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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-23 18:07:59
Primary Accession Number DB00198
Secondary Accession Number
  • APRD01148
Name Oseltamivir
Drug Type
  • Approved
  • Small Molecule
Description An acetamido cyclohexene that is a structural homolog of sialic acid and inhibits neuraminidase. [PubChem]
Synonyms
  1. Oseltamivir phosphate
Brand Names
  1. Tamiflu
Brand Mixtures Not Available
Chemical IUPAC Name ethyl (3R,4R,5S)-4-acetamido-5-amino-3-pentan-3-yloxycyclohexene-1-carboxylate
Chemical Formula C16H28N2O4
Chemical Structure Structure
CAS Registry Number 204255-11-8
InChI Identifier InChI=1/C16H28N2O4/c1-5-12(6-2)22-14-9-11(16(20)21-7-3)8-13(17)15(14)18-10(4)19/h9,12-15H,5-8,17H2,1-4H3,(H,18,19)/t13-,14+,15+/m0/s1/f/h18H
InChI Key VSZGPKBBMSAYNT-HRPFSUSRDU
KEGG Drug D00900 Link Image
KEGG Compound C08093 Link Image
PubChem Compound 65028 Link Image
PubChem Substance 626306 Link Image
ChEBI ID Not Available
PharmGKB ID PA450722 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 02245549 Link Image
RxList Link http://www.rxlist.com/cgi/generic3/oseltamiv.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Oseltamivir Link Image
FDA Label
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 312.4045
Monoisotopic Molecular Weight 312.2049
State Solid
Melting Point Not Available
Experimental Water Solubility Soluble Source: PhysProp
Predicted Water Solubility 6.86e-01 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 1 Source: PhysProp
Predicted LogP 1.30 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -2.66 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 CCOC(=O)C1=C[C@@H](OC(CC)CC)[C@H](NC(C)=O)[C@@H](N)C1
Canonical SMILES CCOC(=O)C1=CC(OC(CC)CC)C(NC(C)=O)C(N)C1
Drug Category
  • Antiviral Agents
  • Enzyme Inhibitors
ATC Codes
AHFS Codes
  • 08:18.28
Indication For the treatment of uncomplicated acute illness due to influenza infection in patients 1 year and older who have been symptomatic for no more than 2 days. Also for the prophylaxis of influenza in adult patients and adolescents 13 years and older.
Pharmacology Oseltamivir is an antiviral drug, a neuraminidase inhibitor used in the treatment and prophylaxis of both influenza A and influenza B. Oseltamivir is a prodrug (usually administered as phosphate), it is hydrolysed hepatically to the active metabolite, the free carboxylate of oseltamivir (GS4071). Like zanamivir, oseltamivir acts as a transition-state analogue inhibitor of influenza neuraminidase.
Mechanism of Action Oseltamivir is an ethyl ester prodrug requiring ester hydrolysis for conversion to the active form, oseltamivir carboxylate. The proposed mechanism of action of oseltamivir is inhibition of influenza virus neuraminidase with the possibility of alteration of virus particle aggregation and release.
Absorption Readily absorbed from the gastrointestinal tract after oral administration with a bioavailability of 75%.
Toxicity At present, there has been no experience with overdose. Single doses of up to 1000 mg of oseltamivir have been associated with nausea and/or vomiting. Mean LD (intravenous, mouse) = 100 mg/kg.
Protein Binding Oseltamivir carboxylate: low (3%), Oseltamivir free base: 42%.
Biotransformation Extensively converted to oseltamivir carboxylate by esterases located predominantly in the liver. Neither oseltamivir nor oseltamivir carboxylate is a substrate for, or inhibitor of, cytochrome P450 isoforms. At least 75% of an oral dose reaches the systemic circulation as oseltamivir carboxylate.
Half Life 1 to 3 hours in most subjects after oral administration.
Dosage Forms
Form Route
Capsule Oral
Capsule Oral
Powder, for suspension Oral
Powder, for suspension Oral
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions Not Available
Food Interactions
  • Take without regard to meals. Food may improve gastric tolerance.
