Mutations at lysine 525 of inducible nitric-oxide synthase affect its Ca2+-independent activity

S. J. Lee, K. Beckingham, J. T. Stull

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Abstract

Calmodulin binding to inducible nitric-oxide synthase may play an important role in its Ca2+-independent activity. Studies of inducible nitric-oxide synthase chimeras containing the calmodulin binding sequence of neuronal or endothelial nitric-oxide synthases show that the calmodulin binding sequence of inducible nitric-oxide synthase is necessary but not sufficient for the Ca2+-independent activity. The mutations at lysine 525 located at the C terminus of the calmodulin binding sequence of inducible nitric-oxide synthase were examined for the effects on the Ca2+-independent activity with chimeras containing the oxygenase or reductase domains of inducible or neuronal nitric-oxide synthases. Results show that the Ca2+-independent binding of calmodulin is not solely responsible for maximal Ca2+-independent activity of inducible nitric-oxide synthase. Lysine 525 of inducible nitric-oxide synthase may also play an important role in coordinating the maximal Ca2+-independent activity.

Original languageEnglish (US)
Pages (from-to)36067-36072
Number of pages6
JournalJournal of Biological Chemistry
Volume275
Issue number46
DOIs
StatePublished - Nov 17 2000

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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