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Showing drug card for Fusidic Acid (DB02703)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-02-19 16:04:40
Primary Accession Number DB02703
Secondary Accession Number
  • EXPT01507
Name Fusidic Acid
Drug Type
  • Approved
  • Small Molecule
Description An antibiotic isolated from the fermentation broth of Fusidium coccineum. (From Merck Index, 11th ed) It acts by inhibiting translocation during protein synthesis.
Synonyms
  1. Diethanolamine fusidate
  2. Fucidate
  3. Fucidate Sodium
  4. Fucidic acid
  5. Fusidate
  6. Fusidate Sodium
Brand Names
  1. Fucidin
  2. Fucidin Cream 2%
  3. Fucidin acid
  4. Fucidine
  5. Fucithalmic
  6. Fusidine
  7. Ramycin
Brand Mixtures
  1. Fucibet (Fusidic acid + betamethasone)
  2. Fucicort (Fusidic acid + hydrocortisone)
Chemical IUPAC Name (2Z)-2-[(3R,4S,5S,8S,9S,10S,11R,13R,14S,16S)-16-acetyloxy-3,11-dihydroxy-4,8,10,14-tetramethyl-2,3,4,5,6,7,9,11,12,13,15,16-dodecahydro-1H-cyclopenta[a]phenanthren-17-ylidene]-6-methylhept-5-enoic acid
Chemical Formula C31H48O6
Chemical Structure Structure
CAS Registry Number 6990-06-3
InChI Identifier InChI=1/C31H48O6/c1-17(2)9-8-10-20(28(35)36)26-22-15-24(34)27-29(5)13-12-23(33)18(3)21(29)11-14-30(27,6)31(22,7)16-25(26)37-19(4)32/h9,18,21-25,27,33-34H,8,10-16H2,1-7H3,(H,35,36)/b26-20-/t18-,21-,22-,23+,24+,25-,27-,29-,30-,31-/m0/s1/f/h35H
InChI Key IECPWNUMDGFDKC-YLSUCPHCDU
KEGG Drug D04281 Link Image
KEGG Compound C06694 Link Image
PubChem Compound 3000226 Link Image
PubChem Substance 8919 Link Image
ChEBI ID Not Available
PharmGKB ID PA10087 Link Image
HET ID FUA Link Image
GenBank ID Not Available
Drug ID Number [DIN] 00586668 Link Image
RxList Link Not Available
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Fusidic_acid Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS) Not Available
Synthesis Reference Not Available
Average Molecular Weight 516.7092
Monoisotopic Molecular Weight 516.3451
State Solid
Melting Point 192.5 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 5.21e-03 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP 4.97 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -5.00 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 1QCA Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES C[C@@H]1[C@H](O)CC[C@@]2(C)[C@H]1CC[C@@]1(C)[C@H]2[C@H](O)C[C@H]2\C([C@H](C[C@]12C)OC(C)=O)=C(/CC\C=C(\C)C)C(O)=O
Canonical SMILES CC1C(O)CCC2(C)C1CCC1(C)C2C(O)CC2C(C(CC12C)OC(C)=O)=C(CCC=C(C)C)C(O)=O
Drug Category
  • Anti-Bacterial Agents
  • Antibacterial Agents
  • Protein Synthesis Inhibitors
ATC Codes Not Available
AHFS Codes Not Available
Indication For the treatment of bacterial infections.
Pharmacology Fusidic acid is a bacteriostatic antibiotic that is often used topically in creams and eyedrops, but may also be given systemically as tablets or injections.
Mechanism of Action Fusidic acid works by interfering with bacterial protein synthesis, specifically by preventing the translocation of the elongation factor G (EF-G) from the ribosome.
Absorption Sodium fusidic acid tablets have a 91% oral bioavailability. Absorption of the film-coated tablets is complete when compared to a solution, however oral absorption is variable. Oral fusidic acid hemihydrate (suspension) achieved a 22.5% bioavailability in pediatric patients following a 20 milligram/kilogram dose.
Toxicity Not Available
Protein Binding 97 to 99%
Biotransformation Metabolites include dicarboxylic ester/acid, 3-keto fusidic acid, hydroxy fusidic acid, glucuronide fusidic acid and a glycol metabolite.
Half Life Approximately 5 to 6 hours in adults.