Pathways Not Available
General References
  1. Kiso M, Mitamura K, Sakai-Tagawa Y, Shiraishi K, Kawakami C, Kimura K, Hayden FG, Sugaya N, Kawaoka Y: Resistant influenza A viruses in children treated with oseltamivir: descriptive study. Lancet. 2004 Aug 28-Sep 3;364(9436):759-65. [PubMed Link Image]
  2. Chokephaibulkit K, Uiprasertkul M, Puthavathana P, Chearskul P, Auewarakul P, Dowell SF, Vanprapar N: A child with avian influenza A (H5N1) infection. Pediatr Infect Dis J. 2005 Feb;24(2):162-6. [PubMed Link Image]
  3. Ward P, Small I, Smith J, Suter P, Dutkowski R: Oseltamivir (Tamiflu) and its potential for use in the event of an influenza pandemic. J Antimicrob Chemother. 2005 Feb;55 Suppl 1:i5-i21. [PubMed Link Image]
  4. de Jong MD, Tran TT, Truong HK, Vo MH, Smith GJ, Nguyen VC, Bach VC, Phan TQ, Do QH, Guan Y, Peiris JS, Tran TH, Farrar J: Oseltamivir resistance during treatment of influenza A (H5N1) infection. N Engl J Med. 2005 Dec 22;353(25):2667-72. [PubMed Link Image]
  5. Wikipedia Link Image
  6. RxList Link Image
Organisms Affected
  • Influenza Virus
Targets
  1. Neuraminidase
  2. Sialidase-1
Drug Target 1 [top]
Target 1 ID 641
Target 1 Name Neuraminidase
Target 1 Synonyms
  1. EC 3.2.1.18
Target 1 Gene Name NA
Target 1 Protein Sequence >Neuraminidase 
MNPNQKIITIGSICMTIGIISLILQIGNIISIWVSHSIQTGSQNHTGICNQRIITYENST
WVNQTYVNINNTNVVAGKDTTSVTLAGNSSLCPIRGWAIYSKDNSIRIGSKGDVFVIREP
FISCSHLECRTFFLTQGALLNDKHSNGTVKDRSPYRALMSCPIGEAPSPYNSRFESVAWS
ASACHDGMGWLTIGISGPDDGAVAVLKYNGIITETIKSWRKRILRTQESECVCVNGSCFT
IMTDGPSNGPASYRIFKIEKGKITKSIELDAPNSHYEECSCYPDTGTVMCVCRDNWHGSN
RPWVSFNQNLDYQIGYICSGVFGDNPRPKDGKGSCDPVTVDGADGVKGFSYRYGNGVWIG
RTKSNSSRKGFEMIWDPNGWTDTDSNFLVKQDVVAMTDWSGYSGSFVQHPELTGLDCMRP
CFWVELIRGRPREKTTIWTSGSSISFCGVNSDTANWSWPDGAELPFTIDK
Target 1 Number of Residues 477
Target 1 Molecular Weight 51875
Target 1 Theoretical pI 7.07
Target 1 GO Classification
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on glycosyl bonds
hydrolase activity, hydrolyzing O-glycosyl compounds
alpha-sialidase activity
exo-alpha-sialidase activity
Process
physiological process
metabolism
macromolecule metabolism
carbohydrate metabolism
Component
cell
membrane
Target 1 General Function Involved in exo-alpha-sialidase activity
Target 1 Specific Function Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft-association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication
Target 1 Pathways
Name SMPDB Link KEGG Link
Glycosphingolipid metabolism map00600 Link Image
N-Glycan degradation map00511 Link Image
Target 1 Reactions
  • Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates ALL_REAC (other) R03491 R04018 R04634 R04650 R05115 R05117 R05996(G) R05998(G) R05999(G) R06012(G) R06147(G) R06253(G) INHIBITOR 2-Deoxy-2,3-dehydro-N-acetylneuraminic acid
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • 7-35
Target 1 Essentiality Essential
