The catalytic efficiency of trehalose-6-phosphate synthase is effected by the N-loop at low temperatures |
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| Authors: | Ying Jiang Xi-Ming Chen Ya-Jie Liu Yuan-Ting Li Hai-Hong Zhang Paul Dyson Hong-Mei Sheng Li-Zhe An |
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| Institution: | (1) Key Laboratory of Arid and Grassland Agroecology of the Ministry of Education, School of Life Sciences, Lanzhou University, 730000 Lanzhou, People’s Republic of China;(2) Institute of Life Science, School of Medicine, Swansea University, Singleton Park, Swansea, SA2 8PP, UK;(3) State Key Laboratory of Arid Agroecology, Lanzhou University, 730000 Lanzhou, People’s Republic of China; |
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| Abstract: | The enzyme OtsA (trehalose-6-phosphate synthase) is ubiquitous in both prokaryotic and eukaryotic organisms, where it plays
a critical role in stress resistance and glucose metabolism. Here, we cloned the otsA gene from Arthrobacter sp. Cjts, and expressed and then purified the recombinant proteins. Enzyme activity analysis indicated that the high catalytic
efficiency of OtsA from Arthrobacter sp. Cjts resulted from the high affinity of the enzyme for uridine 5′-diphosphoglucose (UDP-Glc) at low temperatures. We
also confirmed that the N-loop sequence of OtsA has a large effect on its affinity for UDP-Glc. Sequence analysis indicated
that the flexibility of the N-loop may be directly related to the catalytic efficiency of OtsA at low temperatures. |
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