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Showing drug card for Penicillin G (DB01053)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-02-19 16:04:03
Primary Accession Number DB01053
Secondary Accession Number
  • APRD00646
Name Penicillin G
Drug Type
  • Approved
  • Small Molecule
Description A penicillin derivative commonly used in the form of its sodium or potassium salts in the treatment of a variety of infections. It is effective against most gram-positive bacteria and against gram-negative cocci. It has also been used as an experimental convulsant because of its actions on gamma-aminobutyric acid mediated synaptic transmission. [PubChem]
Synonyms Not Available
Brand Names
  1. Abbocillin
  2. Ayercillin
  3. Benzopenicillin
  4. Benzylpenicillin
  5. Benzylpenicillin G
  6. Benzylpenicillinic Acid
  7. Bicillin
  8. Bicillin L-A
  9. Cillora
  10. Cilloral
  11. Cilopen
  12. Compocillin G
  13. Cosmopen
  14. Crysticillin 300 A.S.
  15. Dropcillin
  16. Free Benzylpenicillin
  17. Free Penicillin G
  18. Free Penicillin Ii
  19. Galofak
  20. Gelacillin
  21. Liquacillin
  22. Megacillin
  23. Pencillin G
  24. Penicillin
  25. Penicillin G Potassium
  26. Penicillin G Potassium in Plastic Container
  27. Penicillin G Sodium
  28. Penicillin-G Potassium
  29. Penicillinic Acid, Benzyl-
  30. Pentids
  31. Pentids '200'
  32. Permapen
  33. Pfizerpen
  34. Pfizerpen G
  35. Pharmacillin
  36. Phenylacetamidopenicillanic Acid
  37. Pradupen
  38. Specilline G
  39. Ursopen
  40. Wycillin
Brand Mixtures Not Available
Chemical IUPAC Name (2S,5R,6R)-3,3-dimethyl-7-oxo-6-[(2-phenylacetyl)amino]-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylic acid
Chemical Formula C16H18N2O4S
Chemical Structure Structure
CAS Registry Number 61-33-6
InChI Identifier InChI=1/C16H18N2O4S/c1-16(2)12(15(21)22)18-13(20)11(14(18)23-16)17-10(19)8-9-6-4-3-5-7-9/h3-7,11-12,14H,8H2,1-2H3,(H,17,19)(H,21,22)/t11-,12+,14-/m1/s1/f/h17,21H
InChI Key JGSARLDLIJGVTE-JGBPDRTNDF
KEGG Drug D02336 Link Image
KEGG Compound C05551 Link Image
PubChem Compound 5904 Link Image
PubChem Substance 7885 Link Image
ChEBI ID 18208 Link Image
PharmGKB ID PA450842 Link Image
HET ID PG1 Link Image
GenBank ID Not Available
Drug ID Number [DIN] 00712981 Link Image
RxList Link http://www.rxlist.com/cgi/generic3/pengk.htm Link Image
PDRhealth Link Not Available
Wikipedia Link Not Available
FDA Label Not Available
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 334.3900
Monoisotopic Molecular Weight 334.0987
State Solid
Melting Point 214-217oC
Experimental Water Solubility Slightly soluble (210 mg/L) Source: PhysProp
Predicted Water Solubility 2.85e-01 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 1.5 Source: PhysProp
Predicted LogP 1.92 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -3.07 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point 2.74
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 CC1(C)S[C@@H]2[C@H](NC(=O)CC3=CC=CC=C3)C(=O)N2[C@H]1C(O)=O
Canonical SMILES CC1(C)SC2C(NC(=O)CC3=CC=CC=C3)C(=O)N2C1C(O)=O
Drug Category
  • Anti-Bacterial Agents
  • Penicillins
ATC Codes
AHFS Codes
  • 08:12.16.04
Indication For use in the treatment of severe infections caused by penicillin G-susceptible microorganisms when rapid and high penicillin levels are required.
