Asp141 and the hydrogen-bond chain Asp141–Asn109–Asp33 are respectively essential for GT80 sialyltransferase activity and structural stability

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• 作者：Xiaoyan Chen ; Yuanming Wang ; Zhenping Ma ; Na Li ; Weiqing Han…
• 关键词：sialyltransferase ; hydrogen ; bond chain ; general base ; stability ; activity
• 刊名：Biochemistry (Moscow)
• 出版年：2015
• 出版时间：August 2015
• 年：2015
• 卷：80
• 期：8
• 页码：1073-1079
• 全文大小：1,232 KB
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• 作者单位：Xiaoyan Chen (1)
  Yuanming Wang (2)
  Zhenping Ma (2)
  Na Li (2)
  Weiqing Han (2)
  Qi Zhang (2)
  Yumei Cai (1)
  Jiansong Cheng (2)
  
  1. College of Animal Science and Veterinary Medicine, Shandong Agricultural University, Shandong, 271018, China
  2. State Key Laboratory of Medicinal Chemical Biology and College of Pharmacy, Nankai University, Tianjin, 300071, China
  
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Biochemistry
  Bioorganic Chemistry
  Microbiology
  Biomedicine
  Russian Library of Science
  
• 出版者：MAIK Nauka/Interperiodica distributed exclusively by Springer Science+Business Media LLC.
• ISSN：1608-3040

文摘

Sialyltransferases are key enzymes involved in the biosynthesis of biologically and pathologically important sialic acid-containing molecules in nature. In this study, the activity of a putative sialyltransferase (Pm0160) harboring an inherent mutation D141Y in the conserved DDG motif, which has been identified in GT52 and GT80 families, was restored by reverse mutation. More interestingly, a hydrogen-bond chain was found to form between three conserved residues (Asp141, Asn109, and Asp33) of GT80 sialyltransferases based on recently determined crystal structures. Our mutagenesis experiments demonstrated that the hydrogen-bond chain connecting the general base Asp141 with Nβ4, Nβ1, and Nα1 plays an essential role in maintaining protein structural stability other than keeping the general base Asp141 in a productive orientation for sialic acid transfer.