Journal Article10.1016/0006-2952(95)00181-6
Isoforms of nitric oxide synthase. Properties, cellular distribution and expressional control.
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TL;DR: Information on NOS has increased to such an extent that this new commentary had to be restricted to some important biochemical aspects of the NOS enzymes, namely their protein and cDNA structure, their cellular distribution, and the mechanism controlling their expression.
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About: This article is published in Biochemical Pharmacology. The article was published on 26 Oct 1995. The article focuses on the topics: Soluble guanylyl cyclase & Isozyme.
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References
Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme.
David S. Bredt,Solomon H. Snyder +1 more
TL;DR: It is shown that nitric oxide synthetase activity requires calmodulin, and the native enzyme appears to be a monomer.
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Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme (endothelium-derived relaxing factor/arginine/cGMP)
David S. Bredt,Solomon H. Snyder +1 more
- 01 Jan 2016
TL;DR: In this paper, it was shown that NO synthetase is a calmodulin-requiring enzyme, and showed that NO formation is accompanied by the stoichiometric conversion of arginine to citrulline.
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Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase.
David S. Bredt,Paul M. Hwang,Charles E. Glatt,Charles J. Lowenstein,Randall R. Reed,Randall R. Reed,Solomon H. Snyder +6 more
TL;DR: 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.
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Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase
David S. Bredt,Paul M. Hwang,Charles E. Glatt,Charles J. Lowenstein,Randall R. Reed,Randall R. Reed,Solomon H. Snyder +6 more
TL;DR: The cloning, characterization and functional expression of cDNAs encoding rat brain nitric oxide synthase (NOS) are described, which is responsible for intracellular synthesis of NO from arginine, and the sequence reveals putative sites for interaction with calmodulin and for phosphorylation by cyclic AMP-dependent protein kinase.
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Role of nitric oxide synthesis in macrophage antimicrobial activity.
TL;DR: It is suggested that synthesis of NO mediates much of the antimicrobial activity of mouse macrophages against some fungal, helminthic, protozoal and bacterial pathogens.
1.6K