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Showing drug card for Praziquantel (DB01058)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-23 18:06:57
Primary Accession Number DB01058
Secondary Accession Number
  • APRD01196
  • EXPT02728
Name Praziquantel
Drug Type
  • Approved
  • Small Molecule
Description An anthelmintic used in most schistosome and many cestode infestations. [PubChem]
Synonyms Not Available
Brand Names
  1. Biltricide
Brand Mixtures
  1. Drontal - Tab (Praziquantel + Pyrantel (Pyrantel Pamoate))
  2. Drontal Plus Tablets for Med. And Large Dogs (Febantel + Praziquantel + Pyrantel (Pyrantel Pamoate))
  3. Drontal Plus Tablets for Small Dogs (Febantel + Praziquantel + Pyrantel (Pyrantel Pamoate))
  4. Drontal Plus Tabs for Medium and Large Dogs (Febantel + Praziquantel + Pyrantel (Pyrantel Pamoate))
  5. Drontal Tab (Praziquantel + Pyrantel (Pyrantel Pamoate))
Chemical IUPAC Name 2-(cyclohexanecarbonyl)-3,6,7,11b-tetrahydro-1H-pyrazino[6,1-a]isoquinolin-4-one
Chemical Formula C19H24N2O2
Chemical Structure Structure
CAS Registry Number 55268-74-1
InChI Identifier InChI=1/C19H24N2O2/c22-18-13-20(19(23)15-7-2-1-3-8-15)12-17-16-9-5-4-6-14(16)10-11-21(17)18/h4-6,9,15,17H,1-3,7-8,10-13H2
InChI Key FSVJFNAIGNNGKK-UHFFFAOYAM
KEGG Drug D00471 Link Image
KEGG Compound C07367 Link Image
PubChem Compound 4891 Link Image
PubChem Substance 9571 Link Image
ChEBI ID Not Available
PharmGKB ID PA451092 Link Image
HET ID PZQ Link Image
GenBank ID Not Available
Drug ID Number [DIN] 02230897 Link Image
RxList Link http://www.rxlist.com/cgi/generic2/praziquantel.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Praziquantel Link Image
FDA Label
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 312.4061
Monoisotopic Molecular Weight 312.1838
State Solid
Melting Point 136 oC
Experimental Water Solubility 400 mg/L Source: PhysProp
Predicted Water Solubility 3.81e-01 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 2.5 Source: PhysProp
Predicted LogP 2.42 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -2.91 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 1GTB Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES O=C1CN(C[C@H]2N1CCC1=CC=CC=C21)C(=O)C1CCCCC1
Canonical SMILES O=C1CN(CC2N1CCC1=CC=CC=C21)C(=O)C1CCCCC1
Drug Category
  • Anthelmintics
ATC Codes
AHFS Codes
  • 08:08.00
Indication For the treatment of infections due to all species of schistosoma.
Pharmacology Praziquantel is an anthelmintic used in most schistosome and many cestode infestations. Praziquantel effects the permeability of the cell membrane resulting in the contraction of schistosomes. The drug further causes vacuolization and disintegration of the schistosome tegument. The effect is more marked on adult worms compared to young worms. An increased calcium influx may play an important role. Secondary effects are inhibition of glucose uptake, lowering of glycogen levels and stimulation of lactate release. The action of praziquantel is limited very specifically to trematodes and cestodes; nematodes (including filariae) are not affected.
Mechanism of Action Praziquantel works by causing severe spasms and paralysis of the worms' muscles. This paralysis is accompanied - and probably caused - by a rapid Ca 2+ influx inside the schistosome. Morphological alterations are another early effect of praziquantel. These morphological alterations are accompanied by an increased exposure of schistosome antigens at the parasite surface. The worms are then either completely destroyed in the intestine or passed in the stool. An interesting quirk of praziquantel is that it is relatively ineffective against juvenile schistosomes. While initially effective, effectiveness against schistosomes decreases until it reaches a minimum at 3-4 weeks. Effectiveness then increases again until it is once again fully effective at 6-7 weeks. Glutathione S-transferase (GST), an essential detoxification enzyme in parasitic helminths, is a major vaccine target and a drug target against schistosomiasis.
Absorption Rapidly absorbed (80%)
Toxicity Not Available
Protein Binding 80 to 85%
Biotransformation renal
Half Life 0.8-1.5 hours (in serum)
Dosage Forms
Form Route
Tablet Oral
Patient Information Not Available
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Carbamazepine Markedly lower praziquantel levels
Chloroquine Markedly lower praziquantel levels
Phenytoin Markedly lower praziquantel levels
Rifampin Significant decrease in praziquantel level
Food Interactions
  • Grapefruit and grapefruit juice should be avoided throughout treatment. Grapefruit can increase serum levels of this product.
  • Take with food.
