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J. Biochem, 2003, Vol. 133, No. 2 225-230
© 2003 Japanese Biochemical Society

BIOCHEMISTRY

Catalytic Efficiency and Some Structural Properties of Cold-Active Protein-Tyrosine-Phosphatase

Hiroki Tsuruta+, and Yasuo Aizono§,

Laboratory of Biological Chemistry, Department of Biofunctional Chemistry, Faculty of Agriculture, Kobe University, Nada-ku, Kobe, Hyogo 657-8501

A procedure was established for expression and purification of abundant recombinant cold-active protein-tyrosine-phosphatase (RCPTPase), which showed identical enzymatic characteristics to the native enzyme (NCPTPase). The purified RCPTPase showed high catalytic activity at low temperature and maximal activity at 30°C. RCPTPase has a thermodynamic characteristic in that its activation enthalpy was determined to be low, 4.3 kcal/mol, at temperatures below 19.3°C, where the Arrhenius relationship exhibited an inflection point, in comparison with 20.3 kcal/mol above 19.3°C. Also, the thermostability, {Delta}Gwater, of the catalytic site in the RCPTPase molecule was increased with a decrease in temperature. It was considered that cold-active protein-tyrosine-phosphatase could maintain its catalytic site in a stable conformation for eliciting high catalytic activity with low activation enthalpy at low temperature.

+ Research Fellow of the Japan Society for the Promotion of Science (JSPS). Present address: Center for Cooperative Research and Development, Kobe University, Nada-ku, Kobe, Hyogo 657-8501.

§ To whom all correspondence should be addressed. Tel/Fax: +81-78-803-5939, E-mail: aizono{at}kobe-u.ac.jp


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H. Tsuruta, B. Mikami, and Y. Aizono
Crystal Structure of Cold-Active Protein-Tyrosine Phosphatase from a Psychrophile, Shewanella sp.
J. Biochem., January 1, 2005; 137(1): 69 - 77.
[Abstract] [Full Text] [PDF]


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