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Identification
NameL-Citrulline
Accession NumberDB00155  (NUTR00021)
TypeSmall Molecule
GroupsApproved, Nutraceutical
Description

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.

Structure
Thumb
Synonyms
SynonymLanguageCode
(S)-2-Amino-5-ureidopentanoic acidNot AvailableNot Available
2-Amino-5-ureidovaleric acidNot AvailableNot Available
alpha-amino-delta-Ureidovaleric acidNot AvailableNot Available
CitNot AvailableNot Available
CitrullineNot AvailableNot Available
delta-UreidonorvalineNot AvailableNot Available
L-2-Amino-5-ureidovaleric acidNot AvailableNot Available
L-CitrullineNot AvailableNot Available
N(5)-(Aminocarbonyl)-L-ornithineNot AvailableNot Available
N(delta)-CarbamylornithineNot AvailableNot Available
N5-(Aminocarbonyl)ornithineNot AvailableNot Available
N5-Carbamoyl-L-ornithineNot AvailableNot Available
N5-carbamoylornithineNot AvailableNot Available
α-amino-δ-ureidovaleric acidNot AvailableNot Available
δ-ureidonorvalineNot AvailableNot Available
SaltsNot Available
Brand namesNot Available
Brand mixturesNot Available
Categories
CAS number372-75-8
WeightAverage: 175.1857
Monoisotopic: 175.095691297
Chemical FormulaC6H13N3O3
InChI KeyRHGKLRLOHDJJDR-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
Mass SpecNot Available
Taxonomy
KingdomOrganic Compounds
SuperclassOrganic Acids and Derivatives
ClassCarboxylic Acids and Derivatives
SubclassAmino Acids, Peptides, and Analogues
Direct parentAlpha Amino Acids and Derivatives
Alternative parentsAmino Fatty Acids; Enolates; Polyamines; Carboxylic Acids; Monoalkylamines
Substituentscarboxylic acid; enolate; polyamine; primary amine; amine; primary aliphatic amine; organonitrogen compound
Classification descriptionThis compound belongs to the alpha amino acids and derivatives. These are amino acids in which the amino group is attached to the carbon atom immediately adjacent to the carboxylate group (alpha carbon), or a derivative thereof.
Pharmacology
IndicationUsed for nutritional supplementation, also for treating dietary shortage or imbalance.
PharmacodynamicsA 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 actionL-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.
AbsorptionNot Available
Volume of distributionNot Available
Protein bindingNot Available
Metabolism
Route of eliminationNot Available
Half lifeNot Available
ClearanceNot Available
ToxicityNot Available
Affected organisms
  • Humans and other mammals
Pathways
PathwayCategorySMPDB ID
Canavan DiseaseDiseaseSMP00175
HypoacetylaspartiaDiseaseSMP00192
Aspartate MetabolismMetabolicSMP00067
Hyperprolinemia Type IIDiseaseSMP00360
Urea CycleMetabolicSMP00059
