Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase

• DOI: 10.1038/351714a0
• Publication Date: 2003-06-12T23:12:12Z
• Authors: David S. Bredt; Paul M. Hwang; Charles E. Glatt; Charles Lowenstein; Randall R. Reed; Solomon H. Snyder
• Keywords: Binding Sites; Base Sequence; Flavin Mononucleotide; Molecular Sequence Data; Gene Expression; DNA; Cell Line; Calmodulin; Cerebellum; Flavin-Adenine Dinucleotide; Animals; Humans; Amino Acid Oxidoreductases; Amino Acid Sequence; RNA, Messenger; Cloning, Molecular; Nitric Oxide Synthase; Phosphorylation; NADP; NADPH-Ferrihemoprotein Reductase

Nitric oxide is a messenger molecule, mediating the effect of endothelium-derived relaxing factor in blood vessels and the cytotoxic actions of macrophages, and playing a part in neuronal communication in the brain. Cloning of a complementary DNA for brain nitric oxide synthase reveals recognition sites for NADPH, FAD, flavin mononucleotide and calmodulin as well as phosphorylation sites, indicating that the synthase is regulated by many different factors. The only known mammalian enzyme with close homology is cytochrome P-450 reductase.