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Showing drug card for Meclofenamic acid (DB00939)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-23 18:07:06
Primary Accession Number DB00939
Secondary Accession Number
  • APRD01090
Name Meclofenamic acid
Drug Type
  • Approved
  • Small Molecule
Description A non-steroidal anti-inflammatory agent with antipyretic and antigranulation activities. It also inhibits prostaglandin biosynthesis. [PubChem]
Synonyms
  1. Acide meclofenamique [INN-French]
  2. Acido meclofenamico [INN-Spanish]
  3. Acidum meclofenamicum [INN-Latin]
  4. Meclofenamate
  5. Meclomen (free acid)
  6. Meclophenamic acid
Brand Names
  1. Arquel
Brand Mixtures Not Available
Chemical IUPAC Name 2-[(2,6-dichloro-3-methylphenyl)amino]benzoic acid
Chemical Formula C14H11Cl2NO2
Chemical Structure Structure
CAS Registry Number 644-62-2
InChI Identifier InChI=1/C14H11Cl2NO2/c1-8-6-7-10(15)13(12(8)16)17-11-5-3-2-4-9(11)14(18)19/h2-7,17H,1H3,(H,18,19)/f/h18H
InChI Key SBDNJUWAMKYJOX-GPQMBLKYCQ
KEGG Drug D02341 Link Image
KEGG Compound C02996 Link Image
PubChem Compound 4037 Link Image
PubChem Substance 7849400 Link Image
ChEBI ID Not Available
PharmGKB ID PA450341 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] Not Available
RxList Link http://www.rxlist.com/cgi/generic/meclofen.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Meclofenamic_acid Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 296.1490
Monoisotopic Molecular Weight 295.0167
State Solid
Melting Point 257 oC
Experimental Water Solubility 30 mg/L Source: PhysProp
Predicted Water Solubility 3.66e-03 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 5 Source: PhysProp
Predicted LogP 5.11 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -4.91 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point Not Available
Mass Spectrum Not Available
MOL File Show Link Image | Download Link Image
SDF File Show Link Image | Download Link Image
PDB File Show Link Image | Download Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Isomeric SMILES CC1=C(Cl)C(NC2=CC=CC=C2C(O)=O)=C(Cl)C=C1
Canonical SMILES CC1=C(Cl)C(NC2=CC=CC=C2C(O)=O)=C(Cl)C=C1
Drug Category
  • Anti-Inflammatory Agents, Non-Steroidal
  • Cyclooxygenase Inhibitors
ATC Codes
AHFS Codes Not Available
Indication For the relief of mild to moderate pain, for the treatment of primary dysmenorrhea and for the treatment of idiopathic heavy menstrual blood loss. Also for relief of the signs and symptoms of acute and chronic rheumatoid arthritis and osteoarthritis.
Pharmacology Meclofenamic acid is a nonsteroidal agent which has demonstrated anti-inflammatory, analgesic, and antipyretic activity in laboratory animals.
Mechanism of Action The mode of action, like that of other nonsteroidal anti-inflammatory agents, is not known. Therapeutic action does not result from pituitary-adrenal stimulation. In animal studies, meclofenamic acid was found to inhibit prostaglandin synthesis and to compete for binding at the prostaglandin receptor site. In vitro meclofenamic acid was found to be an inhibitor of human leukocyte 5-lipoxygenase activity. These properties may be responsible for the anti-inflammatory action of meclofenamic acid. There is no evidence that meclofenamic acid alters the course of the underlying disease.
Absorption Rapidly absorbed in man following single and multiple oral doses with peak plasma concentrations occurring in 0.5 to 2 hours. The concomitant administration of antacids (aluminum and magnesium hydroxides) does not interfere with absorption of meclofenamic acid. Unlike most NSAIDs, which when administered with food have a decrease in rate but not in extent of absorption, meclofenamic acid is decreased in both. It has been reported that following the administration of meclofenamic acid capsules one-half hour after a meal, the average extent of bioavailability decreased by 26%, the average peak concentration (Cmax) decreased fourfold and the time to Cmax was delayed by 3 hours.
Toxicity After a massive overdose, CNS stimulation may be manifested by irrational behavior, marked agitation and generalized seizures. Following this phase, renal toxicity (falling urine output, rising creatinine, abnormal urinary cellular elements) may be noted with possible oliguria or anuria and azotemia. A 24 year-old male was anuric for approximately one week after ingesting an overdose of 6 to 7 grams of meclofenamate sodium. Spontaneous diuresis and recovery subsequently occurred.
Protein Binding Greater than 99% bound to plasma proteins over a wide drug concentration range.
