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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-04-30 00:55:55
Primary Accession Number DB00685
Secondary Accession Number
  • APRD01281
Name Trovafloxacin
Drug Type
  • Small Molecule
Description Trovafloxacin (sold as Trovan by Pfizer) is a broad spectrum antibiotic that inhibits the uncoiling of supercoiled DNA in various bacteria by blocking the activity of DNA gyrase and topoisomerase IV. It was withdrawn from the market due to the risk of hepatotoxicity. It had better gram-positive bacterial coverage and less gram-negative coverage than the previous fluoroquinolones. [Wikipedia]
Synonyms
  1. TVFX
  2. Trovafloxacin mesylate
Brand Names
  1. Trovan
Brand Mixtures
  1. Trovan/Zithromax Compliance Pak (Trovafloxacin + Azithromycin)
Chemical IUPAC Name 7-[(1R,5S)-6-amino-3-azabicyclo[3.1.0]hexan-3-yl]-1-(2,4-difluorophenyl)-6-fluoro-4-oxo-1,8-naphthyridine-3-carboxylic acid
Chemical Formula C20H15F3N4O3
Chemical Structure Structure
CAS Registry Number 147059-72-1
InChI Identifier InChI=1/C20H15F3N4O3/c21-8-1-2-15(13(22)3-8)27-7-12(20(29)30)17(28)9-4-14(23)19(25-18(9)27)26-5-10-11(6-26)16(10)24/h1-4,7,10-11,16H,5-6,24H2,(H,29,30)/t10-,11+,16?/f/h29H
InChI Key WVPSKSLAZQPAKQ-LGYPRZIVDQ
KEGG Drug Not Available
KEGG Compound C07664 Link Image
PubChem Compound 62959 Link Image
PubChem Substance 9866 Link Image
ChEBI ID Not Available
PharmGKB ID PA451804 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 02239191 Link Image
RxList Link http://www.rxlist.com/cgi/generic/trovazit.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Trovafloxacin Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS) Not Available
Synthesis Reference Not Available
Average Molecular Weight 416.3533
Monoisotopic Molecular Weight 416.1096
State Solid
Melting Point Not Available
Experimental Water Solubility 12.3 mg/L Source: PhysProp
Predicted Water Solubility 7.04e-02 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 3.7 Source: PhysProp
Predicted LogP 0.86 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -3.77 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 N[C@H]1[C@@H]2CN(C[C@H]12)C1=C(F)C=C2C(=O)C(=CN(C2=N1)C1=C(F)C=C(F)C=C1)C(O)=O
Canonical SMILES NC1C2CN(CC12)C1=C(F)C=C2C(=O)C(=CN(C2=N1)C1=C(F)C=C(F)C=C1)C(O)=O
Drug Category
  • Anti-Infective Agents
  • Anti-Infectives
  • Fluoroquinolones
  • Quinolones
ATC Codes
AHFS Codes Not Available
Indication For treatment of infections caused by susceptible strains of the designated microorganisms in uncomplicated urethral gonorrhea in males and endocervical and rectal gonorrhea in females caused by Neisseria gonorrhoeae as well as non gonoccocal urethritis and cervicitis due to Chlamydia trachomatis.
Pharmacology Trovafloxacin is a broad spectrum antibiotic that inhibits DNA supercoiling in various bacteria by blocking the activity of DNA gyrase and topoisomerase IV. It is not used widely due to the risk of hepatotoxicity. It tends to have better gram-positive bacterial coverage and less gram-negative coverage than the previous fluoroquinolones. Mechanism of action of fluoroquinolones including trovafloxacin is different from that of penicillins, cephalosporins, aminoglycosides, macrolides, and tetracyclines. Therefore fluoroquinolones may be active against pathogens that are resistant to these antibiotics. There is no cross-resistance between trovafloxacin and the mentioned classes of antibiotics. The overall results obtained from in vitro synergy studies, testing combinations of trovafloxacin with beta-lactams and aminoglycosides, indicate that synergy is strain specific and not commonly encountered. This agrees with results obtained previously with other fluoroquinolones. Resistance to trovafloxacin in vitro develops slowly via multiple-step mutation in a manner similar to other fluoroquinolones. Resistance to trovafloxacin in vitro occurs at a general frequency of between 1x10-7 to 10-10. Although cross-resistance has been observed between trovafloxacin and some other fluoroquinolones, some microorganisms resistant to other fluoroquinolones may be susceptible to trovafloxacin.
Mechanism of Action Trovafloxacin is a fluoronaphthyridone related to the fluoroquinolones with in vitro activity against a wide range of gram-negative and gram-positive aerobic and anaerobic microorganisms. The bactericidal action of trovafloxacin results from inhibition of DNA gyrase and topoisomerase IV. DNA gyrase is an essential enzyme that is involved in the replication, transcription, and repair of bacterial DNA. Topoisomerase IV is an enzyme known to play a key role in the partitioning of the chromosomal DNA during bacterial cell division.
Absorption Well-absorbed from the gastrointestinal tract after oral administration and does not depend on concomitant food intake. The absolute bioavailability is approximately 88%.
Toxicity Symptoms of overdose include convulsions, decreased activity, diarrhea, sleepiness, tremors, and/or vomiting.
Protein Binding The mean plasma protein bound fraction is approximately 76%, and is concentration-independent.
Biotransformation Metabolism Trovafloxacin is metabolized by conjugation (the role of cytochrome P450 oxidative metabolism of trovafloxacin is minimal). The major metabolites include the ester glucuronide, which appears in the urine (13% of the administered dose); and the N -acetyl metabolite, which appears in the feces and serum (9% and 2.5% of the administered dose, respectively). Other minor metabolites include diacid, hydroxycarboxylic acid, and sulfamate, which have been identified in both the feces and the urine in small amounts (< 4% of the administered dose).
Half Life Following oral administration, half-life ranged from 9.1 hours to 12.2 hours over the dosage range of 100 to 200 mg tablets. Following intravenous infusion, half-life ranged from 9.4 to 12.7 hours over a dosage range of 100 to 300 mg.
