The protein VAT-1 from Torpedo electric organ exhibits an ATPase activity

Michal Linial*, Orit Levius

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

16 Scopus citations


VAT-1 is an abundant protein in Torpedo electric organ which copurifies with a major ATPase activity from synaptic vesicles. VAT-1 was expressed in E. coli and the product was purified and analyzed. The protein binds specifically to an ATP column and displays an ATPase activity as measured by the kinetics of [32P]phosphate release. The activity is dependent on divalent ions, with both Mg2+ and Ca2+ supporting the reaction. The apparent Km for ATP is 18 μM. This ATPase activity is not affected by known inhibitors of the vesicular V- and P-type ATPases such as vanadate and N-ethylmaleimide. We suggest that VAT-1 activity may affect ATP-dependent reactions in Torpedo nerve terminals, such as phosphorylation and dephosphorylation of proteins.

Original languageAmerican English
Pages (from-to)155-157
Number of pages3
JournalNeuroscience Letters
Issue number1-2
StatePublished - 2 Apr 1993

Bibliographical note

Funding Information:
This work was supported in part by US-Israel BSF Grant 209-89 and by the National Institute for Psychobiology in Israel. M.L. is a member of the Otto Lewie Center for Molecular and Cellular Neurobiology in Jerusalem.


  • Adenosine triphosphatase
  • Electric organ
  • Expression vector
  • Nerve terminal
  • Synaptic vesicle protein
  • Torpedo


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