Identification
- Generic Name
- Citrulline
- DrugBank Accession Number
- DB00155
- Background
Citrulline is an amino acid. It is made from ornithine and carbamoyl phosphate in one of the central reactions in the urea cycle. It is also produced from arginine as a by-product of the reaction catalyzed by NOS family. Its name is derived from citrullus, the Latin word for watermelon, from which it was first isolated.
- Type
- Small Molecule
- Groups
- Investigational, Nutraceutical
- Structure
Structure for Citrulline (DB00155)
- Weight
- Average: 175.1857
Monoisotopic: 175.095691297 - Chemical Formula
- C6H13N3O3
- Synonyms
- (S)-2-Amino-5-ureidopentanoic acid
- 2-Amino-5-ureidovaleric acid
- alpha-amino-delta-Ureidovaleric acid
- Cit
- Citrulina
- Citrulline
- delta-Ureidonorvaline
- L-2-Amino-5-ureidovaleric acid
- L-Citrulline
- N(5)-(Aminocarbonyl)-L-ornithine
- N(delta)-Carbamylornithine
- N5-(Aminocarbonyl)ornithine
- N5-Carbamoyl-L-ornithine
- N5-carbamoylornithine
- α-amino-δ-ureidovaleric acid
- δ-ureidonorvaline
Pharmacology
- Indication
Used for nutritional supplementation, also for treating dietary shortage or imbalance.
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- Contraindications & Blackbox Warnings
Prevent Adverse Drug Events TodayTap into our Clinical API for life-saving information on contraindications & blackbox warnings, population restrictions, harmful risks, & more.Avoid life-threatening adverse drug events with our Clinical API- Pharmacodynamics
A non-essential amino acid and a precursor of arginine. Citrulline supplements have been claimed to promote energy levels, stimulate the immune system and help detoxify ammonia (a cell toxin). L-citrulline is made from L-ornithine and carbamoyl phosphate in one of the central reactions in the urea cycle. It is also produced from L-arginine as a by-product of the reaction catalyzed by the enzyme NO synthase. L-citrulline, while being an amino acid, is not involved in protein synthesis and is not one of the amino acids coded for by DNA. Although citrulline cannot be incorporated in proteins during protein synthesis, several proteins are known to contain citrulline as an amino acid. These citrulline residues are generated by a family of enzymes called peptidylarginine deiminases (PADs), which convert the amino acid arginine into citrulline. Proteins that contain citrulline residues include myelin basic protein (MBP), fillagrin and several histone proteins.
- Mechanism of action
L-citrulline is converted to L-arginine by argininosuccinate synthase. L-arginine is in turn responsible for citrulline's therapeutic affects. Many of L-arginine's activities, including its possible anti-atherogenic actions, may be accounted for by its role as the precursor to nitric oxide or NO. NO is produced by all tissues of the body and plays very important roles in the cardiovascular system, immune system and nervous system. NO is formed from L-arginine via the enzyme nitric oxide synthase or synthetase (NOS), and the effects of NO are mainly mediated by 3',5' -cyclic guanylate or cyclic GMP. NO activates the enzyme guanylate cyclase, which catalyzes the synthesis of cyclic GMP from guanosine triphosphate or GTP. Cyclic GMP is converted to guanylic acid via the enzyme cyclic GMP phosphodiesterase. NOS is a heme-containing enzyme with some sequences similar to cytochrome P-450 reductase. Several isoforms of NOS exist, two of which are constitutive and one of which is inducible by immunological stimuli. The constitutive NOS found in the vascular endothelium is designated eNOS and that present in the brain, spinal cord and peripheral nervous system is designated nNOS. The form of NOS induced by immunological or inflammatory stimuli is known as iNOS. iNOS may be expressed constitutively in select tissues such as lung epithelium. All the nitric oxide synthases use NADPH (reduced nicotinamide adenine dinucleotide phosphate) and oxygen (O2) as cosubstrates, as well as the cofactors FAD (flavin adenine dinucleotide), FMN (flavin mononucleotide), tetrahydrobiopterin and heme. Interestingly, ascorbic acid appears to enhance NOS activity by increasing intracellular tetrahydrobiopterin. eNOS and nNOS synthesize NO in response to an increased concentration of calcium ions or in some cases in response to calcium-independent stimuli, such as shear stress. In vitro studies of NOS indicate that the Km of the enzyme for L-arginine is in the micromolar range. The concentration of L-arginine in endothelial cells, as well as in other cells, and in plasma is in the millimolar range. What this means is that, under physiological conditions, NOS is saturated with its L-arginine substrate. In other words, L-arginine would not be expected to be rate-limiting for the enzyme, and it would not appear that supraphysiological levels of L-arginine which could occur with oral supplementation of the amino acid would make any difference with regard to NO production. The reaction would appear to have reached its maximum level. However, in vivo studies have demonstrated that, under certain conditions, e.g. hypercholesterolemia, L-arginine could enhance endothelial-dependent vasodilation and NO production.
