NOS1

NOS1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	4D1N, 4UCH, 4UH5, 4UH6, 4V3U, 5ADF, 5ADG, 5ADI, 5FVX, 5FVW, 5FVU, 5FVV
Identifiers
Aliases	NOS1, IHPS1, N-NOS, NC-NOS, NOS, bNOS, nNOS, nitric oxide synthase 1
External IDs	MGI: 97360 HomoloGene: 37327 GeneCards: NOS1
Targeted by Drug
	7-nitroindazole, nitroarginine
Gene ontology
Molecular function	• ion channel binding; • tetrahydrobiopterin binding; • NADP binding; • cadmium ion binding; • FMN binding; • metal ion binding; • heme binding; • oxidoreductase activity; • iron ion binding; • scaffold protein binding; • calmodulin binding; • protein binding; • sodium channel regulator activity; • flavin adenine dinucleotide binding; • arginine binding; • nitric-oxide synthase activity; • NADPH-hemoprotein reductase activity;
Cellular component	• membrane; • photoreceptor inner segment; • T-tubule; • synapse; • ryanodine receptor complex; • mitochondrion; • perinuclear region of cytoplasm; • caveola; • cytoskeleton; • cell projection; • dendritic spine; • Z disc; • sarcoplasmic reticulum membrane; • membrane raft; • protein complex; • sarcoplasmic reticulum; • sarcolemma; • cytosol; • cytoplasm; • nucleoplasm; • plasma membrane;
Biological process	• multicellular organismal response to stress; • positive regulation of guanylate cyclase activity; • positive regulation of adrenergic receptor signaling pathway involved in heart process; • regulation of sodium ion transport; • positive regulation of the force of heart contraction; • negative regulation of hydrolase activity; • striated muscle contraction; • regulation of neurogenesis; • negative regulation of serotonin uptake; • exogenous drug catabolic process; • positive regulation of transcription, DNA-templated; • peptidyl-cysteine S-nitrosylation; • negative regulation of adrenergic receptor signaling pathway involved in heart process; • cell redox homeostasis; • arginine catabolic process; • negative regulation of potassium ion transport; • nitric oxide mediated signal transduction; • negative regulation of calcium ion transport into cytosol; • myoblast fusion; • regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; • regulation of ryanodine-sensitive calcium-release channel activity; • regulation of cardiac conduction; • nitric oxide biosynthetic process; • positive regulation of sodium ion transmembrane transport; • cellular response to growth factor stimulus; • neurotransmitter biosynthetic process; • positive regulation of histone acetylation; • negative regulation of calcium ion transport; • regulation of cardiac muscle contraction; • oxidation-reduction process; • positive regulation of transcription from RNA polymerase II promoter; • response to hypoxia; • response to heat; • negative regulation of blood pressure; • retrograde trans-synaptic signaling by nitric oxide; • vasodilation;
	Sources:Amigo / QuickGO
RNA expression pattern
	; ;
	More reference expression data
Orthologs
	4842
	18125
	ENSG00000089250
	ENSMUSG00000029361
	P29475
	Q9Z0J4
	NM_000620; NM_001204213; NM_001204214; NM_001204218
	NM_008712
	NP_000611; NP_001191142; NP_001191143; NP_001191147
	NP_032738.1; NP_032738
	Wikidata
View/Edit Human	View/Edit Mouse

Nitric oxide synthase 1 (neuronal), also known as NOS1, is an enzyme that in humans is encoded by the NOS1 gene.^[4]^[5]

Function[edit]

Nitric oxide (NO) is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter and may be involved in long term potentiation. It is implicated in neurotoxicity associated with stroke and neurodegenerative diseases, neural regulation of smooth muscle, including peristalsis, and penile erection. NO is also responsible for endothelium-derived relaxing factor activity regulating blood pressure. In macrophages, NO mediates tumoricidal and bactericidal actions, as indicated by the fact that inhibitors of NO synthase (NOS) block these effects. Neuronal NOS and macrophage NOS are distinct isoforms.^[6] Both the neuronal and the macrophage forms are unusual among oxidative enzymes in requiring several electron donors: flavin adenine dinucleotide (FAD), flavin mononucleotide (FMN), NADPH, and tetrahydrobiopterin.^[7]

Clinical significance[edit]

It has been implicated in asthma,^[8]^[9] schizophrenia^[10]^[11] and restless leg syndrome.^[12] It has also been investigated with respect to bipolar disorder ^[13] and air pollution exposure.^[14]

Interactions[edit]

NOS1 has been shown to interact with DLG4^[15]^[16] and NOS1AP.^[15]

References[edit]