Biotransformation Hepatic. Meclofenamic acid is extensively metabolized to an active metabolite (Metabolite I; 3-hydroxymethyl metabolite of meclofenamic acid) and at least six other less well characterized minor metabolites. Only Metabolite I has been shown in vitro to inhibit cyclooxygenase activity with approximately one fifth the activity of meclofenamic acid.
Half Life In a study in 10 healthy subjects following a single oral dose the apparent elimination half-life ranged from 0.8 to 5.3 hours. Metabolite I (3-hydroxymethyl metabolite of meclofenamic acid) has a mean half-life of approximately 15 hours.
Dosage Forms
Form Route
Capsule Oral
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions Not Available
Food Interactions Not Available
Pathways Not Available
General References
  1. Wikipedia Link Image
  2. RxList Link Image
Organisms Affected
  • Humans and other mammals
Targets
  1. Prostaglandin G/H synthase 1
  2. Arachidonate 5-lipoxygenase
  3. Prostaglandin G/H synthase 2
Drug Target 1 [top]
Target 1 ID 20
Target 1 Name Prostaglandin G/H synthase 1
Target 1 Synonyms
  1. COX-1
  2. Cyclooxygenase- 1
  3. EC 1.14.99.1
  4. PGH synthase 1
  5. PGHS-1
  6. PHS 1
  7. Prostaglandin G/H synthase 1 precursor
  8. Prostaglandin H2 synthase 1
  9. Prostaglandin-endoperoxide synthase 1
Target 1 Gene Name PTGS1
Target 1 Protein Sequence >Prostaglandin G/H synthase 1 precursor 
MSRSLLLRFLLFLLLLPPLPVLLADPGAPTPVNPCCYYPCQHQGICVRFGLDRYQCDCTR
TGYSGPNCTIPGLWTWLRNSLRPSPSFTHFLLTHGRWFWEFVNATFIREMLMRLVLTVRS
NLIPSPPTYNSAHDYISWESFSNVSYYTRILPSVPKDCPTPMGTKGKKQLPDAQLLARRF
LLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTSGKMGPGFTKALGHGVDLGHIYGDNLERQ
YQLRLFKDGKLKYQVLDGEMYPPSVEEAPVLMHYPRGIPPQSQMAVGQEVFGLLPGLMLY
ATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSGYFLQLKF
DPELLFGVQFQYRNRIAMEFNHLYHWHPLMPDSFKVGSQEYSYEQFLFNTSMLVDYGVEA
LVDAFSRQIAGRIGGGRNMDHHILHVAVDVIRESREMRLQPFNEYRKRFGMKPYTSFQEL
VGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESMIEIGAPFSLKGLLGNPICS
PEYWKPSTFGGEVGFNIVKTATLKKLVCLNTKTCPYVSFRVPDASQDDGPAVERPSTEL
Target 1 Number of Residues 608
Target 1 Molecular Weight 68657
Target 1 Theoretical pI 7.39
Target 1 GO Classification
Function
antioxidant activity
peroxidase activity
Process
Not Available
Component
Not Available
Target 1 General Function Involved in peroxidase activity
Target 1 Specific Function May play an important role in regulating or promoting cell proliferation in some normal and neoplastically transformed cells
Target 1 Pathways
Name SMPDB Link KEGG Link
Prostaglandin and leukotriene metabolism map00590 Link Image
Target 1 Reactions
  • arachidonate + AH2 + 2 O2 = prostaglandin H2 + A + H2O
Target 1 Pfam Domain Function
Target 1 Signals
  • 1-23
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 387018 Link Image
Target 1 UniProtKB/Swiss-Prot ID P23219 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name PGH1_HUMAN Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location