Dosage Forms
Form Route
Liquid Intravenous
Tablet Oral
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Aluminium Aluminum may decrease the absorption of orally administered Trovafloxacin. Administer Trovafloxacin 2 hours before or 6 hours after a dose of the aluminum containing agent to minimize the interaction.
Calcium Acetate Calcium may decrease the absorption of orally administered Trovafloxacin. Administer Trovafloxacin 2 hours before or 6 hours after a dose of the calcium containining agent to minimize the interaction.
Calcium Chloride Calcium may decrease the absorption of orally administered Trovafloxacin. Administer Trovafloxacin 2 hours before or 6 hours after a dose of the calcium containing agent to minimize the interaction.
Calcium Gluceptate Calcium may decrease the absorption of orally administered Trovafloxacin. Administer Trovafloxacin 2 hours before or 6 hours after a dose of the calcium containing agent to minimize the interaction.
Didanosine Didanosine may decrease the absorption of orally administered Trovafloxacin. The Didanosine formulation contains magnesium and aluminum ions that intefere with Trovafloxacin absorption. Administer Trovafloxacin 2 hours before or 6 hours after the Didanosine dose to minimize the interaction. This interaction is not observed with enteric coated Didanosine.
Iron Iron may decrease the absorption of orally administered Trovafloxacin. Administer Trovafloxacin 2 hours before or 6 hours after a dose of the iron containing agent to minimize the interaction.
Magnesium Sulfate Magnesium may decrease the absorption of orally administered Trovafloxacin. Administer Trovafloxacin 2 hours before or 6 hours after a dose of the magnesium containing agent to minimize the interaction.
Magnesium oxide Magnesium may decrease the absorption of orally administered Trovafloxacin. Administer Trovafloxacin 2 hours before or 6 hours after a dose of the magnesium containing agent to minimize the interaction.
Morphine Morphine may reduce serum levels of Trovafloxacin decreasing the efficacy of the antibiotic. IV doses of morphine should be administered at least 2 hours after a dose of Trovafloxacin given in a fasting state or 4 hours after if given in a fed state.
Quinapril Quinapril may decrease the absorption of orally administered Trovafloxacin. The Quinapril formulation contains magnesium ions that may intefere with Trovafloxacin absorption. Administer Trovafloxacin 2 hours before or 6 hours after the Quinapril dose to minimize the interaction.
Sevelamer Sevelamer may decrease the absorption of orally administered Trovafloxacin. The Sevelamer formulation contains iron that may intefere with Trovafloxacin absorption. Administer Trovafloxacin 2 hours before or 6 hours after the Sevelamer dose to minimize the interaction.
Sucralfate Sucralfate may decrease the absorption of orally administered Trovafloxacin. The Sucralfate formulation contains aluminum ions that may intefere with Trovafloxacin absorption. Administer Trovafloxacin 2 hours before or 6 hours after the Sucralfate dose to minimize the interaction.
Zinc Zinc may decrease the absorption of orally administered Trovafloxacin. Administer Trovafloxacin 2 hours before or 6 hours after a dose of the zinc containing agent to minimize the interaction.
Food Interactions Not Available
Pathways Not Available
General References
  1. Wikipedia Link Image
  2. RxList Link Image
Organisms Affected
  • Enteric bacteria and other eubacteria
Targets
  1. DNA gyrase subunit A
  2. DNA topoisomerase 4 subunit A
  3. DNA topoisomerase 2-alpha
Drug Target 1 [top]
Target 1 ID 404
Target 1 Name DNA gyrase subunit A
Target 1 Synonyms
  1. EC 5.99.1.3
Target 1 Gene Name gyrA
Target 1 Protein Sequence >DNA gyrase subunit A 
MTDSIQSSITPVNIEEELKSSYLDYAMSVIVGRALPDVRDGLKPVHRRVLFSMDREGNTA