Pharmacology Penicillin G is a penicillin beta-lactam antibiotic used in the treatment of bacterial infections caused by susceptible, usually gram-positive, organisms. The name "penicillin" can either refer to several variants of penicillin available, or to the group of antibiotics derived from the penicillins. Penicillin G has in vitro activity against gram-positive and gram-negative aerobic and anaerobic bacteria. The bactericidal activity of penicillin G results from the inhibition of cell wall synthesis and is mediated through penicillin G binding to penicillin binding proteins (PBPs). Penicillin G is stable against hydrolysis by a variety of beta-lactamases, including penicillinases, and cephalosporinases and extended spectrum beta-lactamases.
Mechanism of Action By binding to specific penicillin-binding proteins (PBPs) located inside the bacterial cell wall, penicillin G inhibits the third and last stage of bacterial cell wall synthesis. Cell lysis is then mediated by bacterial cell wall autolytic enzymes such as autolysins; it is possible that penicillin G interferes with an autolysin inhibitor.
Absorption Rapidly absorbed following both intramuscular and subcutaneous injection. Initial blood levels following parenteral administration are high but transient.
Toxicity Oral LD50 in rat is 8900 mk/kg. Neurological adverse reactions, including convulsions, may occur with the attainment of high CSF levels of beta-lactams.
Protein Binding Bind to serum proteins, mainly albumin.
Biotransformation Not Available
Half Life Not Available
Dosage Forms
Form Route
Powder, for solution Intramuscular
Powder, for solution Intravenous
Powder, for solution Oral
Suspension Oral
Tablet Oral
Patient Information Not Available
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Acenocoumarol The IV penicillin increases the anticoagulant effect
Anisindione The IV penicillin increases the anticoagulant effect
Demeclocycline Possible antagonism of action
Dicumarol The IV penicillin increases the anticoagulant effect
Doxycycline Possible antagonism of action
Ethinyl Estradiol This anti-infectious agent could decreases the effect of the oral contraceptive
Mestranol This anti-infectious agent could decreases the effect of the oral contraceptive
Methacycline Possible antagonism of action
Methotrexate The penicillin increases the effect and toxicity of methotrexate
Minocycline Possible antagonism of action
Oxytetracycline Possible antagonism of action
Rolitetracycline Possible antagonism of action
Tetracycline Possible antagonism of action
Warfarin The IV penicillin increases the anticoagulant effect
Food Interactions Not Available
Pathways Not Available
General References
  1. Drugs.com Link Image
  2. RxList Link Image
Organisms Affected
  • Enteric bacteria and other eubacteria
Targets
