Drugbank Logo

Showing drug card for Levofloxacin (DB01137)

Legend: drug field target field enzyme field

for drugs
Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-02-19 16:04:10
Primary Accession Number DB01137
Secondary Accession Number
  • APRD00477
Name Levofloxacin
Drug Type
  • Approved
  • Investigational
  • Small Molecule
Description A synthetic fluoroquinolone (fluoroquinolones) antibacterial agent that inhibits the supercoiling activity of bacterial DNA gyrase, halting DNA replication. [PubChem]
Synonyms
  1. L-Ofloxacin
  2. levofloxacin
Brand Names
  1. Cravit
  2. Cravit Ophthalmic
  3. Elequine
  4. Floxel
  5. Iquix
  6. Leroxacin
  7. Lesacin
  8. Levaquin
  9. Levokacin
  10. Levox
  11. Levoxacin
  12. Mosardal
  13. Nofaxin
  14. Quixin
  15. Reskuin
  16. Tavanic
  17. Volequin
Brand Mixtures Not Available
Chemical IUPAC Name (-)-(S)-9-fluoro-2,3-dihydro-3-methyl-10-(4-methyl-1-piperazinyl)-7-oxo-7Hpyrido[1,2,3-de]-1,4 benzoxazine-6-carboxylic acid hemihydrate
Chemical Formula C18H20FN3O4
Chemical Structure Structure
CAS Registry Number 100986-85-4
InChI Identifier InChI=1/C18H20FN3O4/c1-10-9-26-17-14-11(16(23)12(18(24)25)8-22(10)14)7-13(19)15(17)21-5-3-20(2)4-6-21/h7-8,10H,3-6,9H2,1-2H3,(H,24,25)/t10-/m0/s1/f/h24H
InChI Key GSDSWSVVBLHKDQ-QVNXLTHBDA
KEGG Drug Not Available
KEGG Compound C07660 Link Image
PubChem Compound 149096 Link Image
PubChem Substance 195031 Link Image
ChEBI ID Not Available
PharmGKB ID PA450214 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 02248263 Link Image
RxList Link http://www.rxlist.com/cgi/generic2/quixin.htm Link Image
PDRhealth Link http://www.pdrhealth.com/drug_info/rxdrugprofiles/drugs/flo1181.shtml Link Image
Wikipedia Link http://en.wikipedia.org/wiki/Levofloxacin Link Image
FDA Label
Material Safety Data Sheet (MSDS) Not Available
Synthesis Reference Mitscher, Lester A. et al.; J.Med.Chem.; 30; 12; 2283-2286(1987)
Average Molecular Weight 361.3675
Monoisotopic Molecular Weight 361.1438
State Solid
Melting Point Not Available
Experimental Water Solubility Insoluble Source: PhysProp
Predicted Water Solubility 1.44e+00 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 2.1 Source: PhysProp
Predicted LogP -0.02 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -2.40 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 C[C@H]1COC2=C3N1C=C(C(O)=O)C(=O)C3=CC(F)=C2N1CCN(C)CC1
Canonical SMILES CC1COC2=C3N1C=C(C(O)=O)C(=O)C3=CC(F)=C2N1CCN(C)CC1
Drug Category
  • Anti-Bacterial Agents
  • Anti-Infective Agents, Urinary
  • Nucleic Acid Synthesis Inhibitors
  • Quinolones
ATC Codes
AHFS Codes
  • 08:12.18
Indication For the treatment of bacterial conjunctivitis caused by susceptible strains of the following organisms: Corynebacterium species, Staphylococus aureus, Staphylococcus epidermidis, Streptococcus pneumoniae, Streptococcus (Groups C/F/G), Viridans group streptococci, Acinetobacter lwoffii, Haemophilus influenzae, Serratia marcescens.
Pharmacology Levofloxacin, a fluoroquinolone antiinfective, is the optically active L-isomer of ofloxacin. Levofloxacin is used to treat bacterial conjunctivitis, sinusitis, chronic bronchitis, community-acquired pneumonia and pneumonia caused by penicillin-resistant strains of Streptococcus pneumoniae, skin and skin structure infections, complicated urinary tract infections and acute pyelonephritis.
Mechanism of Action Levofloxacin inhibits bacterial type II topoisomerases, topoisomerase IV and DNA gyrase. Levofloxacin, like other fluoroquinolones, inhibits the A subunits of DNA gyrase, two subunits encoded by the gyrA gene. This results in strand breakage on a bacterial chromosome, supercoiling, and resealing; DNA replication and transcription is inhibited.
Absorption Absorption of ofloxacin after single or multiple doses of 200 to 400 mg is predictable, and the amount of drug absorbed increases proportionately with the dose.
Toxicity Side effects include disorientation, dizziness, drowsiness, hot and cold flashes, nausea, slurring of speech, swelling and numbness in the face
Protein Binding 24-38% (to plasma proteins)
Biotransformation Not Available
Half Life 6-8 hours
Dosage Forms
Form Route
Solution Intravenous
Tablet Oral
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Acenocoumarol The quinolone increases the anticoagulant effect
Aluminium Formation of non-absorbable complexes
Amiodarone Increased risk of cardiotoxicity and arrhythmias
Anisindione The quinolone increases the anticoagulant effect
Bepridil Increased risk of cardiotoxicity and arrhythmias
Bismuth Formation of non-absorbable complexes
Bretylium Increased risk of cardiotoxicity and arrhythmias
Calcium Formation of non-absorbable complexes
Chlorpromazine Increased risk of cardiotoxicity and arrhythmias
Dicumarol The quinolone increases the anticoagulant effect
Dihydroquinidine barbiturate Increased risk of cardiotoxicity and arrhythmias
