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NOS1

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From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens

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

OMIM:163731;MGI:97360;HomoloGene:37327;GeneCards:NOS1;OMA:NOS1 - orthologs

Gene location (Human)

Chr.	Chromosome 12 (human)^[1]

Band	12q24.22	Start	117,208,142bp^[1]
Band	12q24.22	End	117,452,170bp^[1]

Gene location (Mouse)

Chr.	Chromosome 5 (mouse)^[2]

Band	5 F\|5 57.29 cM	Start	117,919,097bp^[2]
Band	5 F\|5 57.29 cM	End	118,096,905bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

body of tongue

biceps brachii

Skeletal muscle tissue of biceps brachii

Skeletal muscle tissue of rectus abdominis

muscle of thigh

pons

gastrocnemius muscle

spinal ganglia

buccal mucosa cell

vastus lateralis muscle

Top expressed in

anterior amygdaloid area

pontine nuclei

subiculum

digastric muscle

temporal muscle

mammillary body

dorsal tegmental nucleus

ventromedial nucleus

lateral hypothalamus

sternocleidomastoid muscle

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	transmembrane transporter binding tetrahydrobiopterin binding NADP binding cadmium ion binding FMN binding metal ion binding heme binding oxidoreductase activity 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 discdkac sarcoplasmic reticulum membrane membrane raft sarcoplasmic reticulum sarcolemma cytosol cytoplasm nucleoplasm plasma membrane protein-containing complex calyx of Held nucleus vesicle membrane postsynaptic density
Biological process	multicellular organismal response to stress positive regulation of guanylate cyclase activity 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 positive regulation of transcription, DNA-templated peptidyl-cysteine S-nitrosylation 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 positive regulation of transcription by RNA polymerase II response to hypoxia response to heat negative regulation of blood pressure retrograde trans-synaptic signaling by nitric oxide vasodilation positive regulation of adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process synaptic signaling by nitric oxide response to hormone response to lipopolysaccharide positive regulation of peptidyl-serine phosphorylation
Sources:Amigo /QuickGO

Orthologs

Species

Human

Mouse

Entrez


4842


18125

Ensembl


ENSG00000089250


ENSMUSG00000029361

UniProt


P29475


Q9Z0J4

RefSeq (mRNA)


NM_000620 NM_001204213 NM_001204214 NM_001204218


NM_008712

RefSeq (protein)


NP_000611 NP_001191142 NP_001191143 NP_001191147


NP_032738

Location (UCSC)

Chr 12: 117.21 – 117.45 Mb

Chr 5: 117.92 – 118.1 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Nitric oxide synthase 1 (neuronal), also known asNOS1, is anenzyme that in humans is encoded by theNOS1gene.^[5]^[6]

Function

[edit]

Nitric oxide synthases (EC 1.14.13.39) (NOSs) are a family ofsynthases thatcatalyze the production ofnitric oxide (NO) fromL-arginine. NO is a chemical messenger with diverse functions throughout the body depending on its enzymatic source and tissue localization. In the brain and peripheral nervous system, where NOS1 is largely present, NO displays many properties of aneurotransmitter and may be involved inlong term potentiation. It is implicated inneurotoxicity associated withstroke and neurodegenerative diseases, neural regulation of smooth muscle, includingperistalsis and sphincter relaxation, and penile erection. NO is also responsible forendothelium-derived relaxing factor activity regulating blood pressure as produced from its related enzyme NOS3. Inmacrophages, NO mediates tumoricidal and bactericidal actions, as produced from its related enzyme NOS2. Various pharmacological inhibitors of NO synthases (NOS) block these effects, but further distinction of their function has been elucidated by animal models in which these specific genes have been inactivated. Neuronal NOS (NOS1), Endothelial NOS (NOS3), and Inducible NOSmacrophage NOS are distinct isoforms.^[7] 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, andtetrahydrobiopterin.^[8]

Clinical significance

[edit]

It has been implicated inasthma,^[9]^[10]schizophrenia,^[11]^[12]restless leg syndrome,^[13] andpsychostimulant neurotoxicity. It has also been investigated with respect tobipolar disorder^[14] andair pollution exposure.^[15]

