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

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Veröffentlicht in:	Nature (London) 1991-06, Vol.351 (6329), p.714-718
Hauptverfasser:	Bredt, David S, Hwang, Paul M, Glatt, Charles E, Lowenstein, Charles, Reed, Randall R, Snyder, Solomon H
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Oxidoreductases - chemistry Amino Acid Oxidoreductases - genetics Amino Acid Oxidoreductases - metabolism Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Base Sequence Binding Sites Biological and medical sciences Brain Calmodulin - metabolism Cell Line Cerebellum - enzymology Cloning Cloning, Molecular Cytochrome Deoxyribonucleic acid DNA DNA - genetics Enzymes Enzymes and enzyme inhibitors FAD Flavin Mononucleotide - metabolism Flavin-Adenine Dinucleotide - metabolism Fundamental and applied biological sciences. Psychology Gene Expression Humans Molecular Sequence Data NADP - metabolism NADPH NADPH-Ferrihemoprotein Reductase - genetics Nitric oxide Nitric Oxide Synthase Oxidoreductases Phosphorylation Rats RNA, Messenger - analysis RNA, Messenger - genetics Sequence Homology, Nucleic Acid Tissue Distribution Transfection
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Zusammenfassung:	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.
ISSN:	0028-0836 1476-4687
DOI:	10.1038/351714a0