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Showing drug card for Meropenem (DB00760)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-23 18:08:04
Primary Accession Number DB00760
Secondary Accession Number
  • APRD01097
  • EXPT02153
Name Meropenem
Drug Type
  • Approved
  • Investigational
  • Small Molecule
Description Meropenem is a broad-spectrum carbapenem antibiotic. It is active against Gram-positive and Gram-negative bacteria. Meropenem exerts its action by penetrating bacterial cells readily and interfering with the synthesis of vital cell wall components, which leads to cell death.
Synonyms
  1. Antibiotic SM 7338
  2. Meropenem anhydrous
  3. Meropenemum [INN-Latin]
  4. meropenem
Brand Names
  1. Meronem
  2. Merrem
  3. Merrem I.V.
Brand Mixtures Not Available
Chemical IUPAC Name (4R,5S,6S)-3-[(2S,5S)-5-(dimethylcarbamoyl)pyrrolidin-2-yl]sulfanyl-6-(1-hydroxyethyl)-4-methyl-7-oxo-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid
Chemical Formula C17H25N3O5S
Chemical Structure Structure
CAS Registry Number 119478-56-7
InChI Identifier InChI=1/C17H25N3O5S/c1-7-12-11(8(2)21)16(23)20(12)13(17(24)25)14(7)26-10-6-5-9(18-10)15(22)19(3)4/h7-12,18,21H,5-6H2,1-4H3,(H,24,25)/t7-,8-,9+,10+,11-,12-/m1/s1/f/h24H
InChI Key FSTGLKRHSQANLP-CWFNKILDDW
KEGG Drug D02222 Link Image
KEGG Compound Not Available
PubChem Compound 64778 Link Image
PubChem Substance 206724 Link Image
ChEBI ID Not Available
PharmGKB ID PA450383 Link Image
HET ID MER Link Image
GenBank ID Not Available
Drug ID Number [DIN] 02218496 Link Image
RxList Link http://www.rxlist.com/cgi/generic2/meropen.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Meropenem Link Image
FDA Label
Material Safety Data Sheet (MSDS) Not Available
Synthesis Reference Not Available
Average Molecular Weight 383.4630
Monoisotopic Molecular Weight 383.1515
State Solid
Melting Point Not Available
Experimental Water Solubility Sparingly Source: PhysProp
Predicted Water Solubility 5.64e+00 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity -0.6 Source: PhysProp
Predicted LogP -0.80 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -1.83 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](O)[C@@H]1[C@H]2[C@@H](C)C(S[C@H]3CC[C@H](N3)C(=O)N(C)C)=C(N2C1=O)C(O)=O
Canonical SMILES CC(O)C1C2C(C)C(SC3CCC(N3)C(=O)N(C)C)=C(N2C1=O)C(O)=O
Drug Category
  • Anti-Bacterial Agents
  • Antibacterials for Systemic Use
ATC Codes
AHFS Codes
  • 08:12.07.08
Indication For use as single agent therapy for the treatment of the following infections when caused by susceptible isolates of the designated microorganisms: complicated skin and skin structure infections due to Staphylococcus aureus (b-lactamase and non-b-lactamase producing, methicillin-susceptible isolates only), Streptococcus pyogenes, Streptococcus agalactiae, viridans group streptococci, Enterococcus faecalis (excluding vancomycin-resistant isolates), Pseudomonas aeruginosa, Escherichia coli, Proteus mirabilis, Bacteroides fragilis and Peptostreptococcus species; complicated appendicitis and peritonitis caused by viridans group streptococci, Escherichia coli, Klebsiella pneumoniae, Pseudomonas aeruginosa, Bacteroides fragilis, B. thetaiotaomicron, and Peptostreptococcus species. Also for use in the treatment of bacterial meningitis caused by Streptococcus pneumoniae, Haemophilus influenzae (b-lactamase and non-b-lactamase-producing isolates), and Neisseria meningitidis.
Pharmacology Meropenem is a broad-spectrum carbapenem antibiotic. It is active against Gram-positive and Gram-negative bacteria. Meropenem exerts its action by penetrating bacterial cells readily and interfering with the synthesis of vital cell wall components, which leads to cell death.