Target Actions Organism UNitric oxide synthase, endothelial Not Available Humans UArgininosuccinate synthase Not Available Humans UN(G),N(G)-dimethylarginine dimethylaminohydrolase 2 Not Available Humans UN(G),N(G)-dimethylarginine dimethylaminohydrolase 1 Not Available Humans UOrnithine carbamoyltransferase, mitochondrial Not Available Humans UNitric oxide synthase, brain Not Available Humans UNitric oxide synthase, inducible Not Available Humans UProtein-arginine deiminase type-4 Not Available Humans NProtein-arginine deiminase type-6 product ofHumans UProtein-arginine deiminase type-1 Not Available Humans UProtein-arginine deiminase type-3 Not Available Humans UProtein-arginine deiminase type-2 Not Available Humans - Absorption
Not Available
- Volume of distribution
Not Available
- Protein binding
Not Available
- Metabolism
- Not Available
- Route of elimination
Not Available
- Half-life
Not Available
- Clearance
Not Available
- Adverse Effects
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Not Available
- Pathways
- Pharmacogenomic Effects/ADRs Browse all" title="About SNP Mediated Effects/ADRs" id="snp-actions-info" class="drug-info-popup" href="javascript:void(0);">
- Not Available
Interactions
- Drug Interactions Learn More" title="About Drug Interactions" id="structured-interactions-info" class="drug-info-popup" href="javascript:void(0);">
- This information should not be interpreted without the help of a healthcare provider. If you believe you are experiencing an interaction, contact a healthcare provider immediately. The absence of an interaction does not necessarily mean no interactions exist.
Drug Interaction Integrate drug-drug
interactions in your softwareAcetazolamide The excretion of Citrulline can be decreased when combined with Acetazolamide. Acetylsalicylic acid The excretion of Citrulline can be decreased when combined with Acetylsalicylic acid. Acyclovir The excretion of Citrulline can be decreased when combined with Acyclovir. Adefovir dipivoxil The excretion of Citrulline can be decreased when combined with Adefovir dipivoxil. Aminohippuric acid The excretion of Citrulline can be decreased when combined with Aminohippuric acid. - Food Interactions
- No interactions found.