  • Microsome
  • microsomal membrane
  • peripheral membrane protein
Target 1 Gene Sequence >1800 bp 
ATGAGCCGGAGTCTCTTGCTCCGGTTCTTGCTGTTGCTGCTCCTGCTCCCGCCGCTCCCC
GTCCTGCTCGCGGACCCAGGGGCGCCCACGCCAGTGAATCCCTGTTGTTACTATCCATGC
CAGCACCAGGGCATCTGTGTCCGCTTCGGCCTTGACCGCTACCAGTGTGACTGCACCCGC
ACGGGCTATTCCGGCCCCAACTGCACCATCCCTGGCCTGTGGACCTGGCTCCGGAATTCA
CTGCGGCCCAGCCCCTCTTTCACCCACTTCCTGCTCACTCACGGGCGCTGGTTCTGGGAG
TTTGTCAATGCCACCTTCATCCGAGAGATGCTCATGCTCCTGGTACTCACAGTGCGCTCC
AACCTTATCCCCAGTCCCCCCACCTACAACTCTGCACATGACTACATCAGCTGGGAGTCT
TTCTCCAACGTGAGCTATTACACTCGTATTCTGCCCTCTGTGCCTAAAGATTGCCCCACA
CCCATGGGAACCAAAGGGAAGAAGCAGTTGCCAGATGCCCAGCTCCTGGCCCGCCGCTTC
CTGCTCAGGAGGAAGTTCATACCTGACCCCCAAGGCACCAACCTCATGTTTGCCTTCTTT
GCACAACACTTCACCCACCAGTTCTTCAAAACTTCTGGCAAGATGGGTCCTGGCTTCACC
AAGGCCTTGGGCCATGGGGTAGACCTCGGCCACATTTATGGAGACAATCTGGAGCGTCAG
TATCAACTGCGGCTCTTTAAGGATGGGAAACTCAAGTACCAGGTGCTGGATGGAGAAATG
TACCCGCCCTCGGTAGAAGAGGCGCCTGTGTTGATGCACTACCCCCGAGGCATCCCGCCC
CAGAGCCAGATGGCTGTGGGCCAGGAGGTGTTTGGGCTGCTTCCTGGGCTCATGCTGTAT
GCCACGCTCTGGCTACGTGAGCACAACCGTGTGTGTGACCTGCTGAAGGCTGAGCACCCC
ACCTGGGGCGATGAGCAGCTTTTCCAGACGACCCGCCTCATCCTCATAGGGGAGACCATC
AAGATTGTCATCGAGGAGTACGTGCAGCAGCTGAGTGGCTATTTCCTGCAGCTGAAATTT
GACCCAGAGCTGCTGTTCGGTGTCCAGTTCCAATACCGCAACCGCATTGCCACGGAGTTC
AACCATCTCTACCACTGGCACCCCCTCATGCCTGACTCCTTCAAGGTGGGCTCCCAGGAG
TACAGCTACGAGCAGTTCTTGTTCAACACCTCCATGTTGGTGGACTATGGGGTTGAGGCC
CTGGTGGATGCCTTCTCTCGCCAGATTGCTGGCCGGATCGGTGGGGGCAGGAACATGGAC
CACCACATCCTGCATGTGGCTGTGGATGTCATCAGGGAGTCTCGGGAGATGCGGCTGCAG
CCCTTCAATGAGTACCGCAAGAGGTTTGGCATGAAACCCTACACCTCCTTCCAGGAGCTC
GTAGGAGAGAAGGAGATGGCAGCAGAGTTGGAGGAATTGTATGGAGACATTGATGCGTTG
GAGTTCTACCCTGGACTGCTTCTTGAAAAGTGCCATCCAAACTCTATCTTTGGGGAGAGT
ATGATAGAGATTGGGGCTCCCTTTTCCCTCAAGGGTCTCCTAGGGAATCCCATCTGTTCT
CCGGAGTACTGGAAGCCGAGCACATTTGGCGGCGAGGTGGGCTTTAACATTGTCAAGACG
GCCACACTGAAGAAGCTGGTCTGCCTCAACACCAAGACCTGTCCCTACGTTTCCTTCCGT
GTGCCGGATGCCAGTCAGGATGATGGGCCTGCTGTGGAGCGACCATCCACAGAGCTCTGA
Target 1 GenBank Gene ID
Target 1 GeneCard ID PTGS1 Link Image
Target 1 GenAtlas ID PTGS1 Link Image
Target 1 HGNC ID HGNC:9604 Link Image
Target 1 Chromosome Location 9
Target 1 Locus 9q32-q33.3
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Diaz A, Reginato AM, Jimenez SA: Alternative splicing of human prostaglandin G/H synthase mRNA and evidence of differential regulation of the resulting transcripts by transforming growth factor beta 1, interleukin 1 beta, and tumor necrosis factor alpha. J Biol Chem. 1992 May 25;267(15):10816-22. [PubMed Link Image]
  2. Takahashi Y, Ueda N, Yoshimoto T, Yamamoto S, Yokoyama C, Miyata A, Tanabe T, Fuse I, Hattori A, Shibata A: Immunoaffinity purification and cDNA cloning of human platelet prostaglandin endoperoxide synthase (cyclooxygenase). Biochem Biophys Res Commun. 1992 Jan 31;182(2):433-8. [PubMed Link Image]
  3. Funk CD, Funk LB, Kennedy ME, Pong AS, Fitzgerald GA: Human platelet/erythroleukemia cell prostaglandin G/H synthase: cDNA cloning, expression, and gene chromosomal assignment. FASEB J. 1991 Jun;5(9):2304-12. [PubMed Link Image]