Dosage Forms Not Available
Patient Information Not Available
Contraindications Not Available
Interactions Not Available
Drug Interactions
Drug Interaction
Amprenavir The protease inhibitor increases the effect and toxicity of fusidic acid
Atorvastatin Increased risk of myopathy/rhabdomyolysis
Fosamprenavir The protease inhibitor increases the effect and toxicity of fusidic acid
Indinavir Indinavir increases the effect and toxicity of fusidic acid
Nelfinavir The protease inhibitor increases the effect and toxicity of fusidic acid
Ritonavir The protease inhibitor increases the effect and toxicity of fusidic acid
Saquinavir The protease inhibitor increases the effect and toxicity of fusidic acid
Simvastatin Increased risk of myopathy/rhabdomyolysis
Food Interactions
  • Take with food to reduce irritation.
Pathways Not Available
General References
  1. Wikipedia Link Image
Organisms Affected
  • Enteric bacteria and other eubacteria
Targets
  1. Chloramphenicol acetyltransferase 3
  2. Chloramphenicol acetyltransferase
Drug Target 1 [top]
Target 1 ID 2808
Target 1 Name Chloramphenicol acetyltransferase 3
Target 1 Synonyms
  1. Chloramphenicol acetyltransferase III
  2. EC 2.3.1.28
  3. catIII
Target 1 Gene Name cat3
Target 1 Protein Sequence >Chloramphenicol acetyltransferase 3 
MNYTKFDVKNWVRREHFEFYRHRLPCGFSLTSKIDITTLKKSLDDSAYKFYPVMIYLIAQ
AVNQFDELRMAIKDDELIVWDSVDPQFTVFHQETETFSALSCPYSSDIDQFMVNYLSVME
RYKSDTKLFPQGVTPENHLNISALPWVNFDSFNLNVANFTDYFAPIITMAKYQQEGDRLL
LPLSVQVHHAVCDGFHVARFINRLQELCNSKLK
Target 1 Number of Residues 216
Target 1 Molecular Weight 24994
Target 1 Theoretical pI 6.15
Target 1 GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring acyl groups
transferase activity, transferring groups other than amino-acyl groups
acyltransferase activity
O-acyltransferase activity
O-acetyltransferase activity
chloramphenicol O-acetyltransferase activity
Process
Not Available
Component
Not Available
Target 1 General Function Involved in chloramphenicol O-acetyltransferase activity
Target 1 Specific Function This enzyme is an effector of chloramphenicol resistance in bacteria
Target 1 Pathways Not Available
Target 1 Reactions
  • acetyl-CoA + chloramphenicol = CoA + chloramphenicol 3-acetate
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Essential
Target 1 GenBank ID Protein 47025 Link Image
Target 1 UniProtKB/Swiss-Prot ID P00484 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name CAT3_ECOLI Link Image
Target 1 PDB ID 3CLA Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location Not Available
Target 1 Gene Sequence >642 bp 
ATGAACTATACAAAATTTGATGTAAAAAATTGGGTTCGCCGTGAGCATTTTGAGTTTTAT
CGGCATCGTTTACCATGTGGTTTTAGCTTAACAAGCAAAATTGATATCACGACGTTAAAA
AAGTCATTGGATGATTCAGCGTATAAGTTTTATCCGGTAATGATCTATCTGATTGCTCAG
GCCGTGAATCAATTTGATGAGTTGAGAATGGCGATAAAAGATGATGAATTGATCGTATGG
GATTCAGTCGACCCACAATTCACCGTATTCCATCAAGAAACAGAGACATTTTCAGCACTG
AGTTGCCCATACTCATCCGATATTGATCAATTTATGGTGAATTATTTATCGGTAATGGAA
CGTTATAAAAGTGATACCAAGTTATTTCCTCAAGGGGTAACACCAGAAAATCATTTAAAT
ATTTCAGCATTACCTTGGGTTAATTTTGATAGCTTTAATTTAAATGTTGCTAATTTTACC
GATTATTTTGCACCCATTATAACAATGGCAAAATATCAGCAAGAAGGGGATAGACTGTTA
TTGCCGCTCTCAGTACAGGTTCATCATGCAGTTTGTGATGGCTTCCATGTTGCACGCTTT
ATTAATCGGCTACAAGAGTTGTGTAACAGTAAATTAAAATAA
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. Leslie AG: Refined crystal structure of type III chloramphenicol acetyltransferase at 1.75 A resolution. J Mol Biol. 1990 May 5;213(1):167-86. [PubMed Link Image]