Products
Drug product information from 10+ global regionsOur datasets provide approved product information including:dosage, form, labeller, route of administration, and marketing period.Access drug product information from over 10 global regions.- Product Ingredients
Ingredient UNII CAS InChI Key Citrulline malate PAB4036KHO 70796-17-7 DROVUXYZTXCEBX-WCCKRBBISA-N - Over the Counter Products
Name Dosage Strength Route Labeller Marketing Start Marketing End Region Image STIMOL ORAL SOLUTION 1g/10ml Solution 1 g/10ml Oral EP PLUS GROUP SDN. BHD. 2020-09-08 2022-01-14 Malaysia 
- Mixture Products
Name Ingredients Dosage Route Labeller Marketing Start Marketing End Region Image โปลิเลโว Citrulline (100 mg) + Arginine hydrochloride (200 mg) + Cyanocobalamin (500 mcg) + Folic acid (1 mg) + Nicotinamide (15 mg) + Ornithine hydrochloride (100 mg) Solution บริษัท มิลลิเมด จำกัด จำกัด 2012-03-08 Not applicable Thailand 
- Unapproved/Other Products
Name Ingredients Dosage Route Labeller Marketing Start Marketing End Region Image Lipovite Citrulline (1 mg/1mL) + Choline (1 mg/1mL) + Chromium (1 mg/1mL) + Dexpanthenol (1 mg/1mL) + Inositol (1 mg/1mL) + Levocarnitine (1 mg/1mL) + Lidocaine (1 mg/1mL) + Mecobalamin (1 mg/1mL) + Methionine sulfoximine (1 mg/1mL) + Nicotinamide (1 mg/1mL) + Pyridoxine (1 mg/1mL) + Riboflavin (1 mg/1mL) + Thiamine chloride (1 mg/1mL) Injection Intramuscular Perdido Key Health And Wellness Inc 2015-11-23 Not applicable US 
Categories
- Drug Categories
- Chemical TaxonomyProvided by Classyfire
- Description
- This compound belongs to the class of organic compounds known as l-alpha-amino acids. These are alpha amino acids which have the L-configuration of the alpha-carbon atom.
- Kingdom
- Organic compounds
- Super Class
- Organic acids and derivatives
- Class
- Carboxylic acids and derivatives
- Sub Class
- Amino acids, peptides, and analogues
- Direct Parent
- L-alpha-amino acids
- Alternative Parents
- Fatty acids and conjugates / Isoureas / Amino acids / Monocarboxylic acids and derivatives / Carboxylic acids / Carboximidamides / Organopnictogen compounds / Organic oxides / Monoalkylamines / Imines show 2 more
- Substituents
- Aliphatic acyclic compound / Amine / Amino acid / Carbonyl group / Carboximidamide / Carboximidic acid derivative / Carboxylic acid / Fatty acid / Hydrocarbon derivative / Imine show 11 more
- Molecular Framework
- Aliphatic acyclic compounds
- External Descriptors
- citrulline (CHEBI:16349) / Other amino acids (C00327)
- Affected organisms
- Humans and other mammals
Chemical Identifiers
- UNII
- 29VT07BGDA
- CAS number
- 372-75-8
- InChI Key
- RHGKLRLOHDJJDR-BYPYZUCNSA-N
- InChI
- InChI=1S/C6H13N3O3/c7-4(5(10)11)2-1-3-9-6(8)12/h4H,1-3,7H2,(H,10,11)(H3,8,9,12)/t4-/m0/s1
- IUPAC Name
- (2S)-2-amino-5-(carbamoylamino)pentanoic acid
- SMILES
- N[C@@H](CCCNC(N)=O)C(O)=O
References
- Synthesis Reference
Hua Bai, Peijie Yang, Zhengjie Chen, Chongyan Xu, Zhaorul Li, Zigang Zhao, Luyan Jiang, Zongyi Yang, Jiang Li, "PROCESSES FOR THE PRODUCTION OF L-CITRULLINE." U.S. Patent US20090142813, issued June 04, 2009.
US20090142813- General References
- Not Available
- External Links
- Human Metabolome Database
- HMDB0000904
- KEGG Drug
- D07706
- KEGG Compound
- C00327
- PubChem Compound
- 9750
- PubChem Substance
- 46506583
- ChemSpider
- 9367
- BindingDB
- 92903
- 2567
- ChEBI
- 16349
- ChEMBL
- CHEMBL444814
- ZINC
- ZINC000001532614
- PharmGKB
- PA164747225
- Guide to Pharmacology
- GtP Drug Page
- PDBe Ligand
- CIR
- Wikipedia
- Citrulline
- PDB Entries
- 1h70 / 1j1z / 1j21 / 1k97 / 1kod / 1kp3 / 1lxy / 1ol1 / 1qr3 / 2c6z … show 51 more
- MSDS
- Download (72.8 KB)
Clinical Trials
- Clinical Trials Learn More" title="About Clinical Trials" id="clinical-trials-info" class="drug-info-popup" href="javascript:void(0);">
Phase Status Purpose Conditions Count 3 Completed Prevention Heart Defects,Congenital / Pulmonary Hypertension (PH) 1 3 Completed Prevention Lung Injury, Acute (ALI) 1 3 Completed Treatment Duchenne Muscular Dystrophy (DMD) 1 3 Completed Treatment Post-Poliomyelitis Syndrome 1 3 Not Yet Recruiting Treatment Malnutrition / Severe Chronic Obstructive Pulmonary Disease 1
Pharmacoeconomics
- Manufacturers
- Not Available
- Packagers
- Medisca Inc.