Pathways Not Available
General References
  1. Wikipedia Link Image
  2. RxList Link Image
Organisms Affected Not Available
Targets
  1. Glutathione S-transferase class-mu 26 kDa isozyme
  2. Glutathione S-transferase A2
Drug Target 1 [top]
Target 1 ID 652
Target 1 Name Glutathione S-transferase class-mu 26 kDa isozyme
Target 1 Synonyms
  1. EC 2.5.1.18
  2. GST 26
  3. Sj26 antigen
  4. SjGST
Target 1 Gene Name Not Available
Target 1 Protein Sequence >Glutathione S-transferase 26 kDa 
SPILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKWRNKKFELGLEFPNLPYYIDG
DVKLTQSMAIIRYIADKHNMLGGCPKERAEISMLEGAVLDIRYGVSRIAYSKDFETLKVD
FLSKLPEMLKMFEDRLCHKTYLNGDHVTHPDFMLYDALDVVLYMDPMCLDAFPKLVCFKK
RIEAIPQIDKYLKSSKYIAWPLQGWQATFGGGDHPPK
Target 1 Number of Residues 220
Target 1 Molecular Weight 25368
Target 1 Theoretical pI 6.51
Target 1 GO Classification Not Available
Target 1 General Function Involved in glutathione transferase activity
Target 1 Specific Function GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut
Target 1 Pathways
Name SMPDB Link KEGG Link
Glutathione metabolism SMP00015 Link Image map00480 Link Image
Target 1 Reactions
  • RX + glutathione = HX + R-S-glutathione
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Essential
Target 1 GenBank ID Protein 160927 Link Image
Target 1 UniProtKB/Swiss-Prot ID P08515 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name GST26_SCHJA Link Image
Target 1 PDB ID 1UA5 Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location Not Available
Target 1 Gene Sequence >657 bp 
ATGTCCCCTATACTAGGTTATTGGAAAATTAAGGGCCTTGTGCAACCCACTCGACTTCTT
TTGGAATATCTTGAAGAAAAATATGAAGAGCATTTGTATGAGCGCGATGAAGGTGATAAA
TGGCGAAACAAAAAGTTTGAATTGGGTTTGGAGTTTCCCAATCTTCCTTATTATATTGAT
GGTGATGTTAAATTAACACAGTCTATGGCCATCATACGTTATATAGCTGACAAGCACAAC
ATGTTGGGTGGTTGTCCAAAAGAGCGTGCAGAGATTTCAATGCTTGAAGGAGCGGTTTTG
GATATTAGATACGGTGTTTCGAGAATTGCATATAGTAAAGACTTTGAAACTCTCAAAGTT
GATTTTCTTAGCAAGCTACCTGAAATGCTGAAAATGTTCGAAGATCGTTTATGTCATAAA
ACATATTTAAATGGTGATCATGTAACCCATCCTGACTTCATGTTGTATGACGCTCTTGAT
GTTGTTTTATACATGGACCCAATGTGCCTGGATGCGTTCCCAAAATTAGTTTGTTTTAAA
AAACGTATTGAAGCTATCCCACAAATTGATAAGTACTTGAAATCCAGCAAGTATATAGCA
TGGCCTTTGCAGGGCTGGCAAGCCACGTTTGGTGGTGGCGACCATCCTCCAAAATAA
Target 1 GenBank Gene ID
Target 1 GeneCard ID Not Available
Target 1 GenAtlas ID Not Available
Target 1 HGNC ID Not Available
Target 1 Chromosome Location Not Available
Target 1 Locus Not Available
Target 1 SNPs Not Available
Target 1 General References
  1. Smith DB, Davern KM, Board PG, Tiu WU, Garcia EG, Mitchell GF: Mr 26,000 antigen of Schistosoma japonicum recognized by resistant WEHI 129/J mice is a parasite glutathione S-transferase. Proc Natl Acad Sci U S A. 1986 Nov;83(22):8703-7. [PubMed Link Image]
  2. Smith DB, Rubira MR, Simpson RJ, Davern KM, Tiu WU, Board PG, Mitchell GF: Expression of an enzymatically active parasite molecule in Escherichia coli: Schistosoma japonicum glutathione S-transferase. Mol Biochem Parasitol. 1988 Jan 15;27(2-3):249-56. [PubMed Link Image]
  3. Lim K, Ho JX, Keeling K, Gilliland GL, Ji X, Ruker F, Carter DC: Three-dimensional structure of Schistosoma japonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of gp41 from HIV. Protein Sci. 1994 Dec;3(12):2233-44. [PubMed Link Image]
  4. McTigue MA, Williams DR, Tainer JA: Crystal structures of a schistosomal drug and vaccine target: glutathione S-transferase from Schistosoma japonica and its complex with the leading antischistosomal drug praziquantel. J Mol Biol. 1995 Feb 10;246(1):21-7. [PubMed Link Image]
Target 1 Drug References
  1. Rufer AC, Thiebach L, Baer K, Klein HW, Hennig M: X-ray structure of glutathione S-transferase from Schistosoma japonicum in a new crystal form reveals flexibility of the substrate-binding site. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Mar 1;61(Pt 3):263-5. Epub 2005 Feb 24. [PubMed Link Image]
  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 Link Image]
  3. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