Ornithine Transcarbamylase Deficiency (OTC Deficiency)DiseaseSMP00205
Hyperprolinemia Type IDiseaseSMP00361
Creatine deficiency, guanidinoacetate methyltransferase deficiencyDiseaseSMP00504
Prolinemia Type IIDiseaseSMP00208
ArgininemiaDiseaseSMP00357
Hyperornithinemia with gyrate atrophy (HOGA)DiseaseSMP00505
Arginine and Proline MetabolismMetabolicSMP00020
Arginine: Glycine Amidinotransferase Deficiency (AGAT Deficiency)DiseaseSMP00362
Ornithine Aminotransferase Deficiency (OAT Deficiency)DiseaseSMP00363
Citrullinemia Type IDiseaseSMP00001
L-arginine:glycine amidinotransferase deficiencyDiseaseSMP00507
Prolidase Deficiency (PD)DiseaseSMP00207
Guanidinoacetate Methyltransferase Deficiency (GAMT Deficiency)DiseaseSMP00188
Argininosuccinic AciduriaDiseaseSMP00003
Carbamoyl Phosphate Synthetase DeficiencyDiseaseSMP00002
Hyperornithinemia-hyperammonemia-homocitrullinuria [HHH-syndrome]DiseaseSMP00506
SNP Mediated EffectsNot Available
SNP Mediated Adverse Drug ReactionsNot Available
ADMET
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 substrate Non-inhibitor 0.9149
CYP450 2D6 substrate Non-inhibitor 0.97
CYP450 2C19 substrate Non-inhibitor 0.9018
CYP450 3A4 substrate 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
Pharmacoeconomics
ManufacturersNot Available
Packagers
Dosage formsNot Available
Prices
Unit descriptionCostUnit
L-citrulline powder1.01USDg
DrugBank does not sell nor buy drugs. Pricing information is supplied for informational purposes only.
PatentsNot Available
Properties
Statesolid
Experimental Properties
PropertyValueSource
melting point235.5 °CPhysProp
water solubility200 g/L (at 20 °C)Not Available
logP-3.19SANGSTER (1994)
pKa2.43 (at 25 °C)KORTUM,G ET AL (1961)
Predicted Properties
PropertyValueSource
Water Solubility21.8ALOGPS
logP-3.3ALOGPS
logP-3.9ChemAxon
logS-0.9ALOGPS
pKa (Strongest Acidic)2.27ChemAxon
pKa (Strongest Basic)9.23ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count4ChemAxon
Hydrogen Donor Count4ChemAxon
Polar Surface Area118.44 Å2ChemAxon
Rotatable Bond Count5ChemAxon
Refractivity41.33 m3·mol-1ChemAxon
Polarizability17.35 Å3ChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterNoChemAxon
Veber's RuleNoChemAxon
MDDR-like RuleNoChemAxon
Spectra
SpectraGC-MSMS/MSLC-MS1D NMR2D NMR
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 ReferenceNot Available
External Links
ResourceLink
KEGG CompoundC00327
PubChem Compound9750
PubChem Substance46506583
ChemSpider9367
ChEBI16349
ChEMBLCHEMBL444814
PharmGKBPA164747225
IUPHAR722
Guide to Pharmacology722
HETCIR
ATC CodesNot Available
AHFS CodesNot Available
PDB Entries
FDA labelNot Available
MSDSshow(72.8 KB)
Interactions
Drug InteractionsNot Available
Food InteractionsNot Available