Target 1 GenBank ID Protein 60811 Link Image
Target 1 UniProtKB/Swiss-Prot ID P11485 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name NRAM_IACHI Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location
  • Virion
  • apical cell membrane
  • single-pass type II membrane protein (
  • virion membrane. Cell membrane
Target 1 Gene Sequence >1413 bp 
ATGAATCCAAATCAGAAAATAATAACCATTGGATCAATCTGTATGACAATCGGAATAATT
AGTCTAATATTGCAAATAGGAAATATTATTTCAATATGGGTTAGCCACTCAATCCAAACT
GGAAGTCAAAACCACACTGGAATATGCAACCAAAGAATCATTACTTATGAAAATAGCACC
TGGGTAAATCAAACATATGTCAATATTAACAACACTAACGTTGTTGCTGGAAAGGACACA
ACTTCAGTGACATTAGCCGGCAATTCATCTCTTTGTCCTATCCGTGGGTGGGCTATATAC
AGCAAAGACAACAGCATAAGAATTGGTTCCAAAGGAGATGTTTTTGTCATAAGAGAACCT
TTTATATCATGTTCTCACTTGGAATGCAGAACCTTTTTTCTGACCCAAGGTGCTCTATTA
AATGACAAGCATTCAAATGGGACCGTTAAGGACAGAAGCCCTTATAGGGCCTTAATGAGC
TGTCCTATAGGTGAAGCTCCGTCTCCATACAATTCAAGGTTTGAATCAGTTGCTTGGTCA
GCAAGCGCATGTCATGATGGCATGGGCTGGCTAACAATCGGAATTTCTGGTCCAGATGAT
GGAGCAGTGGCTGTACTAAAATACAACGGCATAATAACTGAAACCATAAAAAGTTGGAGG
AAGCGAATATTAAGAACACAAGAGTCTGAATGTGTCTGTGTAAACGGTTCATGTTTTACC
ATAATGACCGATGGCCCGAGTAATGGACCTGCCTCGTACAGAATCTTCAAAATCGAGAAG
GGGAAGATTACTAAATCAATAGAGTTGGATGCACCCAATTCTCATTACGAGGAATGTTCC
TGTTACCCAGACACCGGCACAGTGATGTGTGTGTGCAGAGACAATTGGCATGGTTCGAAT
CGACCTTGGGTGTCTTTTAATCAAAACCTGGATTATCAAATAGGATACATCTGCAGTGGG
GTTTTCGGTGACAATCCGCGTCCCAAAGATGGAAAAGGCAGCTGTGATCCAGTAACTGTT
GATGGAGCAGACGGAGTAAAGGGGTTTTCATACAGGTATGGTAATGGTGTTTGGATAGGA
AGGACTAAAAGTAACAGCTCCAGAAAGGGATTTGAGATGATTTGGGATCCTAATGGATGG
ACAGATACCGATAGTAATTTCTTAGTGAAACAGGATGTAGTGGCAATGACTGATTGGTCA
GGGTACAGCGGAAGTTTCGTTCAACATCCTGAGCTAACAGGATTGGACTGTATGAGGCCT
TGCTTCTGGGTTGAATTAATCAGAGGACGACCTAGAGAAAAGACAACAATCTGGACTAGT
GGGAGCAGCATTTCTTTTTGTGGCGTGAATAGTGATACTGCAAATTGGTCTTGGCCAGAC
GGTGCCGAGTTGCCATTCACCATTGACAAGTAG
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. Schreier E, Roeske H, Driesel G, Kunkel U, Petzold DR, Berlinghoff R, Michel S: Complete nucleotide sequence of the neuraminidase gene of the human influenza virus A/Chile/1/83 (H1N1). Brief report. Arch Virol. 1988;99(3-4):271-6. [PubMed Link Image]
Target 1 Drug References
  1. Wang MZ, Tai CY, Mendel DB: Mechanism by which mutations at his274 alter sensitivity of influenza a virus n1 neuraminidase to oseltamivir carboxylate and zanamivir. Antimicrob Agents Chemother. 2002 Dec;46(12):3809-16. [PubMed Link Image]
  2. McKimm-Breschkin J, Trivedi T, Hampson A, Hay A, Klimov A, Tashiro M, Hayden F, Zambon M: Neuraminidase sequence analysis and susceptibilities of influenza virus clinical isolates to zanamivir and oseltamivir. Antimicrob Agents Chemother. 2003 Jul;47(7):2264-72. [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. Du QS, Wang SQ, Chou KC: Analogue inhibitors by modifying oseltamivir based on the crystal neuraminidase structure for treating drug-resistant H5N1 virus. Biochem Biophys Res Commun. 2007 Oct 19;362(2):525-31. Epub 2007 Aug 13. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 1141