NKKYVKSARVVGDVIGKYHPHGDSAVYDTIVRMAQPFSLRYMLVDGQGNFGSIDGDAPAA
MRYTEVRMQKITQALLTDLDKETVNFSPNYDGELMIPDVLPTRIPALLANGSSGIAVGMA
TNIPPHNLNEVLNGCLAYIDKNEITIDELMQHIPGPDFPTAALINGRKGIEEAYRTGRGK
VYVRARATVETNEKGREQIIVSELPYQVNKAKLVEKIAELIREKKIEGISNITDLSNKEG
IRIEIDIKRDAVGEVVLNHLYSLTQMQVTFGINMVALDHGQPRLFNLKEIIEAFVLHRRE
VVTRRSIFELRKARERTHILEGLAVARSNIDEMIAIIRNSKNREEAATSISSRSWTLHSD
IINLLDASARPDELEENLGIQGEQYYLSPAQVNAILELRLHRLTGIAFEEVIKEYEELLV
KIADLLHILSSAERLMEVIREELEEVKAQFGDDRLTEITAASGDIDLEDLIAQEDVVVTL
SHEGYVKYQPLTDYEAQRRGGKGKSATKMKEEDFIEKLLVANTHDTILCFSSRGRLYWLK
VYQLPQASRGARGRPIVNILPLQENERITAILPVSAYEEDKFVVMATAGGIVKKIALTEF
SRPRSNGIIALNLRDEDELIGVDITDGSNEIMLFSSQGRVVRFAENAVRAMGRLATGVRG
IKLALTNDISDDESAVEIEDISDDNAEASLDLNIDKVVSLVVPKGEGAILTATQNGYGKR
TQLSEYPTKSRNTKGVISIKVSERNGKVVAATQVEETDQIMLITDAGTLVRTRVSEVSIV
GRNTQGVRLIRTADDEHVVSLERVCDADEDDSLEESSSEE
Target 1 Number of Residues 894
Target 1 Molecular Weight 97820
Target 1 Theoretical pI 4.85
Target 1 GO Classification
Function
nucleotide binding
purine nucleotide binding
adenyl nucleotide binding
ATP binding
DNA topoisomerase (ATP-hydrolyzing) activity
DNA topoisomerase activity
DNA topoisomerase (ATP-hydrolyzing) activity
binding
nucleic acid binding
DNA binding
Process
DNA replication
DNA-dependent DNA replication
DNA unwinding during replication
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
DNA metabolism
DNA topological change
Component
organelle
non-membrane-bound organelle
intracellular non-membrane-bound organelle
chromosome
Target 1 General Function Replication, recombination and repair
Target 1 Specific Function DNA gyrase negatively supercoils closed circular double- stranded DNA in an ATP-dependent manner and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings
Target 1 Pathways Not Available
Target 1 Reactions
  • ATP-dependent breakage, passage and rejoining of double-stranded DNA INHIBITOR Coumermycin A1; GRI22222X; Nalidixic acid; Novobiocin; Ciprofloxacin
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Essential
Target 1 GenBank ID Protein 1574722 Link Image
Target 1 UniProtKB/Swiss-Prot ID P43700 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name GYRA_HAEIN Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location
  • Cytoplasmic
Target 1 Gene Sequence >2643 bp 
TTATTCTTCAGAACTGCTTTCTTCCAAAGAATCATCTTCATCTGCATCACAAACACGTTC
TAAACTTACTACGTGTTCATCATCGGCAGTACGAATTAAGCGAACACCTTGCGTGTTACG
CCCTACAATGCTCACTTCGCTTACGCGTGTGCGAACAAGGGTTCCTGCATCAGTGATCAA
CATAATTTGGTCTGTTTCTTCTACTTGAGTTGCGGCAACGACTTTACCATTGCGTTCACT
CACTTTAATCGAAATCACACCTTTTGTATTACGTGATTTAGTTGGGTATTCACTTAATTG
TGTGCGTTTTCCGTAGCCGTTTTGCGTTGCGGTTAAAATTGCCCCTTCACCTTTTGGCAC
AACGAGCGAGACCACTTTATCGATATTTAAGTCTAATGATGCTTCAGCGTTGTCATCAGA
AATATCTTCAATTTCTACCGCACTTTCATCGTCAGAAATATCGTTTGTTAAAGCCAGTTT
GATACCGCGAACACCTGTTGCTAAACGCCCCATCGCACGCACGGCATTTTCAGCAAAACG
CACCACGCGACCTTGTGATGAGAACAACATAATTTCGTTGCTGCCATCAGTAATATCCAC
GCCGATTAATTCATCTTCGTCACGTAAATTCAATGCGATGATACCGTTTGAACGTGGACG
GCTAAATTCGGTTAAGGCGATTTTCTTCACAATACCGCCAGCAGTTGCCATGACTACGAA
TTTATCTTCTTCGTAAGCAGAAACTGGCAAGATTGCAGTAATACGTTCGTTTTCTTGTAA
CGGAAGAATATTCACAATTGGACGACCGCGTGCGCCACGGCTCGCTTGCGGAAGTTGATA
TACTTTCAACCAATATAAACGACCACGGCTAGAGAAGCAGAGGATGGTATCGTGAGTATT
TGCTACCAGTAATTTTTCGATGAAATCTTCTTCTTTCATCTTCGTTGCAGATTTGCCTTT
ACCGCCACGGCGTTGTGCTTCATAGTCAGTCAGTGGTTGGTATTTCACATAACCTTCGTG
AGAAAGCGTCACAACCACGTCTTCTTGTGCGATTAAATCTTCTAAATCAATATCGCCAGA
AGCAGCGGTAATTTCAGTTAAACGATCATCACCAAATTGTGCTTTTACTTCTTCCAATTC
TTCACGAATTACTTCCATTAAACGTTCTGCACTACTTAAAATATGAAGAAGATCCGCAAT
TTTAACTAATAATTCTTCATATTCTTTTATAACTTCTTCAAACGCAATGCCCGTTAAACG
GTGTAAGCGAAGTTCTAGAATTGCGTTTACTTGCGCTGGCGATAAGTAATATTGTTCGCC
TTGAATACCAAGATTTTCTTCTAACTCATCAGGACGAGCAGAAGCATCAAGAAGATTAAT
AATATCGCTATGTAACGTCCAAGAGCGTGAACTGATTGATGTTGCGGCTTCTTCACGGTT
TTTAGAGTTACGAATGATCGCAATCATTTCATCGATATTAGAACGAGCAACCGCTAAACC
