The catalytic efficiency of trehalose-6-phosphate synthase is effected by the N-loop at low temperatures.
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.
Jiang
Ying
Y
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.
Chen
Xi-Ming
XM
Liu
Ya-Jie
YJ
Li
Yuan-Ting
YT
Zhang
Hai-Hong
HH
Dyson
Paul
P
Sheng
Hong-Mei
HM
An
Li-Zhe
LZ
D000595:Amino Acid Sequence; D001173:Arthrobacter / Q000201:enzymology / Q000235:genetics*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D003001:Cloning, Molecular; D003080:Cold Temperature; D005798:Genes, Bacterial; D005964:Glucosyltransferases / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D014532:Uridine Diphosphate Glucose / Q000378:metabolism*
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D005964:Glucosyltransferases; C023180:trehalose-6-phosphate synthase; D014532:Uridine Diphosphate Glucose