Target 2 Name Sialidase-1
Target 2 Synonyms
  1. Acetylneuraminyl hydrolase
  2. EC 3.2.1.18
  3. G9 sialidase
  4. Lysosomal sialidase
  5. N-acetyl- alpha-neuraminidase 1
  6. Sialidase-1 precursor
Target 2 Gene Name NEU1
Target 2 Protein Sequence >Sialidase-1 precursor 
MTGERPSTALPDRRWGPRILGFWGGCRVWVFAAIFLLLSLAASWSKAENDFGLVQPLVTM
EQLLWVSGRQIGSVDTFRIPLITATPRGTLLAFAEARKMSSSDEGAKFIALRRSMDQGST
WSPTAFIVNDGDVPDGLNLGAVVSDVETGVVFLFYSLCAHKAGCQVASTMLVWSKDDGVS
WSTPRNLSLDIGTEVFAPGPGSGIQKQREPRKGRLIVCGHGTLERDGVFCLLSDDHGASW
RYGSGVSGIPYGQPKQENDFNPDECQPYELPDGSVVINARNQNNYHCHCRIVLRSYDACD
TLRPRDVTFDPELVDPVVAAGAVVTSSGIVFFSNPAHPEFRVNLTLRWSFSNGTSWRKET
VQLWPGPSGYSSLATLEGSMDGEEQAPQLYVLYEKGRNHYTESISVAKISVYGTL
Target 2 Number of Residues 421
Target 2 Molecular Weight 45468
Target 2 Theoretical pI 5.68
Target 2 GO Classification Not Available
Target 2 General Function Involved in exo-alpha-sialidase activity
Target 2 Specific Function Catalyzes the removal of sialic acid (N-acetylneuramic acid) moities from glycoproteins and glycolipids. To be active, it is strictly dependent on its presence in the multienzyme complex. Appears to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage
Target 2 Pathways
Name SMPDB Link KEGG Link
N-Glycan degradation map00511 Link Image
Target 2 Reactions
  • Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates ALL_REAC (other) R03491 R04018 R04634 R04650 R05115 R05117 R05996(G) R05998(G) R05999(G) R06012(G) R06147(G) R06253(G) INHIBITOR 2-Deoxy-2,3-dehydro-N-acetylneuraminic acid
Target 2 Pfam Domain Function
Target 2 Signals
  • 1-47
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 2773339 Link Image
Target 2 UniProtKB/Swiss-Prot ID Q99519 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name NEUR1_HUMAN Link Image
Target 2 PDB ID Not Available
Target 2 Cellular Location
  • Lysosome
  • lumenal side. Lysosome
  • lysosomal lumen.
  • lysosomal membrane
  • peripheral membrane protein
Target 2 Gene Sequence >1248 bp 
ATGACTGGGGAGCGACCCAGCACGGCGCTCCCGGACAGACGCTGGGGGCCGCGGATTCTG
GGCTTCTGGGGAGGCTGTAGGGTTTGGGTGTTTGCCGCGATCTTCCTGCTGCTGTCTCTG
GCAGCCTCCTGGTCCAAGGCTGAGAACGACTTCGGTCTGGTGCAGCCGCTGGTGACCATG
GAGCAACTGCTGTGGGTGAGCGGGAGACAGATCGGCTCAGTGGACACCTTCCGCATCCCG
CTCATCACAGCCACTCCGCGGGGCACTCTTCTCGCCTTTGCTGAGGCGAGGAAAATGTCC
TCATCCGATGAGGGGGCCAAGTTCATCGCCCTGCGGAGGTCCATGGACCAGGGCAGCACA
TGGTCTCCTACAGCGTTCATTGTCAATGATGGGGATGTCCCCGATGGGCTGAACCTTGGG
GCAGTAGTGAGCGATGTTGAGACAGGAGTAGTATTTCTTTTCTACTCCCTTTGTGCTCAC
AAGGCCGGCTGCCAGGTGGCCTCTACCATGTTGGTATGGAGCAAGGATGATGGTGTTTCC
TGGAGCACACCCCGGAATCTCTCCCTGGATATTGGCACTGAAGTGTTTGCCCCTGGACCG
GGCTCTGGTATTCAGAAACAGCGGGAGCCACGGAAGGGCCGCCTCATCGTGTGTGGCCAT
GGGACGCTGGAGCGGGACGGAGTCTTCTGTCTCCTCAGCGATGATCATGGTGCCTCCTGG
CGCTACGGAAGTGGGGTCAGCGGCATCCCCTACGGTCAGCCCAAGCAGGAAAATGATTTC
AATCCTGATGAATGCCAGCCCTATGAGCTCCCAGATGGCTCAGTCGTCATCAATGCCCGA