  4. Yokoyama C, Tanabe T: Cloning of human gene encoding prostaglandin endoperoxide synthase and primary structure of the enzyme. Biochem Biophys Res Commun. 1989 Dec 15;165(2):888-94. [PubMed Link Image]
Target 1 Drug References
  1. Kalgutkar AS, Crews BC, Rowlinson SW, Marnett AB, Kozak KR, Remmel RP, Marnett LJ: Biochemically based design of cyclooxygenase-2 (COX-2) inhibitors: facile conversion of nonsteroidal antiinflammatory drugs to potent and highly selective COX-2 inhibitors. Proc Natl Acad Sci U S A. 2000 Jan 18;97(2):925-30. [PubMed Link Image]
  2. Shiels IA, Whitehouse MW: Lyprinol: anti-inflammatory and uterine-relaxant activities in rats, with special reference to a model for dysmenorrhoea. Allerg Immunol (Paris). 2000 Sep;32(7):279-83. [PubMed Link Image]
  3. Perez-Vizcaino F, Lopez-Lopez JG, Santiago R, Cogolludo A, Zaragoza-Arnaez F, Moreno L, Alonso MJ, Salaices M, Tamargo J: Postnatal maturation in nitric oxide-induced pulmonary artery relaxation involving cyclooxygenase-1 activity. Am J Physiol Lung Cell Mol Physiol. 2002 Oct;283(4):L839-48. [PubMed Link Image]
  4. Wilson JE, Chandrasekharan NV, Westover KD, Eager KB, Simmons DL: Determination of expression of cyclooxygenase-1 and -2 isozymes in canine tissues and their differential sensitivity to nonsteroidal anti-inflammatory drugs. Am J Vet Res. 2004 Jun;65(6):810-8. [PubMed Link Image]
  5. Meade EA, Smith WL, DeWitt DL: Differential inhibition of prostaglandin endoperoxide synthase (cyclooxygenase) isozymes by aspirin and other non-steroidal anti-inflammatory drugs. J Biol Chem. 1993 Mar 25;268(9):6610-4. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 275
Target 2 Name Arachidonate 5-lipoxygenase
Target 2 Synonyms
  1. 5-LO
  2. 5-lipoxygenase
  3. EC 1.13.11.34
Target 2 Gene Name ALOX5
Target 2 Protein Sequence >Arachidonate 5-lipoxygenase 
PSYTVTVATGSQWFAGTDDYIYLSLVGSAGCSEKHLLDKPFYNDFERGAVDSYDVTVDEE
LGEIQLVRIEKRKYWLNDDWYLKYITLKTPHGDYIEFPCYRWITGDVEVVLRDGRAKLAR
DDQIHILKQHRRKELETRQKQYRWMEWNPGFPLSIDAKCHKDLPRDIQFDSEKGVDFVLN
YSKAMENLFINRFMHMFQSSWNDFADFEKIFVKISNTISERVMNHWQEDLMFGYQFLNGC
NPVLIRRCTELPEKLPVTTEMVECSLERQLSLEQEVQQGNIFIVDFELLDGIDANKTDPC
TLQFLAAPICLLYKNLANKIVPIAIQLNQIPGDENPIFLPSDAKYDWLLAKIWVRSSDFH
VHQTITHLLRTHLVSEVFGIAMYRQLPAVHPIFKLLVAHVRFTIAINTKAREQLICECGL
FDKANATGGGGHVQMVQRAMKDLTYASLCFPEAIKARGMESKEDIPYYFYRDDGLLVWEA
IRTFTAEVVDIYYEGDQVVEEDPELQDFVNDVYVYGMRGRKSSGFPKSVKSREQLSEYLT
VVIFTASAQHAAVNFGQYDWCSWIPNAPPTMRAPPPTAKGVVTIEQIVDTLPDRGRSCWH
LGAVWALSQFQENELFLGMYPEEHFIEKPVKEAMARFRKNLEAIVSVIAERNKKKQLPYY
YLSPDRIPNSVAI
Target 2 Number of Residues 684
Target 2 Molecular Weight 77853
Target 2 Theoretical pI 5.54
Target 2 GO Classification
Function
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on single donors with incorporation of molecular oxygen
oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
lipoxygenase activity
binding
ion binding
cation binding