TTCCAAAATATGCGTACGTTCACGTGCTTTGCGAAGCTCAAAGATAGAACGACGTGTAAC
CACTTCACGGCGGTGTAAAACAAAGGCTTCAATAATTTCTTTAAGATTAAATAAACGTGG
CTGACCGTGATCCAATGCCACCATATTGATACCAAAGGTCACTTGCATTTGAGTGAGTGA
GTAAAGATGGTTTAATACCACTTCCCCCACTGCATCACGTTTAATATCAATTTCAATACG
GATCCCTTCTTTATTTGAAAGGTCAGTAATATTGCTGATACCTTCGATTTTTTTCTCGCG
AATTAATTCGGCGATTTTCTCGACTAATTTTGCTTTATTTACTTGGTATGGCAATTCAGA
CACGATAATTTGCTCGCGTCCTTTTTCGTTGGTTTCTACCGTTGCACGAGCACGAACATA
CACTTTACCACGACCAGTGCGATAGGCCTCTTCAATCCCTTTACGACCATTAATTAACGC
AGCCGTTGGGAAGTCAGGCCCTGGAATATGTTGCATTAATTCATCAATGGTAATTTCATT
TTTGTCAATATAAGCCAAACAACCATTTAATACTTCGTTTAAGTTGTGAGGGGGAATGTT
AGTTGCCATCCCCACCGCAATACCAGAAGAACCATTTGCTAACAGTGCTGGAATACGAGT
CGGCAATACATCTGGAATCATTAATTCGCCATCATAGTTTGGCGAGAAATTGACGGTTTC
TTTATCCAAATCCGTGAGCAATGCTTGCGTAATTTTTTGCATACGTACTTCGGTATAACG
CATTGCAGCTGGCGCATCACCATCAATTGAACCAAAGTTACCTTGCCCATCAACCAACAT
ATAGCGAAGTGAGAAGGGTTGTGCCATACGAACGATGGTATCGTACACGGCGGAGTCACC
ATGCGGGTGATATTTACCGATTACATCACCCACAACACGCGCTGATTTTACGTATTTTTT
ATTGGCGGTATTGCCTTCGCGATCCATTGAGAATAGTACGCGGCGGTGAACAGGTTTTAA
ACCATCTCGAACGTCAGGTAATGCACGCCCAACGATAACCGACATCGCGTAGTCAAGGTA
GGAAGATTTAAGTTCTTCTTCGATATTGACAGGGGTGATAGATGATTGGATTGAATCCGT
CAT
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 SNPJam Report Link Image
Target 1 General References
  1. Fleischmann RD, Adams MD, White O, Clayton RA, Kirkness EF, Kerlavage AR, Bult CJ, Tomb JF, Dougherty BA, Merrick JM, et al.: Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. Science. 1995 Jul 28;269(5223):496-512. [PubMed Link Image]
Target 1 Drug References
  1. Gootz TD, Zaniewski RP, Haskell SL, Kaczmarek FS, Maurice AE: Activities of trovafloxacin compared with those of other fluoroquinolones against purified topoisomerases and gyrA and grlA mutants of Staphylococcus aureus. Antimicrob Agents Chemother. 1999 Aug;43(8):1845-55. [PubMed Link Image]
  2. Brisse S, Milatovic D, Fluit AC, Verhoef J, Martin N, Scheuring S, Kohrer K, Schmitz FJ: Comparative in vitro activities of ciprofloxacin, clinafloxacin, gatifloxacin, levofloxacin, moxifloxacin, and trovafloxacin against Klebsiella pneumoniae, Klebsiella oxytoca, Enterobacter cloacae, and Enterobacter aerogenes clinical isolates with alterations in GyrA and ParC proteins. Antimicrob Agents Chemother. 1999 Aug;43(8):2051-5. [PubMed Link Image]
  3. Bebear CM, Grau O, Charron A, Renaudin H, Gruson D, Bebear C: Cloning and nucleotide sequence of the DNA gyrase (gyrA) gene from Mycoplasma hominis and characterization of quinolone-resistant mutants selected in vitro with trovafloxacin. Antimicrob Agents Chemother. 2000 Oct;44(10):2719-27. [PubMed Link Image]
  4. 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]
  5. 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]
Drug Target 2 [top]
Target 2 ID 477
Target 2 Name DNA topoisomerase 4 subunit A
Target 2 Synonyms
  1. EC 5.99.1.-
  2. Topoisomerase IV subunit A
Target 2 Gene Name parC
Target 2 Protein Sequence >DNA topoisomerase 4 subunit A 
MTNINYEGIEQMPLRTFTEKAYLNYSMYVIMDRALPFIGDGLKPVQRRIVYAMSELGLNA
TAKYKKSARTVGDVLGKFHPHGDSACYEAMVLMAQPFSYRYPLVDGQGNWGAPDDPKSFA
AMRYTESRLSKISEILLNELGQGTVDYQPNFDGTLAEPQYLPARLPHILLNGTTGIAVGM
ATDIPPHNINEIADAAVMLLDNPKAGLDDVLEIVQGPDFPTEAEIISPKSEIRKIYEQGR
GSIKMRATWKKEDGEIIISALPHQSSPSKVIAQIAEQMTAKKLPMLEDIRDEADHENPIR
IVLVPRSNRVDTDALMAHLFATTDLEKSYRVNMNMIGLDHKPAVKGLLEILNEWLDFRRT
TVTRRLQYRLDKVLSRLHILEGLMIAFLNIDEVIEIIRHEDDPKAELMARFNLSDEQADA
ILNLRLRHLAKLEENQLKAEQDELEKERLNLEAILGSERRLNTLIKKEIQEDAKKYANPR
MSQLVEREEAKMISESDMTPAEPVTVILSEMGWVRCAKGHDIDPKSLSYKAGDSYLAHAC
GKSNQAVVFIDSTGRSYALDPLSLPSARSQGEPLTGKLNLPTGATIEYVVMASEQQELLM
ASDAGYGFICKFEDLIARNKAGKALISLPENAKVLKPKTLINSTALVVAITSAGRMLIFP
AQDLPVLSKGKGNKMITIPAANAKDRSELLTKLLLISDQASLEFYSGKRKIVLKPEDLQK
FRAERGRKGSTLPRGLHTNLEIMVIEP
Target 2 Number of Residues 759
Target 2 Molecular Weight 83368
Target 2 Theoretical pI 6.42