  1. Penicillin-binding proteins 1A/1B
Drug Target 1 [top]
Target 1 ID 633
Target 1 Name Penicillin-binding proteins 1A/1B
Target 1 Synonyms Not Available
Target 1 Gene Name pbpA
Target 1 Protein Sequence >Penicillin-binding proteins 1A/1B 
MTERKREHKDRKQNKNSPKNQSKVTKFLKWFFIGILLLGITAVTVVGIYVLSIIRSSPEL
DVQAIQSLNQPSILYDDQGNFMDNVITREQRYVVKSEEIPDNLKKAFVAIEDERFYEHKG
IDIKRIFGVIASNIKGKLSGSNTVQGASTITQQLIKNAVLTNEVSYERKIKEMYLALELE
KHLSKDEILTTYLNTIPMGGYQYGVSAAAQRFFSKNVSDLNLVECAYLGGLTQAPTSYDG
LSEANKENPSRYLNRTKSVLFKMHELGYISSEQYNDAINEIDTNGIKFTPNNKLSKTNFE
WFTRPAITQVKQDLMDKYKYTQEEVDKLIANGGLKIYTSMDRNLQNNVQKVLDDPNNYKA
ITNNPNEKNEDGVYKLQASATIIDYKTGHVKALVGGRGEQPAMSHNRAYYDLKSIGSATK
PLTVYGPAIDLGLGGAGSVVNDSPLSNKELSSTGYKDQPKNEYNSYRGPLTFREAIKISS
NLAAIKVANEVGVSNSIAYGEKLGLVYGPHSRGISTTALGQFQNDPNNPDGGNTYTLASA
FGVFGNNGVKTNAKLYTKVLDSHGNVILDTSTPEETKIFSPQASYIVYDMLKDQVESGSA
KSAKFGNIPVAGKTGTTTGDKDYLFAGLTPYYSAAIWIGYDKPREMRTSSGTVTSPIFGK
IMGLAHKDLQYKEVDNLVE
Target 1 Number of Residues 690
Target 1 Molecular Weight 75178
Target 1 Theoretical pI 9.09
Target 1 GO Classification
Function
binding
drug binding
penicillin binding
transferase activity
transferase activity, transferring glycosyl groups
transferase activity, transferring pentosyl groups
hydrolase activity
peptidase activity
catalytic activity
Process
cellular physiological process
cell organization and biogenesis
external encapsulating structure organization and biogenesis
cell wall organization and biogenesis
cell wall organization and biogenesis (sensu Bacteria)
cell wall biosynthesis (sensu Bacteria)
response to stimulus
response to abiotic stimulus
response to chemical stimulus
response to drug
response to antibiotic
physiological process
metabolism
macromolecule metabolism
carbohydrate metabolism
cellular carbohydrate metabolism
peptidoglycan metabolism
peptidoglycan biosynthesis
Component
cell
external encapsulating structure
cell wall
cell wall (sensu Bacteria)
Target 1 General Function Cell wall/membrane/envelope biogenesis
Target 1 Specific Function Not Available
Target 1 Pathways Not Available
Target 1 Reactions Not Available
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • 30-52
Target 1 Essentiality Essential
Target 1 GenBank ID Protein 18145626 Link Image
Target 1 UniProtKB/Swiss-Prot ID Q8XJ01 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name Q8XJ01_CLOPE Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location
  • Cytoplasmic
Target 1 Gene Sequence >2040 bp 
ATGACTGAAAGAAAAAGAGAGCATAAAGATAGAAAGCAGAATAAAAATTCACCTAAAAAT
CAATCGAAAGTAACAAAATTTTTGAAATGGTTCTTTATAGGGATTCTGCTTCTAGGGATA
ACTGCCGTAACAGTAGTTGGAATTTACGTTCTTTCTATTATACGTTCATCTCCAGAGTTA
GATGTTCAGGCAATTCAATCTCTAAATCAGCCATCCATTCTTTACGATGATCAGGGAAAC
TTTATGGATAATGTTATAACTCGTGAACAACGTTATGTAGTTAAATCTGAAGAGATACCT
GATAACTTAAAAAAGGCTTTTGTAGCTATTGAAGACGAAAGATTTTATGAGCATAAAGGA
ATAGACATTAAAAGAATTTTTGGGGTAATAGCTTCTAATATTAAAGGTAAACTTTCAGGA
