Vanadate-sensitive ATPase from chromaffin granule membranes formed a phosphoenzyme intermediate and was activated by phosphatidylserine

Yoshinori Moriyama, Nathan Nelson, Masatomo Maeda, Masamitsu Futai

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

Vanadate-sensitive ATPase (115 kDa molecular weight) in adrenal chromaffin granules is an intrinsic membrane enzyme with its catalytic site located at the outer surface of the granules. Upon incubation with [γ-32P]ATP, the purified ATPase formed an alkaline-labile phosphoenzyme intermediate, which was inhibited by vanadate but not by Na+ or K+. Ratio of ATPase or phosphatase activity and formation of phosphoenzyme intermediate was constant during purification after the first glycerol density gradient centrifugation. Phosphatidyl-serine specifically activated the enzyme about three-fold by increasing the Vmax value without changing the Km for ATP. Other phospholipids, including phosphatidyl-glycerol, phosphatidylcholine, phosphatidylinositol, and phosphatidylethanolamine, as well as lysophospholipids and detergents, had no effect. These results indicated that the vanadate-sensitive ATPase belongs to the P-type ATPases, which differ from known cation-translocating P-type ATPases.

Original languageEnglish
Pages (from-to)252-256
Number of pages5
JournalArchives of Biochemistry and Biophysics
Volume286
Issue number1
DOIs
Publication statusPublished - Apr 1991

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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