Homology modeling and function of trehalose synthase from Pseudomonas putida P06

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• 作者：Jing Su (1)
  Tengfei Wang (1)
  Chunling Ma (1)
  Zhongkui Li (1)
  Zhenzhen Li (1)
  Ruiming Wang (1)
  
• 关键词：Catalytic mechanism ; Enzyme–substrate interactions ; Homology modeling ; Pseudomonas putida P06 ; Trehalose ; Trehalose synthase
• 刊名：Biotechnology Letters
• 出版年：2014
• 出版时间：May 2014
• 年：2014
• 卷：36
• 期：5
• 页码：1009-1013
• 全文大小：703 KB
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• 作者单位：Jing Su (1)
  Tengfei Wang (1)
  Chunling Ma (1)
  Zhongkui Li (1)
  Zhenzhen Li (1)
  Ruiming Wang (1)
  
  1. School of Food & Bioengineering, Qilu University of Technology, Jinan, 250300, China
  
• ISSN：1573-6776

文摘

Trehalose is a non-reducing disaccharide that has wide applications in the food industry and pharmaceutical manufacturing. Trehalose synthase (TreS) from Pseudomonas putida P06 catalyzes the reversible interconversion of maltose and trehalose and may have applications in the food industry. However, the catalytic mechanism of TreS is not well understood. Here, we investigated the structural characteristics of this enzyme by homology modeling. The highly conserved Asp294 residue was identified to be critical for catalytic activity. In addition, flexible docking studies of the enzyme–substrate system were performed to predict the interactions between TreS and its substrate, maltose. Amino acids that interact extensively with the substrate and stabilize the substrate in an orientation suitable for enzyme catalysis were identified. The importance of these residues for catalytic activity was confirmed by the biochemical characterization of the relevant mutants generated by site-directed mutagenesis.