Mechanism of Action The bactericidal activity of meropenem results from the inhibition of cell wall synthesis. Meropenem readily penetrates the cell wall of most Gram-positive and Gram-negative bacteria to reach penicillin-binding- protein (PBP) targets. Its strongest affinities are toward PBPs 2, 3 and 4 of Escherichia coli and Pseudomonas aeruginosa; and PBPs 1, 2 and 4 of Staphylococcus aureus.
Absorption Not Available
Toxicity In mice and rats, large intravenous doses of meropenem (2200-4000 mg/kg) have been associated with ataxia, dyspnea, convulsions, and mortalities.
Protein Binding Approximately 2%.
Biotransformation Primarily excreted unchanged. There is one metabolite which is microbiologically inactive.
Half Life Approximately 1 hour in adults and children 2 years of age and older with normal renal function. Approximately 1.5 hours in children 3 months to 2 years of age.
Dosage Forms
Form Route
Powder, for solution Intravenous
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions Not Available
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. Penicillin-binding protein 4
  2. Beta-lactamase PSE-2
Drug Target 1 [top]
Target 1 ID 819
Target 1 Name Penicillin-binding protein 4
Target 1 Synonyms
  1. D-alanyl-D-alanine-endopeptidase
  2. DD- carboxypeptidase
  3. DD-peptidase
  4. EC 3.4.16.4
  5. EC 3.4.99.-
  6. PBP-4
  7. Penicillin-binding protein 4 precursor
Target 1 Gene Name dacB
Target 1 Protein Sequence >Penicillin-binding protein 4 precursor 
MRFSRFIIGLTSCIAFSVQAANVDEYITQLPAGANLALMVQKVGASAPAIDYHSQQMALP
ASTQKVITALAALIQLGPDFRFTTTLETKGNVENGVLKGDLVARFGADPTLKRQDIRNMV
ATLKKSGVNQIDGNVLIDTSIFASHDKAPGWPWNDMTQCFSAPPAAAIVDRNCFSVSLYS
APKPGDMAFIRVASYYPVTMFSQVRTLPRGSAEAQYCELDVVPGDLNRFTLTGCLPQRSE
PLPLAFAVQDGASYAGAILKDELKQAGITWSGTLLRQTQVNEPGTVVASKQSAPLHDLLK
IMLKKSDNMIADTVFRMIGHARFNVPGTWRAGSDAVRQILRQQAGVDIGNTIIADGSGLS
RHNLIAPATMMQVLQYIAQHDNELNFISMLPLAGYDGSLQYRAGLHQAGVDGKVSAKTGS
LQGVYNLAGFITTASGQRMAFVQYLSGYAVEPADQRNRRIPLVRFESRLYKDIYQNN
Target 1 Number of Residues 484
Target 1 Molecular Weight 51799
Target 1 Theoretical pI 9.02
Target 1 GO Classification
Function
catalytic activity
hydrolase activity
peptidase activity
exopeptidase activity
carboxypeptidase activity
serine carboxypeptidase activity
Process
physiological process
metabolism
macromolecule metabolism
protein metabolism
cellular protein metabolism
proteolysis
Component
Not Available
Target 1 General Function Cell wall/membrane/envelope biogenesis
Target 1 Specific Function Not involved in transpeptidation but exclusively catalyzes a DD-carboxypeptidase and DD-endopeptidase reaction
Target 1 Pathways Not Available
Target 1 Reactions
  • Preferential cleavage: (Ac)2-L-Lys-D-Ala!D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine INHIBITOR Penicillin; beta-Lactam antibiotics
Target 1 Pfam Domain Function
