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Original Articles

Cloning of Cold-active Alkaline Phosphatase Gene of a Psychrophile, Shewanella sp., and Expression of the Recombinant Enzyme

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Pages 754-761 | Received 14 Sep 2001, Accepted 05 Dec 2001, Published online: 22 May 2014

  • 1) Low, P. S., Bada, J. L., and Somero, G. N., Temperature adaptation of enzymes: role of the free energy, the enthalpy, and the entropy of activation. Proc. Natl. Acad. Sci. USA, 70, 430-432 (1973).
  • 2) Devail, S., Feller, G., Narinx, E., and Gerday, C., Cold adaptation of proteins. J. Biol. Chem., 269, 17448-17453 (1994).
  • 3) Rentier-Delrue, F., Mande, S. C., Moyens, S., Terpstra, P., Maniford, V., Gorai, K., Lion, M., Hol, W. G. J., and Martial, J. A., Cloning and overexpression of the triosephosphate isomerase genes from psychrophilic and thermophilic bacteria. J. Mol. Biol., 229, 85-93 (1993).
  • 4) Aprigny, J. L., Feller, G., and Gerday, C., Cloning, sequence and structural features of a lipase from psychrophile Psychrobacter immobolis B10, Biochim. Biophys. Acta, 1171, 331-333 (1993).
  • 5) Feller, G. and Gerday, C., Psychrophilic enzymes: molecular basis of cold-adaptation. Cell Mol. Life Sci., 53, 830-841 (1997).
  • 6) Lonhienne, T., Gerday, C., and Feller, G., Psychrophilic enzymes: revising the thermodynamic parameters of activation may explain local flexibility. Biochim. Biophys. Acta, 1543, 1-10 (2000).
  • 7) Ishida, Y., Tsuruta, H., Tsuneta, S. T., Uno, T., Watanabe, K., and Aizono, Y., Characteristics of psychrophilic alkaline phosphatase. Biosci. Biotechnol. Biochem., 62, 2246-2230 (1998).
  • 8) Torriani, A., Influence of inorganic phosphate in the formation of phosphatases by Escherichia coli. Biochim. Biophys. Acta, 38, 460-479 (1960).
  • 9) Gum, J. R., Hicks, J. W., Sack, T. L., and Kim, Y. S., Molecular cloning of complementary DNAs encoding alkaline phosphatase in human colon cancer cells. Cancer Res., 50, 1085-1091 (1990).
  • 10) Hulett, F. M. and Jensen, K., Critical roles of spo0A and spo0H in vegetative alkaline phosphatase production in Bacillus subtilis. J. Bacteriol., 170, 3765-3768 (1988).
  • 11) Plocke, D. J., Levinthal, C., and Vallee, B. L., Alkaline phosphatase of Escherichia coli: a zinc metalloenzyme. Biochemistry, 1, 373-378 (1962).
  • 12) Stec, B., Holtz, K. M., and Kantrowitz, E. R., A revised mechanism for the alkaline phosphatase reaction involving in three metal ions. J. Mol. Biol., 299, 1303-1311 (2000).
  • 13) Kim, E. E. and Wyckoff, H. W., Structure of alkaline phosphatases. Clin. Chim. Acta, 186, 175-187 (1990).
  • 14) Sambrook, J., Fritsch, E. F., and Maniatis, T., Molecular cloning: A laboratory manual, 2nd eds., Cold Spring Habor Laboratory, Cold Spring Harbor (1989).
  • 15) Trigria, T., Peterson, M. G., and Kemp, D. J., A procedure for in vitro amplification of DNA segments that lie outside the boundaries of known sequences. Nucleic Acid Res., 16, 8186 (1988).
  • 16) Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
  • 17) Morrisey, J. H., Silver stain for proteins in polyacrylamide gel: A modification procedure with enhanced uniform sensitivity. Anal. Biochem., 117, 307-310 (1981).
  • 18) Hulett, F. M., Kim, E. E., Bookstein, C., Kapp, N. V., Edwards, C. W., and Wyckoff, H. W., Bacillus subtilis alkaline phosphatase III and IV. J. Biol. Chem., 266, 1077-1084 (1991).
  • 19) Lee, M. H., Nittayajarn, A., Ross, R. P., Rothschild, C. B., Parsonage, D., Claiborne, A., and Rubens, C. E., Characterization of Enterococcus faecalis alkaline phosphatase and use in identifying Streptococcus agalactiae secreted proteins. J. Bacteriol., 181, 5790-5799 (1999).
  • 20) Bradshaw, R. A., Cancedda, F., Ericsson, L. H., Neumann, P. A., Piccoli, S. P., Schlenger, M. J., Shriefer, K., and Walsh, K. A., Amino acid sequence of Escherichia coli alkaline phosphatase. Proc. Natl. Acad. Sci. USA, 783, 3473-3478 (1981).
  • 21) Tsuruta, H. and Aizono, Y., Cloning of phosphatase I gene from a psychrophile, Shewanella sp., and some properties of the recombinant enzyme. J. Biochem., 127, 143-149 (2000).
  • 22) Yasugi, M., Amino, M., Suzuki, T., Oshima, T., and Yamagishi, A., Cold adaptation of the thermophilic enzyme 3-isopropylmalate dehydrogenase. J. Biochem., 129, 433-484 (2001).
  • 23) Aghajari, N., Feller, G., Gerday, C., and Haser, R., Structures of the psychrophilic Alteromonas haloplanctis α-amylase give insights into cold adaptation at molecular level. Structure, 6, 1503-1506 (1998).
  • 24) Pace, C. N., Grimsley, G. R., Thomson, J. A., and Barnett, B. J., Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds. J. Biol. Chem., 263, 11820-11823 (1988).

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