- Dosage Forms
Form Route Strength Injection Intramuscular Solution Oral 1.000 g Solution Oral 1 g/10ml Tablet Oral Solution - Prices
Unit description Cost Unit L-citrulline powder 1.01USD g DrugBank does not sell nor buy drugs. Pricing information is supplied for informational purposes only.- Patents
- Not Available
Properties
- State
- Solid
- Experimental Properties
Property Value Source melting point (°C) 235.5 °C PhysProp water solubility 200 g/L (at 20 °C) Not Available logP -3.19 SANGSTER (1994) pKa 2.43 (at 25 °C) KORTUM,G ET AL (1961) - Predicted Properties
Property Value Source Water Solubility 21.8 mg/mL ALOGPS logP -3.3 ALOGPS logP -3.9 Chemaxon logS -0.9 ALOGPS pKa (Strongest Acidic) 2.27 Chemaxon pKa (Strongest Basic) 9.23 Chemaxon Physiological Charge 0 Chemaxon Hydrogen Acceptor Count 4 Chemaxon Hydrogen Donor Count 4 Chemaxon Polar Surface Area 118.44 Å2 Chemaxon Rotatable Bond Count 5 Chemaxon Refractivity 41.33 m3·mol-1 Chemaxon Polarizability 17.35 Å3 Chemaxon Number of Rings 0 Chemaxon Bioavailability 1 Chemaxon Rule of Five Yes Chemaxon Ghose Filter No Chemaxon Veber's Rule No Chemaxon MDDR-like Rule No Chemaxon - Predicted ADMET Features
Property Value Probability Human Intestinal Absorption + 0.6863 Blood Brain Barrier + 0.8961 Caco-2 permeable - 0.813 P-glycoprotein substrate Non-substrate 0.616 P-glycoprotein inhibitor I Non-inhibitor 0.9782 P-glycoprotein inhibitor II Non-inhibitor 0.982 Renal organic cation transporter Non-inhibitor 0.9331 CYP450 2C9 substrate Non-substrate 0.7522 CYP450 2D6 substrate Non-substrate 0.7828 CYP450 3A4 substrate Non-substrate 0.8127 CYP450 1A2 substrate Non-inhibitor 0.9415 CYP450 2C9 inhibitor Non-inhibitor 0.9149 CYP450 2D6 inhibitor Non-inhibitor 0.97 CYP450 2C19 inhibitor Non-inhibitor 0.9018 CYP450 3A4 inhibitor Non-inhibitor 0.8309 CYP450 inhibitory promiscuity Low CYP Inhibitory Promiscuity 0.9896 Ames test Non AMES toxic 0.5916 Carcinogenicity Non-carcinogens 0.9113 Biodegradation Ready biodegradable 0.9247 Rat acute toxicity 1.3397 LD50, mol/kg Not applicable hERG inhibition (predictor I) Weak inhibitor 0.972 hERG inhibition (predictor II) Non-inhibitor 0.9716
Spectra
- Mass Spec (NIST)
- Not Available
- Spectra
- Chromatographic Properties
Collision Cross Sections (CCS)
Adduct CCS Value (Å2) Source type Source [M-H]- 145.7304278 predictedDarkChem Lite v0.1.0 [M-H]- 134.6028944 predictedDarkChem Standard v0.1.0 [M-H]- 145.7331278 predictedDarkChem Lite v0.1.0 [M-H]- 130.95819 predictedDeepCCS 1.0 (2019) [M+H]+ 144.9070278 predictedDarkChem Lite v0.1.0 [M+H]+ 134.6671166 predictedDarkChem Standard v0.1.0 [M+H]+ 144.1951278 predictedDarkChem Lite v0.1.0 [M+H]+ 134.78554 predictedDeepCCS 1.0 (2019) [M+Na]+ 144.0727278 predictedDarkChem Lite v0.1.0 [M+Na]+ 144.2345278 predictedDarkChem Lite v0.1.0 [M+Na]+ 144.0088278 predictedDarkChem Lite v0.1.0 [M+Na]+ 144.07446 predictedDeepCCS 1.0 (2019)
Targets
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- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Tetrahydrobiopterin binding
- Specific Function
- Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. NO mediates vascular endothelial growth factor (VEGF)-induce...
