ATPase and GTPase activities copurifying with GTP-binding proteins in E. coli

Abu Sayed, Shin Ichi Matsuyama, Koichi Inoue, Janivette Alsina, Feng Cai, Jingqiu Chen, Masayori Inouye

Research output: Contribution to journalArticlepeer-review

1 Scopus citations


Intrinsic GTPase activity of GTP-binding proteins plays the vital role in regulating the downstream activation pathway. We examined the GTP and ATP hydrolyzing (NTPase) abilities of various bacterial and human GTP-binding proteins under different metabolic conditions. Two metabolic components, acetate and 3-phosphoglyceric acid (3-PG), have shown significant stimulatory action on NTPase activity of G-protein preparations. Acetyl phosphate and 2,3-bisphosphoglyceric acid (2,3-BPG) blocked these stimulations. From gel filtration analyses, we have determined two fractions containing metabolite-inducible NTPase activities which are independent of GTP-binding protein enzymatic actions. Therefore, one should be cautious when NTPase activity is examined in a buffer containing acetate often used for NTPase assay.

Original languageEnglish (US)
Pages (from-to)261-263
Number of pages3
JournalJournal of molecular microbiology and biotechnology
Issue number3
StatePublished - Jul 2000

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Microbiology
  • Applied Microbiology and Biotechnology
  • Molecular Biology


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