  2. Murray IA, Hawkins AR, Keyte JW, Shaw WV: Nucleotide sequence analysis and overexpression of the gene encoding a type III chloramphenicol acetyltransferase. Biochem J. 1988 May 15;252(1):173-9. [PubMed Link Image]
  3. Leslie AG, Moody PC, Shaw WV: Structure of chloramphenicol acetyltransferase at 1.75-A resolution. Proc Natl Acad Sci U S A. 1988 Jun;85(12):4133-7. [PubMed Link Image]
Target 1 Drug References
  1. 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]
  2. 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 3278
Target 2 Name Chloramphenicol acetyltransferase
Target 2 Synonyms
  1. CAT
  2. EC 2.3.1.28
Target 2 Gene Name cat
Target 2 Protein Sequence >Chloramphenicol acetyltransferase 
MEKKITGYTTVDISQWHRKEHFEAFQSVAQCTYNQTVQLDITAFLKTVKKNKHKFYPAFI
HILARLMNAHPEFRMAMKDGELVIWDSVHPCYTVFHEQTETFSSLWSEYHDDFRQFLHIY
SQDVACYGENLAYFPKGFIENMFFVSANPWVSFTSFDLNVANMDNFFAPVFTMGKYYTQG
DKVLMPLAIQVHHAVCDGFHVGRMLNELQQYCDEWQGGA
Target 2 Number of Residues 222
Target 2 Molecular Weight 25663
Target 2 Theoretical pI 6.36
Target 2 GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring acyl groups
transferase activity, transferring groups other than amino-acyl groups
acyltransferase activity
O-acyltransferase activity
O-acetyltransferase activity
chloramphenicol O-acetyltransferase activity
Process
Not Available
Component
Not Available
Target 2 General Function Involved in chloramphenicol O-acetyltransferase activity
Target 2 Specific Function This enzyme is an effector of chloramphenicol resistance in bacteria
Target 2 Pathways Not Available
Target 2 Reactions
  • acetyl-CoA + chloramphenicol = CoA + chloramphenicol 3-acetate
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Essential
Target 2 GenBank ID Protein 16505914 Link Image
Target 2 UniProtKB/Swiss-Prot ID P62580 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name CAT_SALTI Link Image
Target 2 PDB ID 1Q23 Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location Not Available
Target 2 Gene Sequence >660 bp 
ATGGAGAAAAAAATCACTGGATATACCACCGTTGATATATCCCAATGGCATCGTAAAGAA
CATTTTGAGGCATTTCAGTCAGTTGCTCAATGTACCTATAACCAGACCGTTCAGCTGGAT
ATTACGGCCTTTTTAAAGACCGTAAAGAAAAATAAGCACAAGTTTTATCCGGCCTTTATT
CACATTCTTGCCCGCCTGATGAATGCTCATCCGGAATTCCGTATGGCAATGAAAGACGGT
GAGCTGGTGATATGGGATAGTGTTCACCCTTGTTACACCGTTTTCCATGAGCAAACTGAA
ACGTTTTCATCGCTCTGGAGTGAATACCACGACGATTTCCGGCAGTTTCTACACATATAT
TCGCAAGATGTGGCGTGTTACGGTGAAAACCTGGCCTATTTCCCTAAAGGGTTTATTGAG
AATATGTTTTTCGTCTCAGCCAATCCCTGGGTGAGTTTCACCAGTTTTGATTTAAACGTG
GCCAATATGGACAACTTCTTCGCCCCCGTTTTCACCATGGGCAAATATTATACGCAAGGC
GACAAGGTGCTGATGCCGCTGGCGATTCAGGTTCATCATGCCGTTTGTGATGGCTTCCAT
GTCGGCAGAATGCTTAATGAATTACAACAGTACTGCGATGAGTGGCAGGGCGGGGCGTAA
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. Parkhill J, Dougan G, James KD, Thomson NR, Pickard D, Wain J, Churcher C, Mungall KL, Bentley SD, Holden MT, Sebaihia M, Baker S, Basham D, Brooks K, Chillingworth T, Connerton P, Cronin A, Davis P, Davies RM, Dowd L, White N, Farrar J, Feltwell T, Hamlin N, Haque A, Hien TT, Holroyd S, Jagels K, Krogh A, Larsen TS, Leather S, Moule S, O'Gaora P, Parry C, Quail M, Rutherford K, Simmonds M, Skelton J, Stevens K, Whitehead S, Barrell BG: Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18. Nature. 2001 Oct 25;413(6858):848-52. [PubMed Link Image]
Target 2 Drug References
  1. 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]
  2. 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]

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.