SUMMARY: Vibrio parahaemolyotcis utilized ATP, ADP or AMP as the sole source of carbon. About three times higher activity of membrane-bound 5'-nucleotidase was observed in cells grown in the presence of these nucleotides than in their absence: and therefore the enzyme seems to be inducible. Since the 5'-nucleotidase activity could be measured with whole cells, the active site of this enzyme appears to be outwardly oriented. Both Mg and CL− were required for activity. Among the divalent cations tested, Mn and Co could replace Mg to some extent, whereas Zn strongly inhibited activity. Among the anions tested, Br−, I− and NO, could replace C1−, but SO and CHCOO− could not. When cells were grown with ATP, Cl− was indispensable and Zn strongly inhibited growth. Therefore, it is concluded that extracellular ATP and other 5'-nucleotides are cleaved by the membrane-bound 5'-nucleotidase outside the cells and that the adenosine produced is then utilized.


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