Characterization and Identification of The Key Residues Abound The Activity Site Tunnel of Trehalose Synthase from Pseudomonas Stutzeri Qlu3
- DOI
- 10.2991/bep-16.2017.4How to use a DOI?
- Keywords
- characterization; homology modeling; Pseudomonas stutzeri Qlu3; trehalose synthase
- Abstract
The conversion of maltose into trehalose has important applications in the manufacture of food and other products. The enzyme trehalose synthase (TreS) catalyzes the interconversion of maltose and trehalose with glucose as a byproduct. In this study, treS was cloned from Pseudomonas stutzeri Qlu3 genomic DNA. We predicted the structural characteristics of recombinant TreS bound to its substrate by using homology modeling and flexible docking studies of the enzyme-substrate system. These analyses showed six amino acids (Phe115, Phe255, Arg292, Asp403, Asp294, and Glu338) that interact extensively with the substrate during catalysis. In addition, an enclosed active site tunnel was revealed that controls substrate movement during intramolecular isomerization. Disruption of the tunnel by removing two loops led to total loss of isomerization activity. The A309E mutant showed increased isomerase activity and decreased hydrolase activity. In contrast, the Q219R, T308E, and L341Q mutants showed decreased isomerase activity and increased hydrolase activity. These results suggest that the size of the tunnel can influence isomerase activity and hydrolase activity. Therefore, our results exhibited the TreS from Pseudomonas stutzeri Qlu3 have potential industrial use and the analysis in the structure has additional aid for the further molecular modification.
- Copyright
- © 2017, the Authors. Published by Atlantis Press.
- Open Access
- This is an open access article distributed under the CC BY-NC license (http://creativecommons.org/licenses/by-nc/4.0/).
Cite this article
TY - CONF AU - Jing SU AU - Yunxiao ZHANG AU - Zhenzhen LI AU - Piwu LI AU - Lizhen HAO AU - Haijie ZHENG AU - Ruiming WANG PY - 2016/12 DA - 2016/12 TI - Characterization and Identification of The Key Residues Abound The Activity Site Tunnel of Trehalose Synthase from Pseudomonas Stutzeri Qlu3 BT - Proceedings of the 2016 International Conference on Biological Engineering and Pharmacy (BEP 2016) PB - Atlantis Press SP - 16 EP - 21 SN - 2468-5747 UR - https://doi.org/10.2991/bep-16.2017.4 DO - 10.2991/bep-16.2017.4 ID - SU2016/12 ER -