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 language | English (US) |
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Pages (from-to) | 36067-36072 |
Number of pages | 6 |
Journal | Journal of Biological Chemistry |
Volume | 275 |
Issue number | 46 |
DOIs | |
State | Published - Nov 17 2000 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology