Properties of Adenosine Triphosphate-Hydrolyzing Enzymes in Membrane Vesicles of Vibrio parahaemolytieus

Yuki Sakai, Yuiciko Sumida, Masaaki Tsuda, Sumio Shinoda, Tomofusa Tsuchiya

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)


The properties and roles of adenosine triphosphate (ATP)-hydrolyzing enzymes in the membrane of Vibrio parahaemolyticus were investigated. At least two (perhaps three) types of ATP-hydrolyzing enzyme was present in everted membrane vesicles. The adenosine triphosphatase (ATPase) activity of one of the enzymes was sensitive to dicyclohexylcarbodiimide and the activity was lost when the membranes were washed with buffer containing ethylenediaminetetraacetic acid. This enzyme seems to be an H+-translocating ATPase. The other ATP-hydrolyzing activity was due to a tightly bound enzyme that could not be removed from the membranes by the washing. This enzyme required higher concentrations of Mg2+ (10 to 20 mM) and Cl- (100 mm) for maximal activity. Zn2+ strongly inhibited the activity. The substrate specificity of this enzyme activity showed that it was a 5’-nucleotidase.

Original languageEnglish
Pages (from-to)3771-3776
Number of pages6
JournalChemical and Pharmaceutical Bulletin
Issue number9
Publication statusPublished - 1987
Externally publishedYes


  • 5’-nucleotidase
  • H-ATPase
  • Na-ATPase
  • membrane-bound ATPase, V. parahaemolyticus

ASJC Scopus subject areas

  • General Chemistry
  • Drug Discovery


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