Interactions

[edit]

NOS1 has been shown tointeract withDLG4^[16]^[17] andNOS1AP.^[16]

References

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000089250 –Ensembl, May 2017
^^a ^b ^cGRCm38: Ensembl release 89: ENSMUSG00000029361 –Ensembl, May 2017
^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^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.Bibcode:1993PNAS...90.3491G.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.Bibcode:1992PNAS...89.6711L.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. Archived fromthe original on 2013-01-05.
^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.S2CID 24110873.
^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.S2CID 42425890.
^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.S2CID 45596789.
^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 ^bJaffrey 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.S2CID 14613261.
^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.S2CID 15834673.

Miyagoe-Suzuki Y, Takeda SI (2001). "Association of neuronal nitric oxide synthase (nNOS) with alpha1-syntrophin at the sarcolemma".Microsc. Res. Tech.55 (3):164–70.doi:10.1002/jemt.1167.PMID 11747091.S2CID 28225242.
Waddington SN (2002)."Arginase in glomerulonephritis".Kidney Int.61 (3):876–81.doi:10.1046/j.1523-1755.2002.00236.x.PMID 11849441.
Rotilio G, Aquilano K, Ciriolo MR (2004)."Interplay of Cu,Zn superoxide dismutase and nitric oxide synthase in neurodegenerative processes".IUBMB Life.55 (10–11):629–34.doi:10.1080/15216540310001628717.PMID 14711010.S2CID 19518719.

This article incorporates text from theUnited States National Library of Medicine, which is in thepublic domain.

v t e PDB gallery
1b8q: SOLUTION STRUCTURE OF THE EXTENDED NEURONAL NITRIC OXIDE SYNTHASE PDZ DOMAIN COMPLEXED WITH AN ASSOCIATED PEPTIDE 1f20: CRYSTAL STRUCTURE OF RAT NEURONAL NITRIC-OXIDE SYNTHASE FAD/NADP+ DOMAIN AT 1.9A RESOLUTION. 1k2r: Structure of rat brain nNOS heme domain complexed with NG-nitro-L-arginine 1k2s: Structure of rat brain nNOS heme domain complexed with NG-allyl-L-arginine 1k2t: Structure of rat brain nNOS heme domain complexed with S-ethyl-N-phenyl-isothiourea 1k2u: Structure of rat brain nNOS heme domain complexed with S-ethyl-N-[4-(trifluoromethyl)phenyl] isothiourea 1lzx: Rat neuronal NOS heme domain with NG-hydroxy-L-arginine bound 1lzz: Rat neuronal NOS heme domain with N-isopropyl-N'-hydroxyguanidine bound 1m00: Rat neuronal NOS heme domain with N-butyl-N'-hydroxyguanidine bound 1mmv: Rat neuronal NOS heme domain with NG-propyl-L-arginine