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J. Biol. Chem., Vol. 275, Issue 46, 36067-36072, November 17, 2000

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Mutations at Lysine 525 of Inducible Nitric-oxide Synthase Affect Its Ca²⁺-independent Activity^*

Shiow-Ju Lee^§, Kathy Beckingham^¶, and James T. Stull

From the  Department of Physiology, University of Texas Southwestern Medical Center, Dallas, Texas 75390-9040 and ^¶ Department of Biochemistry and Cell Biology, Rice University, Houston, Texas 77005-1892

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.

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