Target 2 GO Classification
Function
DNA topoisomerase (ATP-hydrolyzing) activity
nucleotide binding
purine nucleotide binding
adenyl nucleotide binding
ATP binding
DNA topoisomerase (ATP-hydrolyzing) activity
DNA topoisomerase activity
binding
nucleic acid binding
DNA binding
Process
DNA replication
DNA-dependent DNA replication
DNA unwinding during replication
DNA topological change
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
DNA metabolism
Component
organelle
non-membrane-bound organelle
intracellular non-membrane-bound organelle
chromosome
Target 2 General Function Replication, recombination and repair
Target 2 Specific Function Topoisomerase IV is essential for chromosome segregation. It has relaxation of supercoiled DNA activity. Performs the decatenation events required during the replication of a circular DNA molecule
Target 2 Pathways Not Available
Target 2 Reactions Not Available
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Essential
Target 2 GenBank ID Protein 1574370 Link Image
Target 2 UniProtKB/Swiss-Prot ID P43702 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name PARC_HAEIN Link Image
Target 2 PDB ID Not Available
Target 2 Cellular Location
  • Bacterial cell membrane
  • peripheral membrane protein
Target 2 Gene Sequence >2244 bp 
ATGACAAATATCAACTATGAAGGCATTGAGCAAATGCCTCTACGCACCTTCACTGAAAAG
GCTTATCTCAACTATTCTATGTATGTCATCATGGATCGTGCGTTGCCTTTTATCGGTGAT
GGTTTAAAACCCGTTCAACGTCGTATTGTATATGCGATGTCTGAACTTGGCTTAAATGCC
ACGGCAAAATACAAAAAATCTGCTCGTACCGTCGGTGATGTACTCGGTAAATTCCATCCA
CATGGTGACAGTGCTTGTTATGAAGCTATGGTGTTAATGGCACAACCCTTCTCTTATCGT
TATCCACTTGTAGATGGTCAAGGTAACTGGGGGGCACCAGATGATCCAAAATCCTTCGCA
GCCATGCGTTATACGGAATCTCGCCTATCTAAAATCTCTGAAATCTTGTTGAATGAACTC
GGACAAGGAACAGTAGATTATCAACCAAACTTTGATGGAACCTTGGCTGAACCACAATAT
TTACCTGCTCGTTTACCGCATATTTTATTGAACGGCACAACAGGTATTGCGGTGGGGATG
GCCACAGATATTCCACCACACAATATTAACGAAATTGCTGATGCGGCAGTAATGTTGCTA
GATAATCCTAAAGCGGGATTAGATGATGTACTTGAAATTGTTCAAGGCCCAGATTTTCCA
ACAGAAGCGGAAATTATTTCGCCAAAATCAGAAATTCGTAAAATTTATGAGCAAGGTCGT
GGCTCAATAAAAATGCGTGCAACTTGGAAAAAAGAAGACGGTGAAATTATTATTTCAGCG
CTTCCACATCAATCTTCGCCATCCAAAGTCATTGCACAAATAGCCGAACAAATGACGGCA
AAAAAACTGCCAATGCTAGAAGATATTCGAGATGAAGCCGATCACGAAAATCCAATTCGC
ATTGTGCTAGTTCCTCGCTCAAATCGCGTCGATACTGATGCCTTAATGGCACATTTATTT
GCGACCACAGATCTTGAAAAAAGCTACCGTGTAAATATGAATATGATCGGGCTTGATCAT
AAACCAGCGGTAAAAGGCTTATTAGAAATCTTAAATGAATGGCTTGACTTCCGTCGCACA
ACGGTCACTCGTCGCCTTCAATATCGCCTAGATAAAGTGCTCTCTCGCTTGCATATTTTA
GAAGGCTTGATGATAGCCTTTTTAAATATTGATGAAGTTATCGAAATTATACGCCACGAA
GATGATCCAAAAGCAGAGCTTATGGCACGCTTTAATTTAAGCGATGAACAAGCCGATGCC
ATTTTAAATTTACGCTTACGTCATTTAGCGAAATTAGAAGAAAACCAACTCAAAGCAGAA
CAAGATGAACTTGAAAAAGAGCGGTTAAATTTAGAAGCAATTTTAGGATCAGAACGCCGT
TTGAATACGCTTATCAAAAAAGAAATTCAAGAAGATGCGAAAAAATATGCCAATCCACGT
ATGTCTCAACTGGTCGAACGTGAAGAAGCCAAAATGATCTCTGAAAGTGATATGACACCA
GCAGAACCAGTTACTGTCATCTTATCAGAAATGGGCTGGGTACGTTGTGCAAAAGGACAC
GATATTGATCCTAAATCATTAAGCTACAAAGCTGGTGATAGCTATCTAGCTCACGCTTGT
GGCAAAAGTAATCAAGCCGTTGTATTCATTGATAGCACGGGGCGGAGTTATGCACTCGAT
CCGCTTTCCTTGCCTTCCGCTCGCTCCCAAGGCGAACCACTTACAGGTAAACTCAATTTA
CCCACTGGTGCGACCATTGAATATGTTGTAATGGCCAGCGAACAGCAAGAATTATTGATG
GCTTCTGATGCAGGATATGGTTTTATTTGTAAATTTGAAGATTTAATTGCACGTAACAAG
GCTGGAAAAGCCTTGATTTCTTTACCAGAAAATGCCAAAGTGTTGAAGCCTAAAACATTG
ATAAATTCTACCGCACTTGTTGTCGCAATCACATCAGCAGGCAGAATGTTGATTTTTCCA
GCACAGGATTTACCGGTATTATCAAAAGGTAAAGGCAATAAAATGATCACTATTCCCGCA
GCGAATGCAAAAGATCGTAGCGAACTATTGACAAAATTATTGCTTATTTCAGATCAAGCA
AGTCTTGAATTTTATTCTGGAAAACGAAAAATTGTATTAAAACCAGAAGATCTGCAAAAG
TTCCGCGCAGAACGAGGCAGAAAAGGTTCGACATTACCACGTGGATTACATACCAATCTT
GAAATTATGGTAATCGAGCCGTAA
Target 2 GenBank Gene ID
Target 2 GeneCard ID Not Available
Target 2 GenAtlas ID Not Available
Target 2 HGNC ID Not Available
Target 2 Chromosome Location Not Available
Target 2 Locus Not Available