bound 1mmw: Rat neuronal NOS heme domain with vinyl-L-NIO bound 1om4: STRUCTURE OF RAT NEURONAL NOS HEME DOMAIN WITH L-ARGININE BOUND 1om5: STRUCTURE OF RAT NEURONAL NOS HEME DOMAIN WITH 3-BROMO-7-NITROINDAZOLE BOUND 1p6h: Rat neuronal NOS heme domain with L-N(omega)-nitroarginine-2,4-L-diaminobutyric amide bound 1p6i: Rat neuronal NOS heme domain with (4S)-N-(4-amino-5-[aminoethyl]aminopentyl)-N'-nitroguanidine bound 1p6j: Rat neuronal NOS heme domain with L-N(omega)-nitroarginine-(4R)-amino-L-proline amide bound 1p6k: Rat neuronal NOS D597N mutant heme domain with L-N(omega)-nitroarginine-2,4-L-diaminobutyric amide bound 1qau: UNEXPECTED MODES OF PDZ DOMAIN SCAFFOLDING REVEALED BY STRUCTURE OF NNOS-SYNTROPHIN COMPLEX 1qav: Unexpected Modes of PDZ Domain Scaffolding Revealed by Structure of NNOS-Syntrophin Complex 1qw6: Rat neuronal nitric oxide synthase oxygenase domain in complex with N-omega-propyl-L-Arg. 1qwc: Rat neuronal nitric oxide synthase oxygenase domain in complex with W1400 inhibitor. 1rs6: Rat neuronal NOS heme domain with D-lysine-D-nitroarginine amide bound 1rs7: Rat neuronal NOS heme domain with D-phenylalanine-D-nitroarginine amide bound 1tll: CRYSTAL STRUCTURE OF RAT NEURONAL NITRIC-OXIDE SYNTHASE REDUCTASE MODULE AT 2.3 A RESOLUTION. 1vag: Neuronal nitric oxide synthase oxygenase domain complexed with the inhibitor AR-R17477 1zvi: Rat Neuronal Nitric Oxide Synthase Oxygenase Domain 1zvl: Rat Neuronal Nitric Oxide Synthase Oxygenase Domain complexed with natural substrate L-Arg. 1zzq: Rat nNOS D597N mutant with L-N(omega)-Nitroarginine-(4R)-amino-L-proline amide bound 1zzr: Rat nNOS D597N/M336V double mutant with L-N(omega)-Nitroarginine-(4R)-amino-L-proline amide bound 1zzu: Rat nNOS D597N/M336V double mutant with L-N(omega)-Nitroarginine-2,4-L-Diaminobutyric Amide Bound 2g6h: Structure of rat nNOS heme domain (BH4 bound) in the reduced form 2g6i: Structure of rat nNOS heme domain (BH2-bound) in the reduced form 2g6j: Structure of rat nNOS (L337N) heme domain (4-aminobiopterin bound) complexed with NO 2g6k: Structure of rat nNOS heme domain (BH4 bound) complexed with NO 2g6l: Structure of rat nNOS heme domain (BH2 bound) complexed with NO 2g6m: Structure of rat nNOS heme domain (BH4 bound) complexed with CO 2g6n: Structure of rat nNOS heme domain (BH2 bound) complexed with CO 2hx3: Rat nNOS heme domain complexed with (4S)-N-{4-Amino-5-[(2-aminoethyl)-hydroxyamino]-pentyl}-N'-nitroguanidine 2hx4: Rat nNOS heme domain complexed with 4-N-(Nw-nitro-L-argininyl)-trans-4-hydroxyamino-L-proline amide