transition metal ion binding
iron ion binding
Process
organic acid metabolism
carboxylic acid metabolism
fatty acid metabolism
icosanoid metabolism
leukotriene metabolism
physiological process
metabolism
cellular metabolism
generation of precursor metabolites and energy
electron transport
Component
Not Available
Target 2 General Function Involved in oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
Target 2 Specific Function Not Available
Target 2 Pathways
Name SMPDB Link KEGG Link
Prostaglandin and leukotriene metabolism map00590 Link Image
Target 2 Reactions
  • arachidonate + O2 = (6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyicosa-6,8,11,14-tetraenoate
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 187193 Link Image
Target 2 UniProtKB/Swiss-Prot ID P09917 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name LOX5_HUMAN Link Image
Target 2 PDB ID Not Available
Target 2 Cellular Location
  • Cytoplasm
Target 2 Gene Sequence >2025 bp 
ATGCCCTCCTACACGGTCACCGTGGCCACTGGCAGCCAGTGGTTCGCCGGCACTGACGAC
TACATCTACCTCAGCCTCGTGGGCTCGGCGGGCTGCAGCGAGAAGCACCTGCTGGACAAG
CCCTTCTACAACGACTTCGAGCGTGGCGCGGTGGATTCATACGACGTGACTGTGGACGAG
GAACTGGGCGAGATCCAGCTGGTCAGAATCGAGAAGCGCAAGTACTGGCTGAATGACGAC
TGGTACCTGAAGTACATCACGCTGAAGACGCCCCACGGGGACTACATCGAGTTCCCCTGC
TACCGCTGGATCACCGGCGATGTCGAGGTTGTCCTGAGGGATGGACGCGCAAAGTTGGCC
CGAGATGACCAAATTCACATTCTCAAGCAACACCGACGTAAAGAACTGGAAACACGGCAA
AAACAATATCGATGGATGGAGTGGAACCCTGGCTTCCCCTTGAGCATCGATGCCAAATGC
CACAAGGATTTACCCCGTGATATCCAGTTTGATAGTGAAAAAGGAGTGGACTTTGTTCTG
AATTACTCCAAAGCGATGGAGAACCTGTTCATCAACCGCTTCATGCACATGTTCCAGTCT
TCTTGGAATGACTTCGCCGACTTTGAGAAAATCTTTGTCAAGATCAGCAACACTATTTCT
GAGCGGGTCATGAATCACTGGCAGGAAGACCTGATGTTTGGCTACCAGTTCCTGAATGGC
TGCAACCCTGTGTTGATCCGGCGCTGCACAGAGCTGCCCGAGAAGCTCCCGGTGACCACG
GAGATGGTAGAGTGCAGCCTGGAGCGGCAGCTCAGCTTGGAGCAGGAGGTCCAGCAAGGG
AACATTTTCATCGTGGACTTTGAGCTGCTGGATGGCATCGATGCCAACAAAACAGACCCC
TGCACACTCCAGTTCCTGGCCGCTCCCATCTGCTTGCTGTATAAGAACCTGGCCAACAAG
ATTGTCCCCATTGCCATCCAGCTCAACCAAATCCCGGGAGATGAGAACCCTATTTTCCTC
CCTTCGGATGCAAAATACGACTGGCTTTTGGCCAAAATCTGGGTGCGTTCCAGTGACTTC
CACGTCCACCAGACCATCACCCACCTTCTGCGAACACATCTGGTGTCTGAGGTTTTTGGC
ATTGCAATGTACCGCCAGCTGCCTGCTGTGCACCCCATTTTCAAGCTGCTGGTGGCACAC
GTGAGATTCACCATTGCAATCAACACCAAGGCCCGTGAGCAGCTCATCTGCGAGTGTGGC
CTCTTTGACAAGGCCAACGCCACAGGGGGCGGTGGGCACGTGCAGATGGTGCAGAGGGCC
ATGAAGGACCTGACCTATGCCTCCCTGTGCTTTCCCGAGGCCATCAAGGCCCGGGGCATG
GAGAGCAAAGAAGACATCCCCTACTACTTCTACCGGGACGACGGGCTCCTGGTGTGGGAA
GCCATCAGGACGTTCACGGCCGAGGTGGTAGACATCTACTACGAGGGCGACCAGGTGGTG
GAGGAGGACCCGGAGCTGCAGGACTTCGTGAACGATGTCTACGTGTACGGCATGCGGGGC
CGCAAGTCCTCAGGCTTCCCCAAGTCGGTCAAGAGCCGGGAGCAGCTGTCGGAGTACCTG
ACCGTGGTGATCTTCACCGCCTCCGCCCAGCACGCCGCGGTCAACTTCGGCCAGTACGAC
TGGTGCTCCTGGATCCCCAATGCGCCCCCAACCATGCGAGCCCCGCCACCGACTGCCAAG
GGCGTGGTGACCATTGAGCAGATCGTGGACACGCTGCCCGACCGCGGCCGCTCCTGCTGG
CATCTGGGTGCAGTGTGGGCGCTGAGCCAGTTCCAGGAAAACGAGCTGTTCCTGGGCATG
TACCCAGAAGAGCATTTTATCGAGAAGCCTGTGAAGGAAGCCATGGCCCGATTCCGCAAG
AACCTCGAGGCCATTGTCAGCGTGATTGCTGAGCGCAACAAGAAGAAGCAGCTGCCATAT