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Fleischmann RD, Adams MD, White O, Clayton RA, Kirkness EF, Kerlavage AR, Bult CJ, Tomb JF, Dougherty BA, Merrick JM, et al.: Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. Science. 1995 Jul 28;269(5223):496-512. [PubMed Link Image]
Target 2 Drug References
  1. Ruiz J, Jurado A, Garcia-Mendez E, Marco F, Aguilar L, Jimenez de Anta MT, Vila J: Frequency of selection of fluoroquinolone-resistant mutants of Neisseria gonorrhoeae exposed to gemifloxacin and four other quinolones. J Antimicrob Chemother. 2001 Oct;48(4):545-8. [PubMed Link Image]
  2. Daporta MT, Munoz Bellido JL, Guirao GY, Hernandez MS, Garcia-Rodriguez JA: In vitro activity of older and newer fluoroquinolones against efflux-mediated high-level ciprofloxacin-resistant Streptococcus pneumoniae. Int J Antimicrob Agents. 2004 Aug;24(2):185-7. [PubMed Link Image]
  3. Rafii F, Park M, Novak JS: Alterations in DNA gyrase and topoisomerase IV in resistant mutants of Clostridium perfringens found after in vitro treatment with fluoroquinolones. Antimicrob Agents Chemother. 2005 Feb;49(2):488-92. [PubMed Link Image]
  4. 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]
  5. 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]
Drug Target 3 [top]
Target 3 ID 817
Target 3 Name DNA topoisomerase 2-alpha
Target 3 Synonyms
  1. DNA topoisomerase II, alpha isozyme
  2. EC 5.99.1.3
Target 3 Gene Name TOP2A
Target 3 Protein Sequence >DNA topoisomerase 2-alpha 
MEVSPLQPVNENMQVNKIKKNEDAKKRLSVERIYQKKTQLEHILLRPDTYIGSVELVTQQ
MWVYDEDVGINYREVTFVPGLYKIFDEILVNAADNKQRDPKMSCIRVTIDPENNLISIWN
NGKGIPVVEHKVEKMYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVE
TASREYKKMFKQTWMDNMGRAGEMELKPFNGEDYTCITFQPDLSKFKMQSLDKDIVALMV
RRAYDIAGSTKDVKVFLNGNKLPVKGFRSYVDMYLKDKLDETGNSLKVIHEQVNHRWEVC
LTMSEKGFQQISFVNSIATSKGGRHVDYVADQIVTKLVDVVKKKNKGGVAVKAHQVKNHM
WIFVNALIENPTFDSQTKENMTLQPKSFGSTCQLSEKFIKAAIGCGIVESILNWVKFKAQ
VQLNKKCSAVKHNRIKGIPKLDDANDAGGRNSTECTLILTEGDSAKTLAVSGLGVVGRDK
YGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKNYEDEDSLKTLRYGKIMIMT
DQDQDGSHIKGLLINFIHHNWPSLLRHRFLEEFITPIVKVSKNKQEMAFYSLPEFEEWKS
STPNHKKWKVKYYKGLGTSTSKEAKEYFADMKRHRIQFKYSGPEDDAAISLAFSKKQIDD
RKEWLTNFMEDRRQRKLLGLPEDYLYGQTTTYLTYNDFINKELILFSNSDNERSIPSMVD
GLKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSSYHHGEMSLMMTIINLAQNFVGSNN
LNLLQPIGQFGTRLHGGKDSASPRYIFTMLSSLARLLFPPKDDHTLKFLYDDNQRVEPEW
YIPIIPMVLINGAEGIGTGWSCKIPNFDVREIVNNIRRLMDGEEPLPMLPSYKNFKGTIE
ELAPNQYVISGEVAILNSTTIEISELPVRTWTQTYKEQVLEPMLNGTEKTPPLITDYREY
HTDTTVKFVVKMTEEKLAEAERVGLHKVFKLQTSLTCNSMVLFDHVGCLKKYDTVLDILR
DFFELRLKYYGLRKEWLLGMLGAESAKLNNQARFILEKIDGKIIIENKPKKELIKVLIQR
GYDSDPVKAWKEAQQKVPDEEENEESDNEKETEKSDSVTDSGPTFNYLLDMPLWYLTKEK
KDELCRLRNEKEQELDTLKRKSPSDLWKEDLATFIEELEAVEAKEKQDEQVGLPGKGGKA
KGKKTQMAEVLPSPRGQRVIPRITIEMKAEAEKKNKKKIKNENTEGSPQEDGVELEGLKQ
RLEKKQKREPGTKTKKQTTLAFKPIKKGKKRNPWSDSESDRSSDESNFDVPPRETEPRRA
ATKTKFTMDLDSDEDFSDFDEKTDDEDFVPSDASPPKTKTSPKLSNKELKPQKSVVSDLE
ADDVKGSVPLSSSPPATHFPDETEITNPVPKKNVTVKKTAAKSQSSTSTTGAKKRAAPKG
TKRDPALNSGVSQKPDPAKTKNRRKRKPSTSDDSDSNFEKIVSKAVTSKKSKGESDDFHM
DFDSAVAPRAKSVRAKKPIKYLEESDEDDLF
Target 3 Number of Residues 1556
Target 3 Molecular Weight 174387
Target 3 Theoretical pI 9.17
Target 3 GO Classification
Function
DNA topoisomerase (ATP-hydrolyzing) activity
DNA topoisomerase activity
DNA topoisomerase (ATP-hydrolyzing) activity
nucleic acid binding
DNA binding
binding
nucleotide binding
purine nucleotide binding
adenyl nucleotide binding
ATP binding
Process
DNA topological change
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
DNA metabolism
Component
Not Available
Target 3 General Function Replication, recombination and repair
Target 3 Specific Function Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks
Target 3 Pathways Not Available
Target 3 Reactions