PDB gallery

1b8q: SOLUTION STRUCTURE OF THE EXTENDED NEURONAL NITRIC OXIDE SYNTHASE PDZ DOMAIN COMPLEXED WITH AN ASSOCIATED PEPTIDE
1f20: CRYSTAL STRUCTURE OF RAT NEURONAL NITRIC-OXIDE SYNTHASE FAD/NADP+ DOMAIN AT 1.9A RESOLUTION.
1k2r: Structure of rat brain nNOS heme domain complexed with NG-nitro-L-arginine
1k2s: Structure of rat brain nNOS heme domain complexed with NG-allyl-L-arginine
1k2t: Structure of rat brain nNOS heme domain complexed with S-ethyl-N-phenyl-isothiourea
1k2u: Structure of rat brain nNOS heme domain complexed with S-ethyl-N-[4-(trifluoromethyl)phenyl] isothiourea
1lzx: Rat neuronal NOS heme domain with NG-hydroxy-L-arginine bound
1lzz: Rat neuronal NOS heme domain with N-isopropyl-N'-hydroxyguanidine bound
1m00: Rat neuronal NOS heme domain with N-butyl-N'-hydroxyguanidine bound
1mmv: Rat neuronal NOS heme domain with NG-propyl-L-arginine bound
1mmw: Rat neuronal NOS heme domain with vinyl-L-NIO bound
1om4: STRUCTURE OF RAT NEURONAL NOS HEME DOMAIN WITH L-ARGININE BOUND
1om5: STRUCTURE OF RAT NEURONAL NOS HEME DOMAIN WITH 3-BROMO-7-NITROINDAZOLE BOUND
1p6h: Rat neuronal NOS heme domain with L-N(omega)-nitroarginine-2,4-L-diaminobutyric amide bound
1p6i: Rat neuronal NOS heme domain with (4S)-N-(4-amino-5-[aminoethyl]aminopentyl)-N'-nitroguanidine bound
1p6j: Rat neuronal NOS heme domain with L-N(omega)-nitroarginine-(4R)-amino-L-proline amide bound
1p6k: Rat neuronal NOS D597N mutant heme domain with L-N(omega)-nitroarginine-2,4-L-diaminobutyric amide bound
1qau: UNEXPECTED MODES OF PDZ DOMAIN SCAFFOLDING REVEALED BY STRUCTURE OF NNOS-SYNTROPHIN COMPLEX
1qav: Unexpected Modes of PDZ Domain Scaffolding Revealed by Structure of NNOS-Syntrophin Complex
1qw6: Rat neuronal nitric oxide synthase oxygenase domain in complex with N-omega-propyl-L-Arg.
1qwc: Rat neuronal nitric oxide synthase oxygenase domain in complex with W1400 inhibitor.
1rs6: Rat neuronal NOS heme domain with D-lysine-D-nitroarginine amide bound
1rs7: Rat neuronal NOS heme domain with D-phenylalanine-D-nitroarginine amide bound
1tll: CRYSTAL STRUCTURE OF RAT NEURONAL NITRIC-OXIDE SYNTHASE REDUCTASE MODULE AT 2.3 A RESOLUTION.
1vag: Neuronal nitric oxide synthase oxygenase domain complexed with the inhibitor AR-R17477
1zvi: Rat Neuronal Nitric Oxide Synthase Oxygenase Domain
1zvl: Rat Neuronal Nitric Oxide Synthase Oxygenase Domain complexed with natural substrate L-Arg.
1zzq: Rat nNOS D597N mutant with L-N(omega)-Nitroarginine-(4R)-amino-L-proline amide bound
1zzr: Rat nNOS D597N/M336V double mutant with L-N(omega)-Nitroarginine-(4R)-amino-L-proline amide bound
1zzu: Rat nNOS D597N/M336V double mutant with L-N(omega)-Nitroarginine-2,4-L-Diaminobutyric Amide Bound
2g6h: Structure of rat nNOS heme domain (BH4 bound) in the reduced form
2g6i: Structure of rat nNOS heme domain (BH2-bound) in the reduced form
2g6j: Structure of rat nNOS (L337N) heme domain (4-aminobiopterin bound) complexed with NO
2g6k: Structure of rat nNOS heme domain (BH4 bound) complexed with NO
2g6l: Structure of rat nNOS heme domain (BH2 bound) complexed with NO
2g6m: Structure of rat nNOS heme domain (BH4 bound) complexed with CO
2g6n: Structure of rat nNOS heme domain (BH2 bound) complexed with CO
2hx3: Rat nNOS heme domain complexed with (4S)-N-{4-Amino-5-[(2-aminoethyl)-hydroxyamino]-pentyl}-N'-nitroguanidine
2hx4: Rat nNOS heme domain complexed with 4-N-(Nw-nitro-L-argininyl)-trans-4-hydroxyamino-L-proline amide

v t e Oxidoreductases:dioxygenases, includingsteroid hydroxylases (EC 1.14)
1.14.11:2-oxoglutarate	Prolyl hydroxylase HIF prolyl-hydroxylase EGLN1 EGLN2 EGLN3 P4HTM Lysyl hydroxylase AlkB ALKBH1 FTO
1.14.13:NADH orNADPH	Flavin-containing monooxygenase FMO1 FMO2 FMO3 FMO4 FMO5 Nitric oxide synthase NOS1 NOS2 NOS3 Cholesterol 7 alpha-hydroxylase Methane monooxygenase 3A4 14α-demethylase 24-hydroxycholesterol 7α-hydroxylase
1.14.14: reducedflavin orflavoprotein	19A1 2D6 2E1
1.14.15: reducediron–sulfur protein	11B1 11B2 11A1
1.14.16: reducedpteridine (BH4 dependent)	Phenylalanine hydroxylase Tyrosine hydroxylase Tryptophan hydroxylase
1.14.17: reducedascorbate	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 Ecdysone 20-monooxygenase Deoxyhypusine monooxygenase