Targets

1. Argininosuccinate synthase

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Argininosuccinate synthase P00966 Details

References:

  1. 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. Pubmed
  2. 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. Pubmed
  3. 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. Pubmed
  4. 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. Pubmed
  5. 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. Pubmed

2. N(G),N(G)-dimethylarginine dimethylaminohydrolase 2

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
N(G),N(G)-dimethylarginine dimethylaminohydrolase 2 O95865 Details

References:

  1. 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. Pubmed
  2. Tain YL, Baylis C: Determination of dimethylarginine dimethylaminohydrolase activity in the kidney. Kidney Int. 2007 Oct;72(7):886-9. Epub 2007 Jul 25. Pubmed

3. Argininosuccinate synthetase, isoform CRA_a

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Argininosuccinate synthetase, isoform CRA_a Q5T6L4 Details

References:

  1. Husson A, Brasse-Lagnel C, Fairand A, Renouf S, Lavoinne A: Argininosuccinate synthetase from the urea cycle to the citrulline-NO cycle. Eur J Biochem. 2003 May;270(9):1887-99. Pubmed
  2. Hammermann R, Bliesener N, Mossner J, Klasen S, Wiesinger H, Wessler I, Racke K: Inability of rat alveolar macrophages to recycle L-citrulline to L-arginine despite induction of argininosuccinate synthetase mRNA and protein, and inhibition of nitric oxide synthesis by exogenous L-citrulline. Naunyn Schmiedebergs Arch Pharmacol. 1998 Dec;358(6):601-7. Pubmed
  3. Van Geldre LA, Timmermans JP, Lefebvre RA: L-citrulline recycling by argininosuccinate synthetase and lyase in rat gastric fundus. Eur J Pharmacol. 2002 Nov 29;455(2-3):149-60. Pubmed
  4. Zandvliet MM, Rothuizen J: Transient hyperammonemia due to urea cycle enzyme deficiency in Irish wolfhounds. J Vet Intern Med. 2007 Mar-Apr;21(2):215-8. Pubmed
  5. Takahashi H, Kagawa T, Kobayashi K, Hirabayashi H, Yui M, Begum L, Mine T, Takagi S, Saheki T, Shinohara Y: A case of adult-onset type II citrullinemia—deterioration of clinical course after infusion of hyperosmotic and high sugar solutions. Med Sci Monit. 2006 Feb;12(2):CS13-5. Epub 2006 Jan 26. Pubmed

4. N(G),N(G)-dimethylarginine dimethylaminohydrolase 1

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
N(G),N(G)-dimethylarginine dimethylaminohydrolase 1 O94760 Details

References:

  1. 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. Pubmed
  2. 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. Pubmed
  3. 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. Pubmed

5. Ornithine carbamoyltransferase, mitochondrial

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Ornithine carbamoyltransferase, mitochondrial P00480 Details

References:

  1. 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. Pubmed
  2. 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. Pubmed

6. Nitric oxide synthase, brain

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Nitric oxide synthase, brain P29475 Details

References:

  1. 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 (Tokyo). 1999 Oct;126(4):756-61. Pubmed
  2. 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. Pubmed
  3. 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. Pubmed
  4. 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. Pubmed
  5. 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. Pubmed

7. Nitric oxide synthase, inducible

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Nitric oxide synthase, inducible P35228 Details

References:

  1. 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. Pubmed
  2. 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. Pubmed
  3. 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. Pubmed
  4. 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. Pubmed
  5. 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. Pubmed

8. Nitric oxide synthase, endothelial

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Nitric oxide synthase, endothelial P29474 Details

References:

  1. Hayakawa H, Raij L: Relationship between hypercholesterolaemia, endothelial dysfunction and hypertension. J Hypertens. 1999 May;17(5):611-9. Pubmed
  2. 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. Pubmed
  3. 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. Pubmed
  4. 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. Pubmed
  5. 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. Pubmed

9. Protein-arginine deiminase type-6

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Protein-arginine deiminase type-6 Q6TGC4 Details

References:

  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed

10. Protein-arginine deiminase type-1

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Protein-arginine deiminase type-1 Q9ULC6 Details

References:

  1. 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. Pubmed

11. Protein-arginine deiminase type-3

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Protein-arginine deiminase type-3 Q9ULW8 Details

References:

  1. 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. Pubmed
  2. 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. Pubmed
  3. 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. Pubmed

12. Protein-arginine deiminase type-2

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Protein-arginine deiminase type-2 Q9Y2J8 Details

References:

  1. 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. Pubmed

13. Protein-arginine deiminase type-4

Kind: protein

Organism: Human

Pharmacological action: unknown

Components

Name UniProt ID Details
Protein-arginine deiminase type-4 Q9UM07 Details

References:

  1. 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. Pubmed
  2. Wysocka J, Allis CD, Coonrod S: Histone arginine methylation and its dynamic regulation. Front Biosci. 2006 Jan 1;11:344-55. Pubmed
  3. Yamamoto K, Yamada R: Genome-wide single nucleotide polymorphism analyses of rheumatoid arthritis. J Autoimmun. 2005;25 Suppl:12-5. Epub 2005 Nov 2. Pubmed
  4. Chang X, Han J: Expression of peptidylarginine deiminase type 4 (PAD4) in various tumors. Mol Carcinog. 2006 Mar;45(3):183-96. Pubmed
  5. 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. Pubmed

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Drug created on June 13, 2005 07:24 / Updated on September 24, 2013 13:34