- Gene Name
- NOS3
- Uniprot ID
- P29474
- Uniprot Name
- Nitric oxide synthase, endothelial
- Molecular Weight
- 133287.62 Da
References
- Hayakawa H, Raij L: Relationship between hypercholesterolaemia, endothelial dysfunction and hypertension. J Hypertens. 1999 May;17(5):611-9. [Article]
- Trovati M, Massucco P, Mattiello L, Costamagna C, Aldieri E, Cavalot F, Anfossi G, Bosia A, Ghigo D: Human vascular smooth muscle cells express a constitutive nitric oxide synthase that insulin rapidly activates, thus increasing guanosine 3':5'-cyclic monophosphate and adenosine 3':5'-cyclic monophosphate concentrations. Diabetologia. 1999 Jul;42(7):831-9. [Article]
- McDuffie JE, Coaxum SD, Maleque MA: 5-hydroxytryptamine evokes endothelial nitric oxide synthase activation in bovine aortic endothelial cell cultures. Proc Soc Exp Biol Med. 1999 Sep;221(4):386-90. [Article]
- Tan E, Gurjar MV, Sharma RV, Bhalla RC: Estrogen receptor-alpha gene transfer into bovine aortic endothelial cells induces eNOS gene expression and inhibits cell migration. Cardiovasc Res. 1999 Aug 15;43(3):788-97. [Article]
- Abu-Soud HM, Ichimori K, Presta A, Stuehr DJ: Electron transfer, oxygen binding, and nitric oxide feedback inhibition in endothelial nitric-oxide synthase. J Biol Chem. 2000 Jun 9;275(23):17349-57. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Toxic substance binding
- Specific Function
- Is indirectly involved in the control of blood pressure.
- Gene Name
- ASS1
- Uniprot ID
- P00966
- Uniprot Name
- Argininosuccinate synthase
- Molecular Weight
- 46530.055 Da
References
- Braissant O, Honegger P, Loup M, Iwase K, Takiguchi M, Bachmann C: Hyperammonemia: regulation of argininosuccinate synthetase and argininosuccinate lyase genes in aggregating cell cultures of fetal rat brain. Neurosci Lett. 1999 May 7;266(2):89-92. [Article]
- Braissant O, Gotoh T, Loup M, Mori M, Bachmann C: L-arginine uptake, the citrulline-NO cycle and arginase II in the rat brain: an in situ hybridization study. Brain Res Mol Brain Res. 1999 Jul 5;70(2):231-41. [Article]
- Keilhoff G, Reiser M, Stanarius A, Aoki E, Wolf G: Citrulline immunohistochemistry for demonstration of NOS activity in vivo and in vitro. Nitric Oxide. 2000 Aug;4(4):343-53. [Article]
- Zhang B, Cao GL, Domachowske J, Jackson MJ, Porasuphatana S, Rosen GM: Stable expression of varied levels of inducible nitric oxide synthase in primary cultures of endothelial cells. Anal Biochem. 2000 Nov 15;286(2):198-205. [Article]
- Zhang WY, Gotoh T, Oyadomari S, Mori M: Coinduction of inducible nitric oxide synthase and arginine recycling enzymes in cytokine-stimulated PC12 cells and high output production of nitric oxide. Brain Res Mol Brain Res. 2000 Nov 10;83(1-2):1-8. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Dimethylargininase activity
- Specific Function
- Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation.