AACCAGAACAACTACCACTGCCACTGCCGAATTGTCCTCCGCAGCTATGATGCCTGTGAT
ACACTAAGGCCCCGTGATGTGACCTTCGACCCTGAGCTCGTGGACCCTGTGGTAGCTGCA
GGAGCTGTAGTCACCAGCTCCGGCATTGTCTTCTTCTCCAACCCAGCACATCCAGAGTTC
CGAGTGAACCTGACCCTGCGATGGAGCTTCAGCAATGGTACCTCATGGCGGAAAGAGACA
GTCCAGCTATGGCCAGGCCCCAGTGGCTATTCATCCCTGGCAACCCTGGAGGGCAGCATG
GATGGAGAGGAGCAGGCCCCCCAGCTCTACGTCCTGTATGAGAAAGGCCGGAACCACTAC
ACAGAGAGCATCTCCGTGGCCAAAATCAGTGTCTATGGGACACTCTGA
Target 2 GenBank Gene ID
Target 2 GeneCard ID NEU1 Link Image
Target 2 GenAtlas ID NEU1 Link Image
Target 2 HGNC ID HGNC:7758 Link Image
Target 2 Chromosome Location 6
Target 2 Locus 6p21.3
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Lukong KE, Elsliger MA, Chang Y, Richard C, Thomas G, Carey W, Tylki-Szymanska A, Czartoryska B, Buchholz T, Criado GR, Palmeri S, Pshezhetsky AV: Characterization of the sialidase molecular defects in sialidosis patients suggests the structural organization of the lysosomal multienzyme complex. Hum Mol Genet. 2000 Apr 12;9(7):1075-85. [PubMed Link Image]
  2. Naganawa Y, Itoh K, Shimmoto M, Takiguchi K, Doi H, Nishizawa Y, Kobayashi T, Kamei S, Lukong KE, Pshezhetsky AV, Sakuraba H: Molecular and structural studies of Japanese patients with sialidosis type 1. J Hum Genet. 2000;45(4):241-9. [PubMed Link Image]
  3. Bonten EJ, Arts WF, Beck M, Covanis A, Donati MA, Parini R, Zammarchi E, d'Azzo A: Novel mutations in lysosomal neuraminidase identify functional domains and determine clinical severity in sialidosis. Hum Mol Genet. 2000 Nov 1;9(18):2715-25. [PubMed Link Image]
  4. Lukong KE, Landry K, Elsliger MA, Chang Y, Lefrancois S, Morales CR, Pshezhetsky AV: Mutations in sialidosis impair sialidase binding to the lysosomal multienzyme complex. J Biol Chem. 2001 May 18;276(20):17286-90. Epub 2001 Feb 20. [PubMed Link Image]
  5. Bonten E, van der Spoel A, Fornerod M, Grosveld G, d'Azzo A: Characterization of human lysosomal neuraminidase defines the molecular basis of the metabolic storage disorder sialidosis. Genes Dev. 1996 Dec 15;10(24):3156-69. [PubMed Link Image]
  6. Milner CM, Smith SV, Carrillo MB, Taylor GL, Hollinshead M, Campbell RD: Identification of a sialidase encoded in the human major histocompatibility complex. J Biol Chem. 1997 Feb 14;272(7):4549-58. [PubMed Link Image]
  7. Pshezhetsky AV, Richard C, Michaud L, Igdoura S, Wang S, Elsliger MA, Qu J, Leclerc D, Gravel R, Dallaire L, Potier M: Cloning, expression and chromosomal mapping of human lysosomal sialidase and characterization of mutations in sialidosis. Nat Genet. 1997 Mar;15(3):316-20. [PubMed Link Image]
  8. Vinogradova MV, Michaud L, Mezentsev AV, Lukong KE, El-Alfy M, Morales CR, Potier M, Pshezhetsky AV: Molecular mechanism of lysosomal sialidase deficiency in galactosialidosis involves its rapid degradation. Biochem J. 1998 Mar 1;330 ( Pt 2):641-50. [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.