^ "Drugs that physically interact with Nitric oxide synthase 1 view/edit references on wikidata".
^ "Human PubMed Reference:".
^ "Mouse PubMed Reference:".
^ Kishimoto J, Spurr N, Liao M, Lizhi L, Emson P, Xu W (November 1992). "Localization of brain nitric oxide synthase (NOS) to human chromosome 12". Genomics. 14 (3): 802–4. doi:10.1016/S0888-7543(05)80192-2. PMID 1385308.
^ Geller DA, Lowenstein CJ, Shapiro RA, Nussler AK, Di Silvio M, Wang SC, Nakayama DK, Simmons RL, Snyder SH, Billiar TR (April 1993). "Molecular cloning and expression of inducible nitric oxide synthase from human hepatocytes". Proc. Natl. Acad. Sci. U.S.A. 90 (8): 3491–5. doi:10.1073/pnas.90.8.3491. PMC 46326. PMID 7682706.
^ Lowenstein CJ, Glatt CS, Bredt DS, Snyder SH (August 1992). "Cloned and expressed macrophage nitric oxide synthase contrasts with the brain enzyme". Proc. Natl. Acad. Sci. U.S.A. 89 (15): 6711–5. doi:10.1073/pnas.89.15.6711. PMC 49573. PMID 1379716.
^ "Entrez Gene: NOS1 Nitric oxide synthase 1 (neuronal)".
^ Grasemann H, Yandava CN, Drazen JM (December 1999). "Neuronal NO synthase (NOS1) is a major candidate gene for asthma". Clin. Exp. Allergy. 29. 29 Suppl 4: 39–41. PMID 10641565.
^ Leung TF, Liu EK, Tang NL, Ko FW, Li CY, Lam CW, Wong GW (October 2005). "Nitric oxide synthase polymorphisms and asthma phenotypes in Chinese children". Clin. Exp. Allergy. 35 (10): 1288–94. doi:10.1111/j.1365-2222.2005.02342.x. PMID 16238787.
^ Shinkai T, Ohmori O, Hori H, Nakamura J (2002). "Allelic association of the neuronal nitric oxide synthase (NOS1) gene with schizophrenia". Mol. Psychiatry. 7 (6): 560–3. doi:10.1038/sj.mp.4001041. PMID 12140778.
^ Reif A, Herterich S, Strobel A, Ehlis AC, Saur D, Jacob CP, Wienker T, Töpner T, Fritzen S, Walter U, Schmitt A, Fallgatter AJ, Lesch KP (March 2006). "A neuronal nitric oxide synthase (NOS-I) haplotype associated with schizophrenia modifies prefrontal cortex function". Mol. Psychiatry. 11 (3): 286–300. doi:10.1038/sj.mp.4001779. PMID 16389274.
^ Winkelmann J, Lichtner P, Schormair B, Uhr M, Hauk S, Stiasny-Kolster K, Trenkwalder C, Paulus W, Peglau I, Eisensehr I, Illig T, Wichmann HE, Pfister H, Golic J, Bettecken T, Pütz B, Holsboer F, Meitinger T, Müller-Myhsok B (February 2008). "Variants in the neuronal nitric oxide synthase (nNOS, NOS1) gene are associated with restless legs syndrome". Mov. Disord. 23 (3): 350–8. doi:10.1002/mds.21647. PMID 18058820.
^ Buttenschön HN, Mors O, Ewald H, McQuillin A, Kalsi G, Lawrence J, Gurling H, Kruse TA (January 2004). "No association between a neuronal nitric oxide synthase (NOS1) gene polymorphism on chromosome 12q24 and bipolar disorder". Am. J. Med. Genet. B Neuropsychiatr. Genet. 124B (1): 73–5. doi:10.1002/ajmg.b.20040. PMID 14681919.
^ Steenackers W, De Herdt E, De Boever P, Bos I, Int Panis L (2013). "Neuroinflammation induced by air pollution: gene expression analysis in laboratory animals". Master thesis, GROUP T – Leuven Engineering College.
^ ^a ^b Jaffrey SR, Snowman AM, Eliasson MJ, Cohen NA, Snyder SH (January 1998). "CAPON: a protein associated with neuronal nitric oxide synthase that regulates its interactions with PSD95". Neuron. 20 (1): 115–24. doi:10.1016/S0896-6273(00)80439-0. PMID 9459447.
^ Brenman JE, Chao DS, Gee SH, McGee AW, Craven SE, Santillano DR, Wu Z, Huang F, Xia H, Peters MF, Froehner SC, Bredt DS (March 1996). "Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and alpha1-syntrophin mediated by PDZ domains". Cell. 84 (5): 757–67. doi:10.1016/S0092-8674(00)81053-3. PMID 8625413.

v t e Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14)

1.14.11: 2-oxoglutarate	Prolyl hydroxylase Lysyl hydroxylase

1.14.13: NADH or NADPH	Flavin-containing monooxygenase FMO1 FMO2 FMO3 FMO4 FMO5 Nitric oxide synthase NOS1 NOS2 NOS3 Cholesterol 7 alpha-hydroxylase Methane monooxygenase 3A4 Lanosterol 14 alpha-demethylase 24-hydroxycholesterol 7α-hydroxylase

1.14.14: reduced flavin or flavoprotein	19A1 2D6 2E1

1.14.15: reduced iron-sulfur protein	11B1 11B2 11A1

1.14.16: reduced pteridine (BH4 dependent)	Phenylalanine hydroxylase Tyrosine hydroxylase Tryptophan hydroxylase

1.14.17: reduced ascorbate	Dopamine beta-hydroxylase

1.14.18-19: other	Tyrosinase Stearoyl-CoA desaturase-1

1.14.99 - miscellaneous	Cyclooxygenase Heme oxygenase (HMOX1) Squalene monooxygenase 17A1 21A2

v t e Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

NOS1

Contents

Function[edit]

Clinical significance[edit]

Interactions[edit]

See also[edit]

References[edit]

Further reading[edit]

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