Production of Glycopeptide Derivatives for Exploring Substrate Specificity of Human OGA Toward Sugar Moiety
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....
| Main Authors: | , , , , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Frontiers Media S.A.
2019-01-01
|
| Series: | Frontiers in Chemistry |
| Subjects: | |
| Online Access: | https://www.frontiersin.org/article/10.3389/fchem.2018.00646/full |
| id |
doaj-91b24f2241524ebbbcb3e03e4ba0b604 |
|---|---|
| record_format |
Article |
| spelling |
doaj-91b24f2241524ebbbcb3e03e4ba0b6042020-11-25T00:50:49ZengFrontiers Media S.A.Frontiers in Chemistry2296-26462019-01-01610.3389/fchem.2018.00646429522Production of Glycopeptide Derivatives for Exploring Substrate Specificity of Human OGA Toward Sugar MoietyShanshan Li0Jiajia Wang1Jiajia Wang2Lanlan Zang3Hailiang Zhu4Jianshuang Guo5Jiabin Zhang6Liuqing Wen7Yi Chen8Yanhong Li9Xi Chen10Peng George Wang11Peng George Wang12Jing Li13Department of Chemistry and Center of Diagnostics & Therapeutics, Georgia State University, Atlanta, GA, United StatesSchool of Basic Medical Sciences, Henan University Joint National Laboratory for Antibody Drug Engineering, Kaifeng, ChinaDepartment of Chemistry and Center of Diagnostics & Therapeutics, Georgia State University, Atlanta, GA, United StatesCentral Laboratory, Linyi People's Hospital, Shandong University, Linyi, ChinaDepartment of Chemistry and Center of Diagnostics & Therapeutics, Georgia State University, Atlanta, GA, United StatesState Key Laboratory of Medicinal Chemical Biology, College of Pharmacy and Tianjin Key Laboratory of Molecular Drug Research, Nankai University, Tianjin, ChinaDepartment of Chemistry and Center of Diagnostics & Therapeutics, Georgia State University, Atlanta, GA, United StatesDepartment of Chemistry and Center of Diagnostics & Therapeutics, Georgia State University, Atlanta, GA, United StatesDepartment of Chemistry, University of California, Davis, Davis, CA, United StatesDepartment of Chemistry, University of California, Davis, Davis, CA, United StatesDepartment of Chemistry, University of California, Davis, Davis, CA, United StatesDepartment of Chemistry and Center of Diagnostics & Therapeutics, Georgia State University, Atlanta, GA, United StatesState Key Laboratory of Medicinal Chemical Biology, College of Pharmacy and Tianjin Key Laboratory of Molecular Drug Research, Nankai University, Tianjin, ChinaState Key Laboratory of Medicinal Chemical Biology, College of Pharmacy and Tianjin Key Laboratory of Molecular Drug Research, Nankai University, Tianjin, ChinaO-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.https://www.frontiersin.org/article/10.3389/fchem.2018.00646/fullO-GlcNAcylationO-GlcNAcasesugar moietyGlcNAc derivativessubstrate specificity |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
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 |
| spellingShingle |
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 Production of Glycopeptide Derivatives for Exploring Substrate Specificity of Human OGA Toward Sugar Moiety Frontiers in Chemistry O-GlcNAcylation O-GlcNAcase sugar moiety GlcNAc derivatives substrate specificity |
| author_facet |
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 |
| author_sort |
Shanshan Li |
| title |
Production of Glycopeptide Derivatives for Exploring Substrate Specificity of Human OGA Toward Sugar Moiety |
| title_short |
Production of Glycopeptide Derivatives for Exploring Substrate Specificity of Human OGA Toward Sugar Moiety |
| title_full |
Production of Glycopeptide Derivatives for Exploring Substrate Specificity of Human OGA Toward Sugar Moiety |
| title_fullStr |
Production of Glycopeptide Derivatives for Exploring Substrate Specificity of Human OGA Toward Sugar Moiety |
| title_full_unstemmed |
Production of Glycopeptide Derivatives for Exploring Substrate Specificity of Human OGA Toward Sugar Moiety |
| title_sort |
production of glycopeptide derivatives for exploring substrate specificity of human oga toward sugar moiety |
| publisher |
Frontiers Media S.A. |
| series |
Frontiers in Chemistry |
| issn |
2296-2646 |
| publishDate |
2019-01-01 |
| description |
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. |
| topic |
O-GlcNAcylation O-GlcNAcase sugar moiety GlcNAc derivatives substrate specificity |
| url |
https://www.frontiersin.org/article/10.3389/fchem.2018.00646/full |
| work_keys_str_mv |
AT shanshanli productionofglycopeptidederivativesforexploringsubstratespecificityofhumanogatowardsugarmoiety AT jiajiawang productionofglycopeptidederivativesforexploringsubstratespecificityofhumanogatowardsugarmoiety AT jiajiawang productionofglycopeptidederivativesforexploringsubstratespecificityofhumanogatowardsugarmoiety AT lanlanzang productionofglycopeptidederivativesforexploringsubstratespecificityofhumanogatowardsugarmoiety AT hailiangzhu productionofglycopeptidederivativesforexploringsubstratespecificityofhumanogatowardsugarmoiety AT jianshuangguo productionofglycopeptidederivativesforexploringsubstratespecificityofhumanogatowardsugarmoiety AT jiabinzhang productionofglycopeptidederivativesforexploringsubstratespecificityofhumanogatowardsugarmoiety AT liuqingwen productionofglycopeptidederivativesforexploringsubstratespecificityofhumanogatowardsugarmoiety AT yichen productionofglycopeptidederivativesforexploringsubstratespecificityofhumanogatowardsugarmoiety AT yanhongli productionofglycopeptidederivativesforexploringsubstratespecificityofhumanogatowardsugarmoiety AT xichen productionofglycopeptidederivativesforexploringsubstratespecificityofhumanogatowardsugarmoiety AT penggeorgewang productionofglycopeptidederivativesforexploringsubstratespecificityofhumanogatowardsugarmoiety AT penggeorgewang productionofglycopeptidederivativesforexploringsubstratespecificityofhumanogatowardsugarmoiety AT jingli productionofglycopeptidederivativesforexploringsubstratespecificityofhumanogatowardsugarmoiety |
| _version_ |
1725246447123693568 |