- Gene Name
- DDAH2
- Uniprot ID
- O95865
- Uniprot Name
- N(G),N(G)-dimethylarginine dimethylaminohydrolase 2
- Molecular Weight
- 29643.54 Da
References
- Tran CT, Fox MF, Vallance P, Leiper JM: Chromosomal localization, gene structure, and expression pattern of DDAH1: comparison with DDAH2 and implications for evolutionary origins. Genomics. 2000 Aug 15;68(1):101-5. [Article]
- Tain YL, Baylis C: Determination of dimethylarginine dimethylaminohydrolase activity in the kidney. Kidney Int. 2007 Oct;72(7):886-9. Epub 2007 Jul 25. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Metal ion binding
- Specific Function
- Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation.
- Gene Name
- DDAH1
- Uniprot ID
- O94760
- Uniprot Name
- N(G),N(G)-dimethylarginine dimethylaminohydrolase 1
- Molecular Weight
- 31121.5 Da
References
- Mishima T, Hamada T, Ui-Tei K, Takahashi F, Miyata Y, Imaki J, Suzuki H, Yamashita K: Expression of DDAH1 in chick and rat embryos. Brain Res Dev Brain Res. 2004 Feb 20;148(2):223-32. [Article]
- Tran CT, Fox MF, Vallance P, Leiper JM: Chromosomal localization, gene structure, and expression pattern of DDAH1: comparison with DDAH2 and implications for evolutionary origins. Genomics. 2000 Aug 15;68(1):101-5. [Article]
- Arrigoni FI, Vallance P, Haworth SG, Leiper JM: Metabolism of asymmetric dimethylarginines is regulated in the lung developmentally and with pulmonary hypertension induced by hypobaric hypoxia. Circulation. 2003 Mar 4;107(8):1195-201. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Phospholipid binding
- Specific Function
- Not Available
- Gene Name
- OTC
- Uniprot ID
- P00480
- Uniprot Name
- Ornithine carbamoyltransferase, mitochondrial
- Molecular Weight
- 39934.775 Da
References
- Quintero MJ, Muro-Pastor AM, Herrero A, Flores E: Arginine catabolism in the cyanobacterium Synechocystis sp. Strain PCC 6803 involves the urea cycle and arginase pathway. J Bacteriol. 2000 Feb;182(4):1008-15. [Article]
- Morizono H, Cabrera-Luque J, Shi D, Gallegos R, Yamaguchi S, Yu X, Allewell NM, Malamy MH, Tuchman M: Acetylornithine transcarbamylase: a novel enzyme in arginine biosynthesis. J Bacteriol. 2006 Apr;188(8):2974-82. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Tetrahydrobiopterin binding
- Specific Function
- Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter. P...
- Gene Name
- NOS1
- Uniprot ID
- P29475
- Uniprot Name
- Nitric oxide synthase, brain
- Molecular Weight
- 160969.095 Da
References
- Kominami S, Yamazaki T, Koga T, Hori H: EPR studies on the photo-induced intermediates of ferric NO complexes of rat neuronal nitric oxide synthase trapped at low temperature. J Biochem. 1999 Oct;126(4):756-61. [Article]
- Giraldi-Guimaraes A, Tenorio F, Bruning G, Mayer B, Mendez-Otero R, Cavalcante LA: Nitric oxide synthase expression in the opossum superior colliculus: a histochemical, immunohistochemical and biochemical study. Brain Behav Evol. 1999 Dec;54(6):303-13. [Article]
- Perry JM, Zhao Y, Marletta MA: Cu2+ and Zn2+ inhibit nitric-oxide synthase through an interaction with the reductase domain. J Biol Chem. 2000 May 12;275(19):14070-6. [Article]
- Adak S, Wang Q, Stuehr DJ: Arginine conversion to nitroxide by tetrahydrobiopterin-free neuronal nitric-oxide synthase. Implications for mechanism. J Biol Chem. 2000 Oct 27;275(43):33554-61. [Article]
- Yu W, Juang S, Lee J, Liu T, Cheng J: Decrease of neuronal nitric oxide synthase in the cerebellum of aged rats. Neurosci Lett. 2000 Sep 8;291(1):37-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Tetrahydrobiopterin binding
- Specific Function
- Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity ...
