Characterization of malate dehydrogenase from deep-sea psychrophilic Vibrio sp. strain no. 5710 and cloning of its gene

  1. Moriya Ohkuma1,*,
  2. Kuniyo Ohtoko1,3,
  3. Nobuhiko Takada2,
  4. Tetsuo Hamamoto1,2,
  5. Ron Usami3,
  6. Toshiaki Kudo1,
  7. Koki Horikoshi2,3

Article first published online: 17 JAN 2006

DOI: 10.1111/j.1574-6968.1996.tb08113.x

Issue

FEMS Microbiology Letters

FEMS Microbiology Letters

Volume 137, Issue 2-3, pages 247–252, April 1996

Additional Information

How to Cite

Ohkuma, M., Ohtoko, K., Takada, N., Hamamoto, T., Usami, R., Kudo, T. and Horikoshi, K. (1996), Characterization of malate dehydrogenase from deep-sea psychrophilic Vibrio sp. strain no. 5710 and cloning of its gene. FEMS Microbiology Letters, 137: 247–252. doi: 10.1111/j.1574-6968.1996.tb08113.x

Author Information

  1. 1

    Microbiology Laboratory; The Institute of Physical and Chemical Research (RIKEN), Wako, Saitama 351-01, Japan

  2. 2

    Deepstar Program, Japan Marine Science and Technology Center, Wako, Saitama 351-01, Japan

  3. 3

    Department of Applied Chemistry, Toyo University, Kawagoe, Saitama 350, Japan

* *Corresponding author. Tel.: +81 (48) 462 1111 ext. 5724; Fax: +81 (48)462 4672; E-mail: mohkuma@postman.riken.go.jp

Publication History

  1. Issue published online: 17 JAN 2006
  2. Article first published online: 17 JAN 2006
  3. (Received 6 February 1996, Revised 6 February 1996)

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Keywords:

  • Psychrophile;
  • Vibrio;
  • Deep-sea;
  • Malate dehydrogenase

Abstract A metabolic key enzyme malate dehydrogenase (MDH) was purified from a deep-sea psychrophilic bacterium, Vibrio sp. strain no. 5710. The enzyme displayed an optimal activity shifted toward lower temperature and a pronounced heat lability. A gene encoding this enzyme was isolated and cloned. Recombinant Escherichia coli cells harboring the isolated clone expressed MDH activity with temperature stability identical to that of the parental psychrophile. Nucleotide sequencing of the gene revealed that its primary sequence was similar to that of a mesophile E. coli MDH (78% amino acid identity), for which the three-dimensional structure is known. The enzyme is thus suitable for the analysis of molecular adaptations to low temperatures.

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