Enzymes involved inneurotransmission

monoamine

histidine →histamine

anabolism:	Histidine decarboxylase
catabolism:	Histamine N-methyltransferase Diamine oxidase

tyrosine→dopamine→epinephrine

anabolism:	Tyrosine hydroxylase AromaticL-amino acid decarboxylase Dopamine beta-hydroxylase Phenylethanolamine N-methyltransferase
catabolism:	Catechol-O-methyl transferase Monoamine oxidase A B

glutamate→GABA

anabolism:	Glutamate decarboxylase
catabolism:	4-aminobutyrate transaminase

tryptophan→serotonin→melatonin

arginine→NO

Nitric oxide synthase (NOS1,NOS2,NOS3)

choline→Acetylcholine

anabolism:	Choline acetyltransferase
catabolism:	Cholinesterase (Acetylcholinesterase,Butyrylcholinesterase)

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
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	EC1Oxidoreductases (list) EC2Transferases (list) EC3Hydrolases (list) EC4Lyases (list) EC5Isomerases (list) EC6Ligases (list) EC7Translocases (list)

Nitric oxide signaling modulators

Forms

Targets

sGC	Activators/stimulators:Ataciguat BAY 41-2272 BAY 41-8543 BAY 60-4552 BI-703704 Cinaciguat (BAY 58-2667) GSK-2181236A Praliciguat Riociguat Vericiguat Inhibitors:ODQ

NO donors
(prodrugs)

Nitrosyl compounds:Metal nitrosyl complexes:Roussin's black salt
Roussin's red salt
Sodium nitroprusside (SNP)

NONOates (diazeniumdiolates):Diethylamine/NO (DEA/NO)
Diethylenetriamine/NO (DETA/NO)
GLO/NO
JS-K
Methylamine hexamethylene methylamine/NO (MAHMA/NO)
PROLI/NO
Spermine/NO (SPER/NO)
V-PYRRO/NO

Heterocyclic compounds:Furoxans:Furoxan
REC15/2739;Sydnonimines:Feprosidnine
Linsidomine (SIN-1)
Molsidomine (SIN-10)
Sydnonimine

Unsorted:Cimlanod
FK-409
FR144220
FR146881
N-Acetyl-N-acetoxy-4-chlorobenzenesulfonamide

Enzyme
(inhibitors)

NOS

nNOS	3-Bromo-7-nitroindazole 3-Chloroindazole 3-Chloro-5-nitroindazole 5-Nitroindazole 6-Nitroindazole 7-Nitroindazole A-84643 Aminoguanidine (pimagedine) ARL-17477 Indazole N⁵-(1-Iminoethyl)-L-ornithine (L-NIO) N^ω-Methyl-L-arginine (L-NMA) N^ω-Propyl-L-arginine (L-NPA) Nitroarginine (NNA, NOARG) Pentamidine isethionate TRIM
iNOS	1-Amino-2-hydroxyguanidine 2-Ethylaminoguanidine 2-Iminopiperidine 1400W AEITU Aminoguanidine (pimagedine) AMT AR-C 102222 BYK-191023 Canavanine Cindunistat (SD-6010) EITU IPTU MITU N⁵-(1-Iminoethyl)-L-ornithine (L-NIO) N⁶-(1-Iminoethyl)-L-lysine (L-NIL) N^ω-Methyl-L-arginine (L-NMA) Ronopterin (VAS-203) TRIM
eNOS	Aminoguanidine (pimagedine) N⁵-(1-Iminoethyl)-L-ornithine (L-NIO) N^ω-Methyl-L-arginine (L-NMA) Nitroarginine (NNA, NOARG)
Unsorted	Asymmetric dimethylarginine (ADMA) CKD-712 Guanidinoethyldisulfide (GED) GW-273629 Indospicine KD-7040 Nitroarginine methyl ester (NAME) NCX-456 NXN-462 ONO-1714 VAS-2381