AGTAATACAGTTCAAGGGGCTTCAACCATAACTCAGCAACTTATAAAAAATGCCGTACTT
ACTAATGAAGTTAGTTATGAAAGAAAAATTAAAGAAATGTACTTAGCTTTGGAATTAGAA
AAGCACCTTTCAAAAGATGAAATCCTTACTACGTATTTAAATACAATTCCTATGGGTGGA
TACCAATATGGGGTTAGCGCAGCTGCTCAAAGATTTTTTAGTAAGAATGTTTCAGATTTG
AATTTAGTTGAGTGCGCTTATTTAGGAGGACTTACTCAAGCACCAACTTCTTATGATGGT
CTTTCAGAAGCAAATAAAGAAAATCCAAGTAGATATTTAAATAGAACTAAATCTGTACTA
TTTAAAATGCATGAACTTGGATATATTTCAAGTGAACAATATAATGACGCAATAAATGAA
ATTGACACAAATGGTATAAAATTCACACCAAATAATAAATTAAGTAAAACTAACTTTGAG
TGGTTCACAAGACCAGCTATAACTCAAGTTAAACAAGACTTAATGGATAAATATAAATAT
ACACAAGAGGAAGTTGACAAACTTATAGCTAATGGTGGATTAAAAATCTATACTTCAATG
GATAGAAATCTTCAAAATAATGTTCAAAAAGTTTTAGATGATCCAAATAACTATAAAGCT
ATAACTAATAATCCTAATGAAAAAAATGAAGATGGTGTTTATAAATTACAAGCATCTGCC
ACAATAATAGACTATAAAACAGGCCATGTTAAGGCTTTAGTTGGAGGAAGAGGGGAACAA
CCTGCTATGTCTCACAATAGAGCTTATTATGATTTAAAATCTATAGGTTCTGCAACAAAA
CCATTAACAGTTTATGGTCCTGCTATTGATTTAGGACTTGGTGGCGCTGGCTCTGTAGTA
AATGATTCTCCATTAAGTAATAAAGAGTTATCTTCTACAGGATATAAAGATCAACCTAAG
AATGAATACAATAGTTATAGAGGCCCTTTAACTTTTAGAGAAGCAATTAAAATCTCTAGT
AACTTAGCAGCCATAAAAGTTGCTAATGAAGTAGGTGTTTCAAACTCTATAGCTTATGGA
GAAAAATTAGGTCTTGTTTATGGACCTCATTCTAGAGGTATTTCCACAACAGCCTTAGGT
CAATTCCAAAATGACCCTAATAATCCTGATGGAGGAAATACTTATACTCTAGCTTCAGCC
TTCGGTGTTTTTGGTAATAACGGTGTTAAAACAAATGCTAAATTATATACAAAGGTATTA
GATTCTCATGGAAATGTAATTCTTGATACAAGTACTCCAGAAGAAACTAAAATATTTAGT
CCTCAAGCGTCTTATATAGTTTATGATATGCTTAAGGATCAAGTAGAAAGTGGCTCTGCA
AAATCTGCTAAATTTGGTAATATTCCTGTGGCGGGTAAAACAGGAACTACTACTGGAGAT
AAAGACTATTTATTTGCAGGATTAACTCCATATTATTCTGCGGCTATTTGGATTGGATAT
GATAAGCCTAGAGAAATGAGAACTAGTAGTGGTACTGTTACCTCTCCTATTTTCGGAAAA
ATAATGGGCTTAGCTCATAAAGACTTACAGTACAAAGAGGTTGACAACCTAGTGGAATAA
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. Shimizu T, Ohtani K, Hirakawa H, Ohshima K, Yamashita A, Shiba T, Ogasawara N, Hattori M, Kuhara S, Hayashi H: Complete genome sequence of Clostridium perfringens, an anaerobic flesh-eater. Proc Natl Acad Sci U S A. 2002 Jan 22;99(2):996-1001. Epub 2002 Jan 15. [PubMed Link Image]
Target 1 Drug References
  1. Ishida K, Hung TV, Liou K, Lee HC, Shin CH, Sohng JK: Characterization of pbpA and pbp2 encoding penicillin-binding proteins located on the downstream of clavulanic acid gene cluster in Streptomyces clavuligerus. Biotechnol Lett. 2006 Mar;28(6):409-17. [PubMed Link Image]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  3. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
  4. Godfrey AJ, Bryan LE: Mutation of Pseudomonas aeruginosa specifying reduced affinity for penicillin G. Antimicrob Agents Chemother. 1982 Feb;21(2):216-23. [PubMed Link Image]
  5. Milner JS, Dymock D, Cooper RM, Roberts IS: Penicillin-binding proteins from Erwinia amylovora: mutants lacking PBP2 are avirulent. J Bacteriol. 1993 Oct;175(19):6082-8. [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.