  4. McTigue MA, Williams DR, Tainer JA: Crystal structures of a schistosomal drug and vaccine target: glutathione S-transferase from Schistosoma japonica and its complex with the leading antischistosomal drug praziquantel. J Mol Biol. 1995 Feb 10;246(1):21-7. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 3932
Target 2 Name Glutathione S-transferase A2
Target 2 Synonyms
  1. EC 2.5.1.18
  2. GST class-alpha member 2
  3. GST- gamma
  4. GSTA2-2
  5. GTH2
  6. HA subunit 2
Target 2 Gene Name GSTA2
Target 2 Protein Sequence >Glutathione S-transferase A2 
MAEKPKLHYSNIRGRMESIRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQQVPMVEI
DGMKLVQTRAILNYIASKYNLYGKDIKEKALIDMYIEGIADLGEMILLLPFSQPEEQDAK
LALIQEKTKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLVELLYYVEELDSSLISSFPL
LKALKTRISNLPTVKKFLQPGSPRKPPMDEKSLEESRKIFRF
Target 2 Number of Residues 225
Target 2 Molecular Weight 25664
Target 2 Theoretical pI 9.07
Target 2 GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring alkyl or aryl (other than methyl) groups
glutathione transferase activity
Process
physiological process
metabolism
Component
Not Available
Target 2 General Function Involved in glutathione transferase activity
Target 2 Specific Function Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles
Target 2 Pathways
Name SMPDB Link KEGG Link
Metabolism of xenobiotics by cytochrome P450 map00480 Link Image
Target 2 Reactions
  • RX + glutathione = HX + R-S-glutathione
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 306811 Link Image
Target 2 UniProtKB/Swiss-Prot ID P09210 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name GSTA2_HUMAN Link Image
Target 2 PDB ID 1AGS Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location
  • Cytoplasm
Target 2 Gene Sequence >669 bp 
ATGGCAGAGAAGCCCAAGCTCCACTACTCCAATATACGGGGCAGAATGGAGTCCATCCGG
TGGCTCCTGGCTGCAGCTGGAGTAGAGTTTGAAGAGAAATTTATAAAATCTGCAGAAGAT
TTGGACAAGTTAAGAAATGATGGATATTTGATGTTCCAGCAAGTGCCAATGGTTGAGATT
GATGGGATGAAGCTGGTGCAGACCAGAGCCATTCTCAACTACATTGCCAGCAAATACAAC
CTCTATGGGAAAGACATAAAGGAGAAAGCCCTGATTGATATGTATATAGAAGGTATAGCA
GATTTGGGTGAAATGATCCTTCTTCTGCCCTTTACTCAACCTGAGGAACAAGATGCCAAG
CTTGCCTTGATCCAAGAGAAAACAAAAAATCGCTACTTCCCTGCCTTTGAAAAAGTCTTA
AAGAGCCACGGACAAGACTACCTTGTTGGCAACAAGCTGAGCCGGGCTGACATTCACCTG
GTGGAACTTCTCTACTACGTGGAAGAGCTTGACTCTAGCCTTATTTCCAGCTTCCCTCTG
CTGAAGGCCCTGAAAACCAGAATCAGTAACCTGCCCACAGTGAAGAAGTTTCTACAGCCT
GGCAGCCCAAGGAAGCCTCCCATGGATGAGAAATCTTTAGAAGAATCAAGGAAGATTTTC
AGGTTTTAA
Target 2 GenBank Gene ID
Target 2 GeneCard ID GSTA2 Link Image
Target 2 GenAtlas ID GSTA2 Link Image
Target 2 HGNC ID HGNC:4627 Link Image
Target 2 Chromosome Location 6
Target 2 Locus 6p12.1
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Tetlow N, Liu D, Board P: Polymorphism of human Alpha class glutathione transferases. Pharmacogenetics. 2001 Oct;11(7):609-17. [PubMed Link Image]
  2. Rohrdanz E, Nguyen T, Pickett CB: Isolation and characterization of the human glutathione S-transferase A2 subunit gene. Arch Biochem Biophys. 1992 Nov 1;298(2):747-52. [PubMed Link Image]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  4. Klone A, Hussnatter R, Sies H: Cloning, sequencing and characterization of the human alpha glutathione S-transferase gene corresponding to the cDNA clone pGTH2. Biochem J. 1992 Aug 1;285 ( Pt 3):925-8. [PubMed Link Image]
  5. Hayes JD, Kerr LA, Cronshaw AD: Evidence that glutathione S-transferases B1B1 and B2B2 are the products of separate genes and that their expression in human liver is subject to inter-individual variation. Molecular relationships between the B1 and B2 subunits and other Alpha class glutathione S-transferases. Biochem J. 1989 Dec 1;264(2):437-45. [PubMed Link Image]
  6. Rhoads DM, Zarlengo RP, Tu CP: The basic glutathione S-transferases from human livers are products of separate genes. Biochem Biophys Res Commun. 1987 May 29;145(1):474-81. [PubMed Link Image]
  7. Ahmad H, Singhal SS, Saxena M, Awasthi YC: Characterization of two novel subunits of the alpha-class glutathione S-transferases of human liver. Biochim Biophys Acta. 1993 Feb 13;1161(2-3):333-6. [PubMed Link Image]
Target 2 Drug References
  1. Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [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.