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Bioscience, Biotechnology, and Biochemistry Volume 71, 2007 - Issue 10
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Original Articles

Characterisitics and Gene Cloning of Phospholipase D of the Psychrophile, Shewanella sp.

Hiroki TSURUTAHeadquarters for Innovative Cooperation and Development, Kobe University
,
Ryuhei HAYASHIDepartment of Biofunctional Chemistry, Graduate School of Science and Technology, Kobe University
,
Hiroyuki OHKAWADepartment of Biofunctional Chemistry, Graduate School of Science and Technology, Kobe University
,
Nobuhide OHKATSUDepartment of Biofunctional Chemistry, Graduate School of Science and Technology, Kobe University
,
Masakazu MORIMOTOFaculty of Agriculture, Kobe University
,
Kaname NISHIMOTODepartment of Biofunctional Chemistry, Graduate School of Science and Technology, Kobe University
,
Sigeyuki SANTOUFaculty of Agriculture, Kobe University
&
Yasuo AIZONOFaculty of Agriculture, Kobe University
 show all
Pages 2534-2542 | Received 26 May 2007, Accepted 28 Jun 2007, Published online: 22 May 2014

  • 1) Exton, J. H., Phospholipase D: enzymology, mechanisms of regulation, and function. Physical. Rev., 77, 303–320 (1997).
  • 2) Exton, J. H., Phospholipase D. Ann. NY Acad. Sci., 905, 61–68 (2000).
  • 3) Wang, X., Multiple forms of phospholipase D in plants: the gene family, catalytic and regulatory properties, and cellular functions. Prog. Lipid Res., 39, 109–149 (2000).
  • 4) Grossman, S., Cobley, J., Hogue, P. K., Kearney, E. B., and Singer, T. P., Relation of phospholipase D activity to the decay of succinate dehydrogenase and of covalently bound flavin in yeast cells undergoing glucose repression. Arch. Biochem. Biophys., 158, 744–753 (1973).
  • 5) Okawa, Y., and Yamaguchi, T., Studies on phospholipases from Streptomyces. II. Purification and properties of Streptomyces hachijoensis phospholipase D. J. Biochem., 78, 363–372 (1975).
  • 6) Imamura, S., and Horiuti, Y., Purification of Streptomyces chromofuscus phospholipase D by hydrophobic affinity chromatography on palmitoyl cellulose. J. Biochem., 85, 79–95 (1979).
  • 7) Zambonelli, C., Casali, M., and Roberts, M. F., Mutagenesis of putative catalytic and regulatory residues of Streptomyces chromofuscus phospholipase D differentially modifies phosphatase and phosphoesterase activities. J. Biol. Chem., 278, 52282–52289 (2003).
  • 8) McNamara, P. J., Cuevas, W. A., and Songer, J. G., Toxic phospholipase D of Corynebacterium pseudotuberculosis, C. ulcerans and Arcanobacterium haemolyticum: cloning and sequence homology. Gene, 156, 113–118 (1995).
  • 9) McNamara, P. J., Bradley, G. A., and Songer, J. G., Targeted mutagenesis of the phospholipase D gene results in decreased virulence of Corynebacterium pseudotuberculosis. Mol. Microbiol., 12, 921–930 (1994).
  • 10) Hochachka, P. W., and Somero, G. N., “Biochemical Adaptations,” Princeton University Press, Princeton, pp. 290–449 (1984).
  • 11) Devail, S., Feller, G., Narinx, E., and Gerday, Ch., Cold adaptation of proteins. J. Biol. Chem., 269, 17448–17453 (1994).
  • 12) Tsuruta, H., Tsuneta, S. T., Ishida, Y., Watanabe, K., Uno, T., and Aizono, Y., Purification and some characteristics of phosphatase of a psychrophile. J. Biochem., 123, 219–225 (1998).
  • 13) Ishida, Y., Tsuruta, H., Tsuneta, S. T., Uno, T., Watanabe, K., and Aizono, Y., Characteristics of psychrophilic alkaline phosphatase. Biosci. Biotechnol. Biochem., 62, 2246–2250 (1998).
  • 14) Feller, G., Narinx, E., Aprigny, J. L., Aittaleb, M., Baise, E., Genicot, S., and Gerday, Ch., Enzymes from psychrophilic organisms. FEMS Microbiol. Rev., 18, 189–202 (1989).
  • 15) DeVendittis, E., Palumbo, G., Parlato, G., and Bochini, V., A fluorescence method for the estimation of the critical micelle concentration of surfactants. Anal. Biochem., 115, 278–286 (1981).
  • 16) Friedman, M., Krull, L. H., and Cavins, J. F., The chromatographic determination of cystine and cysteine residues in proteins as S-beta-(4-pyridylethyl)-L-cysteine. J. Biol. Chem., 245, 3868–3871 (1970).
  • 17) Kenneth, J. S., The instability of S-beta-(4-pyridylethyl)-L-cysteine to performic acid. Anal. Biochem., 56, 450–459 (1973).
  • 18) Tsuruta, H., and Aizono, Y., Cloning of phosphatase I gene from a pychrophile, Shewanella sp., and some properties of the recombinant enzyme. J. Biochem., 127, 143–149 (2000).
  • 19) Sambrook, J., Fritsch, E. F., and Maniatis, T., “Molecular Cloning, a Laboratory Manual” 2nd ed., Cold Spring Harbor Laboratory, Cold Spring Harbor (1989).
  • 20) Triglia, T., Peterson, M. G., and Kemp, D. J., A procedure for in vivo amplification of DNA segments that lie outside the boundaries of known sequences. Nucleic Acid Res., 16, 8186 (1988).
  • 21) Shimbo, K., Iwasaki, Y., Yamane, T., and Ina, K., Purification andproperties of phospholipase D from Streptomyces antibioticus. Biosci. Biotechnol. Biochem., 57, 1946–1948 (1993).
  • 22) Shimbo, K., Yano, H., and Miyamoto, Y., Purification and properties of phospholipase D from Streptomyces lydicus. Agric. Biol. Chem., 54, 1189–1193 (1990).
  • 23) Roberts, M. F., Assays of phospholipases on short-chain phospholipids. Methods Enzymol., 197, 95–112 (1991).
  • 24) Dennis, E. A., Kinetic dependence of phospholipase A2 activity on the detergent Triton X-100. J. Lipid Res., 14, 152–159 (1973).
  • 25) Yang, H., and Roberts, M. F., Cloning, overexpression, and characterization of a bacterial Ca2+-dependent phospholipase D. Protein Sci., 11, 2958–2968 (2002).
  • 26) Hayashi, S., and Wu, H. C., Lipoproteins in bacteria. J. Bioenerg. Biomem., 22, 451–471 (1990).
  • 27) Zambonelli, C., and Robert, M. F., An iron-dependent bacterial phospholipase D reminiscent of purple acid phosphatases. J. Biol. Chem., 278, 13706–13711 (2003).
  • 28) Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680–685 (1970).
  • 29) Morrisey, J. H., Silver stain for proteins in polyacrylamide gel: a modification procedure with enhanced uniform sensitivity. Anal. Biochem., 117, 307–310 (1981).

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