Article
Lys842 in neuronal nitric-oxide synthase enables the autoinhibitory insert to antagonize calmodulin binding, increase FMN shielding, and suppress interflavin electron transfer.
The Journal of biological chemistry - 29 Jan 2010
Guan Zhi-Wen, Haque Mohammad Mahfuzul, Wei Chin-Chuan, Garcin Elsa D, Getzoff Elizabeth D, Stuehr Dennis J
Abstract excerpt
Neuronal nitric-oxide synthase (nNOS) contains a unique autoinhibitory insert (AI) in its FMN subdomain that represses nNOS reductase activities and controls the calcium sensitivity of calmodulin (CaM) binding to nNOS. How the AI does this is unclear. A conserved charged residue (Lys(842)) lies within a putative CaM binding helix in the middle of the AI. We investigated its role by substituting residues that...
Topics
- Amino Acid Sequence
- Animals
- Calmodulin
- Cattle
- Cytochrome Reductases
- Flavins
- Humans
- Kinetics
- Lysine
- Molecular Sequence Data
- Mutation
- NADPH Oxidases
- Neurons
- Nitric Oxide Synthase