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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Abbreviations
- OtsA:
-
Trehalose-6-phosphate synthase
- UDP-Glc:
-
UDP-glucose
- Glc-6-P:
-
Glucose-6-phosphate
- Tre-6-P:
-
Trehalose-6-phosphate
- OtsB:
-
Trehalose-phosphate phosphatase
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Acknowledgments
This work was supported by the National Outstanding Youth Foundation of China (30625008), the International Cooperation Project (2009DFA61060), The Agricultural Science and Technology Achievements Transformation Funding Project (0910XCNA066), The National Natural Science Foundation (30700082), and the National University Special Fund for Basic Research (lzujbky-2009-160). The DNA sequence of the otsA A gene described in this study has been deposited in the GenBank database under accession number DQ471452.
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Communicated by Erko Stackebrandt.
Ying Jiang and Xi-Ming Chen contributed equally to this work.
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Jiang, Y., Chen, XM., Liu, YJ. et al. The catalytic efficiency of trehalose-6-phosphate synthase is effected by the N-loop at low temperatures. Arch Microbiol 192, 937–943 (2010). https://doi.org/10.1007/s00203-010-0625-1
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DOI: https://doi.org/10.1007/s00203-010-0625-1