Journal
JOURNAL OF MICROBIOLOGY
Volume 48, Issue 6, Pages 803-807Publisher
MICROBIOLOGICAL SOCIETY KOREA
DOI: 10.1007/s12275-010-0377-2
Keywords
T. onnurineus NA1; thermostability; fructose-1,6-bisphosphatase; hyperthermophilic Archaea; fructose-1,6-bisphosphate
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Funding
- Marine and Extreme Genome Research Center of the Ministry of Land, Transportation, and Maritime Affairs, Republic of Korea
- Korea Basic Science Institute [T30130]
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To understand the physiological functions of thermostable fructose-1,6-bisphosphatase (TNA1-Fbp) from Thermococcus onnurineus NA1, its recombinant enzyme was overexpressed in Escherichia coli, purified, and the enzymatic properties were characterized. The enzyme showed maximal activity for fructose-1,6-bisphosphate at 95 degrees C and pH 8.0 with a half-life (t(1/2)) of about 8 h. TNA1-Fbp had broad substrate specificities for fructose-1,6-bisphosphate and its analogues including fructose-l-phosphate, glucose-1-phosphate, and phosphoenolpyruvate. In addition, its enzyme activity was increased five-fold by addition of 1 mM Mg2+, while Li+ did not enhance enzymatic activity. TNA1-Fbp activity was inhibited by ATP, ADP, and phosphoenolpyruvate, but AMP up to 100 mM did not have any effect. TNA1-Fbp is currently defined as a class V fructose-1,6-bisphosphatase (FBPase) because it is very similar to FBPase of Thermococcus kodakaraensis KOD1 based on sequence homology. However, this enzyme shows a different range of substrate specificities. These results suggest that TNA1-Fbp can establish new criterion for class V FBPases.
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