- Gene Name
- NOS2
- Uniprot ID
- P35228
- Uniprot Name
- Nitric oxide synthase, inducible
- Molecular Weight
- 131116.3 Da
References
- Cunningham JM, Rayne RC: Radiochemical measurement of NOS activity by conversion of [14C]L-arginine to citrulline using HPLC separation. Methods Mol Biol. 1998;100:75-81. [Article]
- Keilhoff G, Reiser M, Stanarius A, Aoki E, Wolf G: Citrulline immunohistochemistry for demonstration of NOS activity in vivo and in vitro. Nitric Oxide. 2000 Aug;4(4):343-53. [Article]
- Conrad KP, Powers RW, Davis AK, Novak J: Citrulline is not the major product using the standard "NOS activity" assay on renal cortical homogenates. Am J Physiol Regul Integr Comp Physiol. 2002 Jan;282(1):R303-10. [Article]
- Knowles RG, Salter M: Measurement of NOS activity by conversion of radiolabeled arginine to citrulline using ion-exchange separation. Methods Mol Biol. 1998;100:67-73. [Article]
- Yi GB, McClendon D, Desaiah D, Goddard J, Lister A, Moffitt J, Meer RK, deShazo R, Lee KS, Rockhold RW: Fire ant venom alkaloid, isosolenopsin A, a potent and selective inhibitor of neuronal nitric oxide synthase. Int J Toxicol. 2003 Mar-Apr;22(2):81-6. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Protein-arginine deiminase activity
- Specific Function
- Catalyzes the citrullination/deimination of arginine residues of proteins such as histones, thereby playing a key role in histone code and regulation of stem cell maintenance. Citrullinates histone...
- Gene Name
- PADI4
- Uniprot ID
- Q9UM07
- Uniprot Name
- Protein-arginine deiminase type-4
- Molecular Weight
- 74078.65 Da
References
- Wang Y, Wysocka J, Sayegh J, Lee YH, Perlin JR, Leonelli L, Sonbuchner LS, McDonald CH, Cook RG, Dou Y, Roeder RG, Clarke S, Stallcup MR, Allis CD, Coonrod SA: Human PAD4 regulates histone arginine methylation levels via demethylimination. Science. 2004 Oct 8;306(5694):279-83. Epub 2004 Sep 2. [Article]
- Wysocka J, Allis CD, Coonrod S: Histone arginine methylation and its dynamic regulation. Front Biosci. 2006 Jan 1;11:344-55. [Article]
- Yamamoto K, Yamada R: Genome-wide single nucleotide polymorphism analyses of rheumatoid arthritis. J Autoimmun. 2005;25 Suppl:12-5. Epub 2005 Nov 2. [Article]
- Chang X, Han J: Expression of peptidylarginine deiminase type 4 (PAD4) in various tumors. Mol Carcinog. 2006 Mar;45(3):183-96. [Article]
- Okazaki Y, Suzuki A, Sawada T, Ohtake-Yamanaka M, Inoue T, Hasebe T, Yamada R, Yamamoto K: Identification of citrullinated eukaryotic translation initiation factor 4G1 as novel autoantigen in rheumatoid arthritis. Biochem Biophys Res Commun. 2006 Mar 3;341(1):94-100. Epub 2006 Jan 6. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- No
- Actions
- Product of
- Curator comments
- Literature referenced performed experimentation of the drug on the target in mice.
- General Function
- Protein-arginine deiminase activity
- Specific Function
- Catalyzes the deimination of arginine residues of proteins. May be involved in cytoskeletal reorganization in the egg and early embryo (By similarity).