TACTACTTGTCCCCAGACCGGATTCCGAACAGTGTGGCCATCTGA
Target 2 GenBank Gene ID
Target 2 GeneCard ID ALOX5 Link Image
Target 2 GenAtlas ID ALOX5 Link Image
Target 2 HGNC ID HGNC:435 Link Image
Target 2 Chromosome Location 10
Target 2 Locus 10q11.2
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Werz O, Szellas D, Steinhilber D, Radmark O: Arachidonic acid promotes phosphorylation of 5-lipoxygenase at Ser-271 by MAPK-activated protein kinase 2 (MK2). J Biol Chem. 2002 Apr 26;277(17):14793-800. Epub 2002 Feb 13. [PubMed Link Image]
  2. Ishii S, Noguchi M, Miyano M, Matsumoto T, Noma M: Mutagenesis studies on the amino acid residues involved in the iron-binding and the activity of human 5-lipoxygenase. Biochem Biophys Res Commun. 1992 Feb 14;182(3):1482-90. [PubMed Link Image]
  3. Nguyen T, Falgueyret JP, Abramovitz M, Riendeau D: Evaluation of the role of conserved His and Met residues among lipoxygenases by site-directed mutagenesis of recombinant human 5-lipoxygenase. J Biol Chem. 1991 Nov 15;266(32):22057-62. [PubMed Link Image]
  4. Hoshiko S, Radmark O, Samuelsson B: Characterization of the human 5-lipoxygenase gene promoter. Proc Natl Acad Sci U S A. 1990 Dec;87(23):9073-7. [PubMed Link Image]
  5. Matsumoto T, Funk CD, Radmark O, Hoog JO, Jornvall H, Samuelsson B: Molecular cloning and amino acid sequence of human 5-lipoxygenase. Adv Prostaglandin Thromboxane Leukot Res. 1989;19:466-9. [PubMed Link Image]
  6. Funk CD, Hoshiko S, Matsumoto T, Rdmark O, Samuelsson B: Characterization of the human 5-lipoxygenase gene. Proc Natl Acad Sci U S A. 1989 Apr;86(8):2587-91. [PubMed Link Image]
  7. Matsumoto T, Funk CD, Radmark O, Hoog JO, Jornvall H, Samuelsson B: Molecular cloning and amino acid sequence of human 5-lipoxygenase. Proc Natl Acad Sci U S A. 1988 Jan;85(1):26-30. [PubMed Link Image]
  8. Dixon RA, Jones RE, Diehl RE, Bennett CD, Kargman S, Rouzer CA: Cloning of the cDNA for human 5-lipoxygenase. Proc Natl Acad Sci U S A. 1988 Jan;85(2):416-20. [PubMed Link Image]
Target 2 Drug References
  1. Yu XY, Hubbard W, Spannhake EW: Inhibition of canine tracheal smooth muscle by mediators from cultured bronchial epithelial cells. Am J Physiol. 1992 Feb;262(2 Pt 1):L229-34. [PubMed Link Image]
  2. Boctor AM, Eickholt M, Pugsley TA: Meclofenamate sodium is an inhibitor of both the 5-lipoxygenase and cyclooxygenase pathways of the arachidonic acid cascade in vitro. Prostaglandins Leukot Med. 1986 Aug;23(2-3):229-38. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 290
Target 3 Name Prostaglandin G/H synthase 2
Target 3 Synonyms
  1. COX-2
  2. Cyclooxygenase- 2
  3. EC 1.14.99.1
  4. PGH synthase 2
  5. PGHS-2
  6. PHS II
  7. Prostaglandin G/H synthase 2 precursor
  8. Prostaglandin H2 synthase 2
  9. Prostaglandin-endoperoxide synthase 2
Target 3 Gene Name PTGS2
Target 3 Protein Sequence >Prostaglandin G/H synthase 2 precursor 
MLARALLLCAVLALSHTANPCCSHPCQNRGVCMSVGFDQYKCDCTRTGFYGENCSTPEFL
