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4,018 results on '"Li, YanHong"'

167. Selective and comparative genome architecture of Asian cultivated rice (Oryza sativa L.) attributed to domestication and modern breeding

Author

Wang, Xueqiang, Wang, Wensheng, Tai, Shuaishuai, Li, Min, Gao, Qiang, Hu, Zhiqiang, Hu, Wushu, Wu, Zhichao, Zhu, Xiaoyang, Xie, Jianyin, Li, Fengmei, Zhang, Zhifang, Zhi, Linran, Zhang, Fan, Ma, Xiaoqian, Yang, Ming, Xu, Jiabao, Li, Yanhong, Zhang, Wenzhuo, Yang, Xiyu, Chen, Ying, Zhao, Yan, Fu, Binying, Zhao, Xiuqin, Li, Jinjie, Wang, Miao, Yue, Zhen, Fang, Xiaodong, Zeng, Wei, Yin, Ye, Zhang, Gengyun, Xu, Jianlong, Zhang, Hongliang, Li, Zichao, and Li, Zhikang

Published
2022
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172. Biochemical characterization of Helicobacter pylori α1-3-fucosyltransferase and its application in the synthesis of fucosylated human milk oligosaccharides.

Author

Bai, Jing, Wu, Zhigang, Sugiarto, Go, Gadi, Madhusudhan Reddy, Yu, Hai, Li, Yanhong, Xiao, Cong, Ngo, Alice, Zhao, Baohua, Chen, Xi, and Guan, Wanyi

Subjects
Milk, Human, Humans, Helicobacter pylori, Metals, Fucosyltransferases, Fucose, Oligosaccharides, Hydrogen-Ion Concentration, Chemistry Techniques, Synthetic, Enzymatic synthesis, Fucosyltransferase, Human milk oligosaccharide, Substrate specificity, Medicinal and Biomolecular Chemistry, Organic Chemistry, Biochemistry and Cell Biology
Abstract

Fucosylated human milk oligosaccharides (HMOs) have important biological functions. Enzymatic synthesis of such compounds requires robust fucosyltransferases. A C-terminal 66-amino acid truncated version of Helicobacter pylori α1-3-fucosyltransferase (Hp3FT) is a good candidate. Hp3FT was biochemically characterized to identify optimal conditions for enzymatic synthesis of fucosides. While N-acetyllactosamine (LacNAc) and lactose were both suitable acceptors, the former is preferred. At a low guanosine 5'-diphospho-β-L-fucose (GDP-Fuc) to acceptor ratio, Hp3FT selectively fucosylated LacNAc. Based on these enzymatic characteristics, diverse fucosylated HMOs, including 3-fucosyllactose (3-FL), lacto-N-fucopentaose (LNFP) III, lacto-N-neofucopentaose (LNnFP) V, lacto-N-neodifucohexaose (LNnDFH) II, difuco- and trifuco-para-lacto-N-neohexaose (DF-paraLNnH and TF-para-LNnH), were synthesized enzymatically by varying the ratio of the donor and acceptor as well as controlling the order of multiple glycosyltransferase-catalyzed reactions.

Published
2019

173. Regioselective One-Pot Multienzyme (OPME) Chemoenzymatic Strategies for Systematic Synthesis of Sialyl Core 2 Glycans

Author

Santra, Abhishek, Li, Yanhong, Ghosh, Tamashree, Li, Riyao, Yu, Hai, and Chen, Xi

Subjects
Biochemistry and Cell Biology, Biological Sciences, Medicinal and Biomolecular Chemistry, Organic Chemistry, Chemical Sciences, biocatalysis, enzymatic synthesis, glycosyltransferase, O-GalNAc glycan, sialyltransferase, Inorganic Chemistry, Chemical Engineering, Industrial biotechnology, Organic chemistry, Physical chemistry
Abstract

O-GalNAc glycans or mucin-type glycans are common protein post-translational modifications in eukaryotes. Core 2 O-GalNAc glycans are branched structures that are broadly distributed in glycoproteins and mucins of all types of cells. To better understand their biological roles, it is important to obtain structurally defined Core 2 O-GalNAc glycans. We present here regioselective one-pot multienzyme (OPME) chemoenzymatic strategies to systematically access a diverse array of sialyl Core 2 glycans. Regioselectivity can be achieved by using OPME systems containing a glycosyltransferase with restricted acceptor specificity or by differentiating the branches using altered glycosylation sequences. This work provides a general regioselective strategy to access diverse Core 2 O-GalNAc glycans which can be extended for the synthesis of other complex branched glycans.

Published
2019

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

Author

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

Subjects
Medicinal and Biomolecular Chemistry, Chemical Sciences, Vaccine Related, 2.2 Factors relating to the physical environment, Aetiology, O-GIcNAcylation, O-GIcNAcase, sugar moiety, GIcNAc derivatives, substrate specificity, GlcNAc derivatives, O-GlcNAcase, O-GlcNAcylation, Chemical sciences
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.

Published
2019

175. Triazole-linked transition state analogs as selective inhibitors against V. cholerae sialidase

Author

Slack, Teri J, Li, Wanqing, Shi, Dashuang, McArthur, John B, Zhao, Gengxiang, Li, Yanhong, Xiao, An, Khedri, Zahra, Yu, Hai, Liu, Yang, and Chen, Xi

Subjects
Medicinal and Biomolecular Chemistry, Organic Chemistry, Chemical Sciences, Emerging Infectious Diseases, Infectious Diseases, Prevention, Foodborne Illness, Vaccine Related, Biodefense, Development of treatments and therapeutic interventions, 5.1 Pharmaceuticals, Infection, Good Health and Well Being, Catalytic Domain, Enzyme Assays, Enzyme Inhibitors, Glycopeptides, Humans, Molecular Docking Simulation, Neuraminidase, Triazoles, Vibrio cholerae, Carbohydrate, Glycopeptide, Sialidase, Sialidase inhibitor, Pharmacology and Pharmaceutical Sciences, Medicinal & Biomolecular Chemistry, Biochemistry and cell biology, Medicinal and biomolecular chemistry, Organic chemistry
Abstract

Sialidases or neuraminidases are enzymes that catalyze the cleavage of terminal sialic acids from oligosaccharides and glycoconjugates. They play important roles in bacterial and viral infection and have been attractive targets for drug development. Structure-based drug design has led to potent inhibitors against neuraminidases of influenza A viruses that have been used successfully as approved therapeutics. However, selective and effective inhibitors against bacterial and human sialidases are still being actively pursued. Guided by crystal structural analysis, several derivatives of 2-deoxy-2,3-didehydro-N-acetylneuraminic acid (Neu5Ac2en or DANA) were designed and synthesized as triazole-linked transition state analogs. Inhibition studies revealed that glycopeptide analog E-(TriazoleNeu5Ac2en)-AKE and compound (TriazoleNeu5Ac2en)-A were selective inhibitors against Vibrio cholerae sialidase, while glycopeptide analog (TriazoleNeu5Ac2en)-AdE selectively inhibited Vibrio cholerae and A. ureafaciens sialidases.

Published
2018

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