  • ATP-dependent breakage, passage and rejoining of double-stranded DNA INHIBITOR Coumermycin A1; GRI22222X; Nalidixic acid; Novobiocin; Ciprofloxacin
Target 3 Pfam Domain Function
Target 3 Signals
  • None
Target 3 Transmembrane Regions
  • None
Target 3 Essentiality Non-Essential
Target 3 GenBank ID Protein 292830 Link Image
Target 3 UniProtKB/Swiss-Prot ID P11388 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name TOP2A_HUMAN Link Image
Target 3 PDB ID Not Available
Target 3 Cellular Location
  • Cytoplasm. Nucleus
  • nucleoplasm. Generally located in the nucleoplasm
Target 3 Gene Sequence >4596 bp 
ATGGAAGTGTCACCATTGCAGCCTGTAAATGAAAATATGCAAGTCAACAAAATAAAGAAA
AATGAAGATGCTAAGAAAAGACTGTCTGTTGAAAGAATCTATCAAAAGAAAACACAATTG
GAACATATTTTGCTCCGCCCAGACACCTACATTGGTTCTGTGGAATTAGTGACCCAGCAA
ATGTGGGTTTACGATGAAGATGTTGGCATTAACTATAGGGAAGTCACTTTTGTTCCTGGT
TTGTACAAAATCTTTGATGAGATTCTAGTTAATGCTGCGGACAACAAACAAAGGGACCCA
AAAATGTCTTGTATTAGAGTCACAATTGATCCGGAAAACAATTTAATTAGTATATGGAAT
AATGGAAAAGGTATTCCTGTTGTTGAACACAAAGTTGAAAAGATGTATGTCCCAGCTCTC
ATATTTGGACAGCTCCTAACTTCTAGTAACTATGATGATGATGAAAAGAAAGTGACAGGT
GGTCGAAATGGCTATGGAGCCAAATTGTGTAACATATTCAGTACCAAATTTACTGTGGAA
ACAGCCAGTAGAGAATACAAGAAAATGTTCAAACAGACATGGATGGATAATATGGGAAGA
GCTGGTGAGATGGAACTCAAGCCCTTCAATGGAGAAGATTATACATGTATCACCTTTCAG
CCTGATTTGTCTAAGTTTAAAATGCAAAGCCTGGACAAAGATATTGTTGCACTAATGGTC
AGAAGAGCATATGATATTGCTGGATCCACCAAAGATGTCAAAGTCTTTCTTAATGGAAAT
AAACTGCCAGTAAAAGGATTTCGTAGTTATGTGGACATGTATTTGAAGGACAAGTTGGAT
GAAACTGGTAACTCCTTGAAAGTAATACATGAACAAGTAAACCACAGGTGGGAAGTGTGT
TTAACTATGAGTGAAAAAGGCTTTCAGCAAATTAGCTTTGTCAACAGCATTGCTACATCC
AAGGGTGGCAGACATGTTGATTATGTAGCTGATCAGATTGTGACTAAACTTGTTGATGTT
GTGAAGAAGAAGAACAAGGGTGGTGTTGCAGTAAAAGCACATCAGGTGAAAAATCACATG
TGGATTTTTGTAAATGCCTTAATTGAAAACCCAACCTTTGACTCTCAGACAAAAGAAAAC
ATGACTTTACAACCCAAGAGCTTTGGATCAACATGCCAATTGAGTGAAAAATTTATCAAA
GCTGCCATTGGCTGTGGTATTGTAGAAAGCATACTAAACTGGGTGAAGTTTAAGGCCCAA
GTCCAGTTAAACAAGAAGTGTTCAGCTGTAAAACATAATAGAATCAAGGGAATTCCCAAA
CTCGATGATGCCAATGATGCAGGGGGCCGAAACTCCACTGAGTGTACGCTTATCCTGACT
GAGGGAGATTCAGCCAAAACTTTGGCTGTTTCAGGCCTTGGTGTGGTTGGGAGAGACAAA
TATGGGGTTTTCCCTCTTAGAGGAAAAATACTCAATGTTCGAGAAGCTTCTCATAAGCAG
ATCATGGAAAATGCTGAGATTAACAATATCATCAAGATTGTGGGTCTTCAGTACAAGAAA
AACTATGAAGATGAAGATTCATTGAAGACGCTTCGTTATGGGAAGATAATGATTATGACA
GATCAGGACCAAGATGGTTCCCACATCAAAGGCTTGCTGATTAATTTTATCCATCACAAC
TGGCCCTCTCTTCTGCGACATCGTTTTCTGGAGGAATTTATCACTCCCATTGTAAAGGTA
TCTAAAAACAAGCAAGAAATGGCATTTTACAGCCTTCCTGAATTTGAAGAGTGGAAGAGT
TCTACTCCAAATCATAAAAAATGGAAAGTCAAATATTACAAAGGTTTGGGCACCAGCACA
TCAAAGGAAGCTAAAGAATACTTTGCAGATATGAAAAGACATCGTATCCAGTTCAAATAT
TCTGGTCCTGAAGATGATGCTGCTATCAGCCTGGCCTTTAGCAAAAAACAGATAGATGAT
CGAAAGGAATGGTTAACTAATTTCATGGAGGATAGAAGACAACGAAAGTTACTTGGGCTT
CCTGAGGATTACTTGTATGGACAAACTACCACATATCTGACATATAATGACTTCATCAAC
AAGGAACTTATCTTGTTCTCAAATTCTGATAACGAGAGATCTATCCCTTCTATGGTGGAT
GGTTTGAAACCAGGTCAGAGAAAGGTTTTGTTTACTTGCTTCAAACGGAATGACAAGCGA
GAAGTAAAGGTTGCCCAATTAGCTGGATCAGTGGCTGAAATGTCTTCTTATCATCATGGT
GAGATGTCACTAATGATGACCATTATCAATTTGGCTCAGAATTTTGTGGGTAGCAATAAT
CTAAACCTCTTGCAGCCCATTGGTCAGTTTGGTACCAGGCTACATGGTGGCAAGGATTCT
GCTAGTCCACGATACATCTTTACAATGCTCAGCTCTTTGGCTCGATTGTTATTTCCACCA
AAAGATGATCACACGTTGAAGTTTTTATATGATGACAACCAGCGTGTTGAGCCTGAATGG
TACATTCCTATTATTCCCATGGTGCTGATAAATGGTGCTGAAGGAATCGGTACTGGGTGG
TCCTGCAAAATCCCCAACTTTGATGTGCGTGAAATTGTAAATAACATCAGGCGTTTGATG
GATGGAGAAGAACCTTTGCCAATGCTTCCAAGTTACAAGAACTTCAAGGGTACTATTGAA
GAACTGGCTCCAAATCAATATGTGATTAGTGGTGAAGTAGCTATTCTTAATTCTACAACC
ATTGAAATCTCAGAGCTTCCCGTCAGAACATGGACCCAGACATACAAAGAACAAGTTCTA
GAACCCATGTTGAATGGCACCGAGAAGACACCTCCTCTCATAACAGACTATAGGGAATAC
CATACAGATACCACTGTGAAATTTGTTGTGAAGATGACTGAAGAAAAACTGGCAGAGGCA
GAGAGAGTTGGACTACACAAAGTCTTCAAACTCCAAACTAGTCTCACATGCAACTCTATG
GTGCTTTTTGACCACGTAGGCTGTTTAAAGAAATATGACACGGTGTTGGATATTCTAAGA
GACTTTTTTGAACTCAGACTTAAATATTATGGATTAAGAAAAGAATGGCTCCTAGGAATG
CTTGGTGCTGAATCTGCTAAACTGAATAATCAGGCTCGCTTTATCTTAGAGAAAATAGAT