TRIKLFLKPTPNTVHYILTHFKGFWNVVNNIPFLRNAIMSYVLTSRSHLIDSPPTYNADY
GYKSWEAFSNLSYYTRALPPVPDDCPTPLGVKGKKQLPDSNEIVEKLLLRRKFIPDPQGS
NMMFAFFAQHFTHQFFKTDHKRGPAFTNGLGHGVDLNHIYGETLARQRKLRLFKDGKMKY
QIIDGEMYPPTVKDTQAEMIYPPQVPEHLRFAVGQEVFGLVPGLMMYATIWLREHNRVCD
VLKQEHPEWGDEQLFQTSRLILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNKQFQYQ
NRIAAEFNTLYHWHPLLPDTFQIHDQKYNYQQFIYNNSILLEHGITQFVESFTRQIAGRV
AGGRNVPPAVQKVSQASIDQSRQMKYQSFNEYRKRFMLKPYESFEELTGEKEMSAELEAL
YGDIDAVELYPALLVEKPRPDAIFGETMVEVGAPFSLKGLMGNVICSPAYWKPSTFGGEV
GFQIINTASIQSLICNNVKGCPFTSFSVPDPELIKTVTINASSSRSGLDDINPTVLLKER
STEL
Target 3 Number of Residues 614
Target 3 Molecular Weight 68997
Target 3 Theoretical pI 7.41
Target 3 GO Classification
Function
antioxidant activity
peroxidase activity
Process
Not Available
Component
Not Available
Target 3 General Function Involved in peroxidase activity
Target 3 Specific Function May have a role as a major mediator of inflammation and/or a role for prostanoid signaling in activity-dependent plasticity
Target 3 Pathways
Name SMPDB Link KEGG Link
Prostaglandin and leukotriene metabolism map00590 Link Image
Target 3 Reactions
  • arachidonate + AH2 + 2 O2 = prostaglandin H2 + A + H2O
Target 3 Pfam Domain Function
Target 3 Signals
  • 1-17
Target 3 Transmembrane Regions
  • None
Target 3 Essentiality Non-Essential
Target 3 GenBank ID Protein 291988 Link Image
Target 3 UniProtKB/Swiss-Prot ID P35354 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name PGH2_HUMAN Link Image
Target 3 PDB ID Not Available
Target 3 Cellular Location
  • Microsome
  • microsomal membrane
  • peripheral membrane protein
Target 3 Gene Sequence >1815 bp 
ATGCTCGCCCGCGCCCTGCTGCTGTGCGCGGTCCTGGCGCTCAGCCATACAGCAAATCCT
TGCTGTTCCCACCCATGTCAAAACCGAGGTGTATGTATGAGTGTGGGATTTGACCAGTAT
AAGTGCGATTGTACCCGGACAGGATTCTATGGAGAAAACTGCTCAACACCGGAATTTTTG
ACAAGAATAAAATTATTTCTGAAACCCACTCCAAACACAGTGCACTACATACTTACCCAC
TTCAAGGGATTTTGGAACGTTGTGAATAACATTCCCTTCCTTCGAAATGCAATTATGAGT
TATGTGTTGACATCCAGATCACATTTGATTGACAGTCCACCAACTTACAATGCTGACTAT
GGCTACAAAAGCTGGGAAGCCTTCTCTAACCTCTCCTATTATACTAGAGCCCTTCCTCCT
GTGCCTGATGATTGCCCGACTCCCTTGGGTGTCAAAGGTAAAAAGCAGCTTCCTGATTCA
AATGAGATTGTGGAAAAATTGCTTCTAAGAAGAAAGTTCATCCCTGATCCCCAGGGCTCA
AACATGATGTTTGCATTCTTTGCCCAGCACTTCACGCATCAGTTTTTCAAGACAGATCAT
AAGCGAGGGCCAGCTTTCACCAACGGGCTGGGCCATGGGGTGGACTTAAATCATATTTAC
GGTGAAACTCTGGCTAGACAGCGTAAACTGCGCCTTTTCAAGGATGGAAAAATGAAATAT
CAGATAATTGATGGAGAGATGTATCCTCCCACAGTCAAAGATACTCAGGCAGAGATGATC
TACCCTCCTCAAGTCCCTGAGCATCTACGGTTTGCTGTGGGGCAGGAGGTCTTTGGTCTG
GTGCCTGGTCTGATGATGTATGCCACAATCTGGCTGCGGGAACACAACAGAGTATGCGAT
GTGCTTAAACAGGAGCATCCTGAATGGGGTGATGAGCAGTTGTTCCAGACAAGCAGGCTA
ATACTGATAGGAGAGACTATTAAGATTGTGATTGAAGATTATGTGCAACACTTGAGTGGC
TATCACTTCAAACTGAAATTTGACCCAGAACTACTTTTCAACAAACAATTCCAGTACCAA
AATCGTATTGCTGCTGAATTTAACACCCTCTATCACTGGCATCCCCTTCTGCCTGACACC
TTTCAAATTCATGACCAGAAATACAACTATCAACAGTTTATCTACAACAACTCTATATTG
CTGGAACATGGAATTACCCAGTTTGTTGAATCATTCACCAGGCAAATTGCTGGCAGGGTT
GCTGGTGGTAGGAATGTTCCACCCGCAGTACAGAAAGTATCACAGGCTTCCACTGACCAG