Disopyramide Increased risk of cardiotoxicity and arrhythmias
Erythromycin Increased risk of cardiotoxicity and arrhythmias
Fluphenazine Increased risk of cardiotoxicity and arrhythmias
Iron Formation of non-absorbable complexes
Josamycin Increased risk of cardiotoxicity and arrhythmias
Magnesium Formation of non-absorbable complexes
Magnesium oxide Formation of non-absorbable complexes
Mesoridazine Increased risk of cardiotoxicity and arrhythmias
Methotrimeprazine Increased risk of cardiotoxicity and arrhythmias
Perphenazine Increased risk of cardiotoxicity and arrhythmias
Procainamide The quinolone increases the effect of procainamide
Prochlorperazine Increased risk of cardiotoxicity and arrhythmias
Promazine Increased risk of cardiotoxicity and arrhythmias
Promethazine Increased risk of cardiotoxicity and arrhythmias
Propiomazine Increased risk of cardiotoxicity and arrhythmias
Quinidine Increased risk of cardiotoxicity and arrhythmias
Quinidine barbiturate Increased risk of cardiotoxicity and arrhythmias
Quinupristin This combination presents an increased risk of toxicity
Sotalol Increased risk of cardiotoxicity and arrhythmias
Sucralfate Formation of non-absorbable complexes
Thiethylperazine Increased risk of cardiotoxicity and arrhythmias
Thioridazine Increased risk of cardiotoxicity and arrhythmias
Trifluoperazine Increased risk of cardiotoxicity and arrhythmias
Triflupromazine Increased risk of cardiotoxicity and arrhythmias
Warfarin The quinolone increases the anticoagulant effect
Zinc Formation of non-absorbable complexes
Food Interactions
  • Take without regard to meals. Take with water, drink lliberally. Taking this product with orange juice can result in reduced quinolone plasma levels.
Pathways Not Available
General References
  1. Drugs.com Link Image
  2. Wikipedia Link Image
  3. RxList Link Image
  4. PDRhealth Link Image
Organisms Affected
  • Enteric bacteria and other eubacteria
Phase 1 Metabolizing Enzymes
  1. Cytochrome P450 1A2 (CYP1A2)
Targets
  1. DNA gyrase subunit A
  2. DNA topoisomerase 4 subunit A
  3. DNA topoisomerase 2-alpha
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name Cytochrome P450 1A2 (CYP1A2)
Enzyme 1 Gene Name CYP1A2
Enzyme 1 SwissProt ID P05177 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 Protein Sequence >P05177|CP1A2_HUMAN Cytochrome P450 1A2 - Homo sapiens (Human). 
MALSQSVPFSATELLLASAIFCLVFWVLKGLRPRVPKGLKSPPEPWGWPLLGHVLTLGKN
PHLALSRMSQRYGDVLQIRIGSTPVLVLSRLDTIRQALVRQGDDFKGRPDLYTSTLITDG
QSLTFSTDSGPVWAARRRLAQNALNTFSIASDPASSSSCYLEEHVSKEAKALISRLQELM
AGPGHFDPYNQVVVSVANVIGAMCFGQHFPESSDEMLSLVKNTHEFVETASSGNPLDFFP
ILRYLPNPALQRFKAFNQRFLWFLQKTVQEHYQDFDKNSVRDITGALFKHSKKGPRASGN
LIPQEKIVNLVNDIFGAGFDTVTTAISWSLMYLVTKPEIQRKIQKELDTVIGRERRPRLS
DRPQLPYLEAFILETFRHSSFLPFTIPHSTTRDTTLNGFYIPKKCCVFVNQWQVNHDPEL
WEDPSEFRPERFLTADGTAINKPLSEKMMLFGMGKRRCIGEVLAKWEIFLFLAILLQQLE
FSVPPGVKVDLTPIYGLTMKHARCEHVQARRFSIN
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. 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]
  2. Messina C, Cafiso V, Campanile F, Santagati M, Stefani S: Rapid method for detection of gyrA and grlA mutations in unrelated strains of Staphylococci susceptible and resistant to levofloxacin. New Microbiol. 2001 Oct;24(4):347-53. [PubMed Link Image]
  3. 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]
  4. 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]
  5. Schmitz FJ, Hofmann B, Hansen B, Scheuring S, Luckefahr M, Klootwijk M, Verhoef J, Fluit A, Heinz HP, Kohrer K, Jones ME: Relationship between ciprofloxacin, ofloxacin, levofloxacin, sparfloxacin and moxifloxacin (BAY 12-8039) MICs and mutations in grlA, grlB, gyrA and gyrB in 116 unrelated clinical isolates of Staphylococcus aureus. J Antimicrob Chemother. 1998 Apr;41(4):481-4. [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. Zheng X, Johnson C, Lu Y, Yanagihara R, Hollingshead S, Crain M, Benjamin W Jr, Waites KB: Clinical isolates of Streptococcus pneumoniae resistant to levofloxacin contain mutations in both gyrA and parC genes. Int J Antimicrob Agents. 2001 Oct;18(4):373-8. [PubMed Link Image]
  2. Deryke CA, Du X, Nicolau DP: Evaluation of bacterial kill when modelling the bronchopulmonary pharmacokinetic profile of moxifloxacin and levofloxacin against parC-containing isolates of Streptococcus pneumoniae. J Antimicrob Chemother. 2006 Sep;58(3):601-9. Epub 2006 Jul 19. [PubMed Link Image]
  3. 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]
  4. 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]
  5. Schafer J, Hovde LB, Simonson D, Rotschafer JC: In vitro pharmacodynamics of moxifloxacin versus levofloxacin against 4 strains of Streptococcus pneumoniae: 1 wild type, 2 first-step parC mutants, and 1 pump mutant. Diagn Microbiol Infect Dis. 2007 Oct 1;. [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]

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.