- Gene Name
- PADI6
- Uniprot ID
- Q6TGC4
- Uniprot Name
- Protein-arginine deiminase type-6
- Molecular Weight
- 77726.735 Da
References
- Snow AJ, Puri P, Acker-Palmer A, Bouwmeester T, Vijayaraghavan S, Kline D: Phosphorylation-dependent interaction of tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein (YWHA) with PADI6 following oocyte maturation in mice. Biol Reprod. 2008 Aug;79(2):337-47. doi: 10.1095/biolreprod.108.069328. Epub 2008 May 7. [Article]
- Esposito G, Vitale AM, Leijten FP, Strik AM, Koonen-Reemst AM, Yurttas P, Robben TJ, Coonrod S, Gossen JA: Peptidylarginine deiminase (PAD) 6 is essential for oocyte cytoskeletal sheet formation and female fertility. Mol Cell Endocrinol. 2007 Jul 15;273(1-2):25-31. doi: 10.1016/j.mce.2007.05.005. Epub 2007 May 17. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Protein-arginine deiminase activity
- Specific Function
- Catalyzes the deimination of arginine residues of proteins.
- Gene Name
- PADI1
- Uniprot ID
- Q9ULC6
- Uniprot Name
- Protein-arginine deiminase type-1
- Molecular Weight
- 74664.97 Da
References
- Iida A, Nakamura Y: Identification of 45 novel SNPs in the 83-kb region containing peptidylarginine deiminase types 1 and 3 loci on chromosomal band 1p36.13. J Hum Genet. 2004;49(7):387-90. Epub 2004 May 19. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Protein-arginine deiminase activity
- Specific Function
- Catalyzes the deimination of arginine residues of proteins.
- Gene Name
- PADI3
- Uniprot ID
- Q9ULW8
- Uniprot Name
- Protein-arginine deiminase type-3
- Molecular Weight
- 74742.705 Da
References
- Dong S, Kanno T, Yamaki A, Kojima T, Shiraiwa M, Kawada A, Mechin MC, Chavanas S, Serre G, Simon M, Takahara H: NF-Y and Sp1/Sp3 are involved in the transcriptional regulation of the peptidylarginine deiminase type III gene (PADI3) in human keratinocytes. Biochem J. 2006 Aug 1;397(3):449-59. [Article]
- Iida A, Nakamura Y: Identification of 45 novel SNPs in the 83-kb region containing peptidylarginine deiminase types 1 and 3 loci on chromosomal band 1p36.13. J Hum Genet. 2004;49(7):387-90. Epub 2004 May 19. [Article]
- Kanno T, Kawada A, Yamanouchi J, Yosida-Noro C, Yoshiki A, Shiraiwa M, Kusakabe M, Manabe M, Tezuka T, Takahara H: Human peptidylarginine deiminase type III: molecular cloning and nucleotide sequence of the cDNA, properties of the recombinant enzyme, and immunohistochemical localization in human skin. J Invest Dermatol. 2000 Nov;115(5):813-23. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Protein-arginine deiminase activity
- Specific Function
- Catalyzes the deimination of arginine residues of proteins.
- Gene Name
- PADI2
- Uniprot ID
- Q9Y2J8
- Uniprot Name
- Protein-arginine deiminase type-2
- Molecular Weight
- 75563.35 Da
References
- Dong S, Kojima T, Shiraiwa M, Mechin MC, Chavanas S, Serre G, Simon M, Kawada A, Takahara H: Regulation of the expression of peptidylarginine deiminase type II gene (PADI2) in human keratinocytes involves Sp1 and Sp3 transcription factors. J Invest Dermatol. 2005 May;124(5):1026-33. [Article]
Transporters
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- Curator comments
- Substrate profile was investigated in vitro using HEK293 cells, where the reported Km value was 238 ± 13 μM.
- General Function
- Sodium-independent organic anion transmembrane transporter activity
- Specific Function
- Involved in the renal elimination of endogenous and exogenous organic anions. Functions as organic anion exchanger when the uptake of one molecule of organic anion is coupled with an efflux of one ...
- Gene Name
- SLC22A6
- Uniprot ID
- Q4U2R8
- Uniprot Name
- Solute carrier family 22 member 6
- Molecular Weight
- 61815.78 Da
References
- VanWert AL, Gionfriddo MR, Sweet DH: Organic anion transporters: discovery, pharmacology, regulation and roles in pathophysiology. Biopharm Drug Dispos. 2010 Jan;31(1):1-71. doi: 10.1002/bdd.693. [Article]
Drug created at June 13, 2005 13:24 / Updated at February 13, 2024 02:57