GGCAAAATAATCATTGAAAATAAGCCTAAGAAAGAATTAATTAAAGTTCTGATTCAGAGG
GGATATGATTCGGATCCTGTGAAGGCCTGGAAAGAAGCCCAGCAAAAGGTTCCAGATGAA
GAAGAAAATGAAGAGAGTGACAACGAAAAGGAAACTGAAAAGAGTGACTCCGTAACAGAT
TCTGGACCAACCTTCAACTATCTTCTTGATATGCCCCTTTGGTATTTAACCAAGGAAAAG
AAAGATGAACTCTGCAGGCTAAGAAATGAAAAAGAACAAGAGCTGGACACATTAAAAAGA
AAGAGTCCATCAGATTTGTGGAAAGAAGACTTGGCTACATTTATTGAAGAATTGGAGGCT
GTTGAAGCCAAGGAAAAACAAGATGAACAAGTCGGACTTCCTGGGAAAGGGGGGAAGGCC
AAGGGGAAAAAAACACAAATGGCTGAAGTTTTGCCTTCTCCGCGTGGTCAAAGAGTCATT
CCACGAATAACCATAGAAATGAAAGCAGAGGCAGAAAAGAAAAATAAAAAGAAAATTAAG
AATGAAAATACTGAAGGAAGCCCTCAAGAAGATGGTGTGGAACTAGAAGGCCTAAAACAA
AGATTAGAAAAGAAACAGAAAAGAGAACCAGGTACAAAGACAAAGAAACAAACTACATTG
GCATTTAAGCCAATCAAAAAAGGAAAGAAGAGAAATCCCTGGCCTGATTCAGAATCAGAT
AGGAGCAGTGACGAAAGTAATTTTGATGTCCCTCCACGAGAAACAGAGCCACGGAGAGCA
GCAACAAAAACAAAATTCACAATGGATTTGGATTCAGATGAAGATTTCTCAGATTTTGAT
GAAAAAACTGATGATGAAGATTTTGTCCCATCAGATGCTAGTCCACCTAAGACCAAAACT
TCCCCAAAACTTAGTAACAAAGAACTGAAACCACAGAAAAGTGTCGTGTCAGACCTTGAA
GCTGATGATGTTAAGGGCAGTGTACCACTGTCTTCAAGCCCTCCTGCTACACATTTCCCA
GATGAAACTGAAATTACAAACCCAGTTCCTAAAAAGAATGTGACAGTGAAGAAGACAGCA
GCAAAAAGTCAGTCTTCCACCTCCACTACCGGTGCCAAAAAAAGGGCTGCCCCAAAAGGA
ACTAAAAGGGATCCAGCTTTGAATTCTGGTGTCTCTCAAAAGCCTGATCCTGCCAAAACC
AAGAATCGCCGCAAAAGGAAGCCATCCACTTCTGATGATTCTGACTCTAATTTTGAGAAA
ATTGTTTCGAAAGCAGTCACAAGCAAGAAATCCAAGGGGGAGAGTGATGACTTCCATATG
GACTTTGACTCAGCTGTGGCTCCTCGGGCAAAATCTGTACGGGCAAAGAAACCTATAAAG
TACCTGGAAGAGTCAGATGAAGATGATCTGTTTTAA
Target 3 GenBank Gene ID
Target 3 GeneCard ID TOP2A Link Image
Target 3 GenAtlas ID TOP2A Link Image
Target 3 HGNC ID HGNC:11989 Link Image
Target 3 Chromosome Location 17
Target 3 Locus 17q21-q22
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Sng JH, Heaton VJ, Bell M, Maini P, Austin CA, Fisher LM: Molecular cloning and characterization of the human topoisomerase IIalpha and IIbeta genes: evidence for isoform evolution through gene duplication. Biochim Biophys Acta. 1999 Mar 19;1444(3):395-406. [PubMed Link Image]
  2. Escargueil AE, Plisov SY, Filhol O, Cochet C, Larsen AK: Mitotic phosphorylation of DNA topoisomerase II alpha by protein kinase CK2 creates the MPM-2 phosphoepitope on Ser-1469. J Biol Chem. 2000 Nov 3;275(44):34710-8. [PubMed Link Image]
  3. Mirski SE, Bielawski JC, Cole SP: Identification of functional nuclear export sequences in human topoisomerase IIalpha and beta. Biochem Biophys Res Commun. 2003 Jul 11;306(4):905-11. [PubMed Link Image]
  4. Hinds M, Deisseroth K, Mayes J, Altschuler E, Jansen R, Ledley FD, Zwelling LA: Identification of a point mutation in the topoisomerase II gene from a human leukemia cell line containing an amsacrine-resistant form of topoisomerase II. Cancer Res. 1991 Sep 1;51(17):4729-31. [PubMed Link Image]
  5. Bugg BY, Danks MK, Beck WT, Suttle DP: Expression of a mutant DNA topoisomerase II in CCRF-CEM human leukemic cells selected for resistance to teniposide. Proc Natl Acad Sci U S A. 1991 Sep 1;88(17):7654-8. [PubMed Link Image]
  6. Tsai-Pflugfelder M, Liu LF, Liu AA, Tewey KM, Whang-Peng J, Knutsen T, Huebner K, Croce CM, Wang JC: Cloning and sequencing of cDNA encoding human DNA topoisomerase II and localization of the gene to chromosome region 17q21-22. Proc Natl Acad Sci U S A. 1988 Oct;85(19):7177-81. [PubMed Link Image]
  7. Wasserman RA, Austin CA, Fisher LM, Wang JC: Use of yeast in the study of anticancer drugs targeting DNA topoisomerases: expression of a functional recombinant human DNA topoisomerase II alpha in yeast. Cancer Res. 1993 Aug 1;53(15):3591-6. [PubMed Link Image]
  8. Lang AJ, Mirski SE, Cummings HJ, Yu Q, Gerlach JH, Cole SP: Structural organization of the human TOP2A and TOP2B genes. Gene. 1998 Oct 23;221(2):255-66. [PubMed Link Image]
Target 3 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]

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