AGCAGGCAGATGAAATACCAGTCTTTTAATGAGTACCGCAAACGCTTTATGCTGAAGCCC
TATGAATCATTTGAAGAACTTACAGGAGAAAAGGAAATGTCTGCAGAGTTGGAAGCACTC
TATGGTGACATCGATGCTGTGGAGCTGTATCCTGCCCTTCTGGTAGAAAAGCCTCGGCCA
GATGCCATCTTTGGTGAAACCATGGTAGAAGTTGGAGCACCATTCTCCTTGAAAGGACTT
ATGGGTAATGTTATATGTTCTCCTGCCTACTGGAAGCCAAGCACTTTTGGTGGAGAAGTG
GGTTTTCAAATCATCAACACTGCCTCAATTCAGTCTCTCATCTGCAATAACGTGAAGGGC
TGTCCCTTTACTTCATTCAGTGTTCCAGATCCAGAGCTCATTAAAACAGTCACCATCAAT
GCAAGTTCTTCCCGCTCCGGACTAGATGATATCAATCCCACAGTACTACTAAAAGAACGT
TCGACTGAACTGTAG
Target 3 GenBank Gene ID
Target 3 GeneCard ID PTGS2 Link Image
Target 3 GenAtlas ID PTGS2 Link Image
Target 3 HGNC ID HGNC:9605 Link Image
Target 3 Chromosome Location 1
Target 3 Locus 1q25.2-q25.3
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Hla T, Neilson K: Human cyclooxygenase-2 cDNA. Proc Natl Acad Sci U S A. 1992 Aug 15;89(16):7384-8. [PubMed Link Image]
  2. Appleby SB, Ristimaki A, Neilson K, Narko K, Hla T: Structure of the human cyclo-oxygenase-2 gene. Biochem J. 1994 Sep 15;302 ( Pt 3):723-7. [PubMed Link Image]
  3. Kosaka T, Miyata A, Ihara H, Hara S, Sugimoto T, Takeda O, Takahashi E, Tanabe T: Characterization of the human gene (PTGS2) encoding prostaglandin-endoperoxide synthase 2. Eur J Biochem. 1994 May 1;221(3):889-97. [PubMed Link Image]
  4. Jones DA, Carlton DP, McIntyre TM, Zimmerman GA, Prescott SM: Molecular cloning of human prostaglandin endoperoxide synthase type II and demonstration of expression in response to cytokines. J Biol Chem. 1993 Apr 25;268(12):9049-54. [PubMed Link Image]
Target 3 Drug References
  1. Kalgutkar AS, Crews BC, Rowlinson SW, Marnett AB, Kozak KR, Remmel RP, Marnett LJ: Biochemically based design of cyclooxygenase-2 (COX-2) inhibitors: facile conversion of nonsteroidal antiinflammatory drugs to potent and highly selective COX-2 inhibitors. Proc Natl Acad Sci U S A. 2000 Jan 18;97(2):925-30. [PubMed Link Image]
  2. Traupe T, Lang M, Goettsch W, Munter K, Morawietz H, Vetter W, Barton M: Obesity increases prostanoid-mediated vasoconstriction and vascular thromboxane receptor gene expression. J Hypertens. 2002 Nov;20(11):2239-45. [PubMed Link Image]
  3. Wilson JE, Chandrasekharan NV, Westover KD, Eager KB, Simmons DL: Determination of expression of cyclooxygenase-1 and -2 isozymes in canine tissues and their differential sensitivity to nonsteroidal anti-inflammatory drugs. Am J Vet Res. 2004 Jun;65(6):810-8. [PubMed Link Image]
  4. Narsinghani T, Chaturvedi SC: QSAR analysis of meclofenamic acid analogues as selective COX-2 inhibitors. Bioorg Med Chem Lett. 2006 Jan 15;16(2):461-8. Epub 2005 Nov 14. [PubMed Link Image]
  5. Smith WL, Meade EA, DeWitt DL: Interactions of PGH synthase isozymes-1 and -2 with NSAIDs. Ann N Y Acad Sci. 1994 Nov 15;744:50-7. [PubMed Link Image]

This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also supported in part by GenomeQuest, Inc., an enterprise genomic information company serving the life science community.