chemistry and Center of Diagnostics & Therapeutics, Georgia State University, Atlanta, GA, United States
Jiajia Wang: School of Basic Medical Sciences, Henan University Joint National Laboratory for Antibody Drug Engineering, Kaifeng, China
Jiajia Wang: Department of Chemistry and Center of Diagnostics & Therapeutics, Georgia State University, Atlanta, GA, United States
Lanlan Zang: Central Laboratory, Linyi People's Hospital, Shandong University, Linyi, China
Hailiang Zhu: Department of Chemistry and Center of Diagnostics & Therapeutics, Georgia State University, Atlanta, GA, United States
Jianshuang Guo: State Key Laboratory of Medicinal Chemical Biology, College of Pharmacy and Tianjin Key Laboratory of Molecular Drug Research, Nankai University, Tianjin, China
Jiabin Zhang: Department of Chemistry and Center of Diagnostics & Therapeutics, Georgia State University, Atlanta, GA, United States
Liuqing Wen: Department of Chemistry and Center of Diagnostics & Therapeutics, Georgia State University, Atlanta, GA, United States
Yi Chen: Department of Chemistry, University of California, Davis, Davis, CA, United States
Yanhong Li: Department of Chemistry, University of California, Davis, Davis, CA, United States
Xi Chen: Department of Chemistry, University of California, Davis, Davis, CA, United States
Peng George Wang: Department of Chemistry and Center of Diagnostics & Therapeutics, Georgia State University, Atlanta, GA, United States
Peng George Wang: State Key Laboratory of Medicinal Chemical Biology, College of Pharmacy and Tianjin Key Laboratory of Molecular Drug Research, Nankai University, Tianjin, China
Jing Li: State Key Laboratory of Medicinal Chemical Biology, College of Pharmacy and Tianjin Key Laboratory of Molecular Drug Research, Nankai University, Tianjin, China

DOI: https://doi.org/10.3389/fchem.2018.00646
Journal volume & issue: Vol. 6

Abstract

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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.

Published in Frontiers in Chemistry

ISSN: 2296-2646 (Online)
Publisher: Frontiers Media S.A.
Country of publisher: Switzerland
LCC subjects: Science: Chemistry
Website: http://journal.frontiersin.org/journal/chemistry

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