Target 1 Signals
  • 1-20
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Essential
Target 1 GenBank ID Protein 41216 Link Image
Target 1 UniProtKB/Swiss-Prot ID P24228 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name PBP4_ECOLI Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location
  • Periplasm (Potential)
Target 1 Gene Sequence >1434 bp 
ATGCGATTTTCCAGATTTATCATCGGATTGACCAGCTGTATAGCGTTCAGTGTTCAGGCC
GCAAATGTTGATGAGTACATTACTCAACTCCCCGCTGGTGCCAACCTTGCCCTGATGGTG
CAAAAAGTCGGCGCGTCGGCCCCCGCTATTGATTACCACAGTCAGCAGATGGCGCTGCCT
GCCAGTACCCAGAAAGTGATTACTGCGCTGGCGGCGTTGATTCAACTCGGCCCCGATTTT
CGTTTTACCACGACGCTTGAAACCAAAGGCAATGTGGAAAACGGCGTACTTAAGGGTGAC
TTAGTGGCGCGATTTGGTGCCGATCCGACGTTAAAACGTCAGGATATTCGCAATATGGTC
GCGACTTTGAAAAAATCTGGCGTCAACCAAATCGATGGCAATGTGTTGATAGATACCTCC
ATTTTCGCCAGCCACGATAAAGCCCCCGGCTGGCCATGGAATGACATGACACAATGCTTT
AGCGCTCCGCCTGCCGCCGCCATAGTTGACCGCAACTGTTTCTCCGTCTCGCTCTACAGT
GCCCCAAAGCCTGGTGATATGGCTTTTATACGCGTGGCATCTTATTACCCCGTTACGATG
TTCAGCCAGGTACGCACCCTCCCCCGTGGTTCTGCCGAAGCGCAATACTGCGAACTGGAT
GTGGTGCCAGGCGACCTGAACCGCTTTACGCTGACGGGATGCCTGCCACAACGTTCTGAG
CCGCTCCCGTTGGCTTTTGCCGTGCAGGATGGAGCCAGCTATGCCGGTGCAATTCTGAAA
GATGAGTTAAAACAGGCGGGTATCACCTGGAGCGGAACACTGCTGCGCCAGACTCAGGTT
AACGAACCTGGAACGGTAGTTGCCAGTAAACAGTCGGCCCCGCTGCACGATCTGCTTAAG
ATTATGCTGAAAAAGTCGGACAACATGATCGCCGATACGGTTTTCCGCATGATAGGCCAT
GCGCGCTTCAATGTGCCTGGAACATGGCGGGCCGGGTCGGACGCCGTGCGTCAGATCCTG
CGCCAGCAAGCCGGTGTCGATATTGGAAACACCATTATTGCCGATGGTTCAGGGCTTTCG
CGGCATAACCTGATTGCCCCCGCCACCATGATGCAGGTGCTGCAATACATTGCCCAACAC
GACAATGAACTTAACTTTATCTCCATGCTGCCGCTGGCGGGCTATGACGGCTCTTTGCAG
TACCGTGCAGGTCTGCATCAGGCGGGCGTGGATGGAAAAGTCTCAGCGAAAACCGGTTCG
TTGCAGGGGGTATATAACCTGGCGGGATTCATTACCACAGCGAGCGGGCAACGAATGGCG
TTTGTGCAATATCTTTCTGGCTATGCAGTAGAACCTGCGGATCAGCGTAATCGCCGTATT
CCGTTAGTGCGTTTTGAAAGCCGTTTGTATAAAGATATTTATCAGAACAATTAG
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. Mottl H, Terpstra P, Keck W: Penicillin-binding protein 4 of Escherichia coli shows a novel type of primary structure among penicillin-interacting proteins. FEMS Microbiol Lett. 1991 Mar 1;62(2-3):213-20. [PubMed Link Image]
  2. Korat B, Mottl H, Keck W: Penicillin-binding protein 4 of Escherichia coli: molecular cloning of the dacB gene, controlled overexpression, and alterations in murein composition. Mol Microbiol. 1991 Mar;5(3):675-84. [PubMed Link Image]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed Link Image]
Target 1 Drug References
  1. Ubukata K, Shibasaki Y, Yamamoto K, Chiba N, Hasegawa K, Takeuchi Y, Sunakawa K, Inoue M, Konno M: Association of amino acid substitutions in penicillin-binding protein 3 with beta-lactam resistance in beta-lactamase-negative ampicillin-resistant Haemophilus influenzae. Antimicrob Agents Chemother. 2001 Jun;45(6):1693-9. [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. Kanazawa K, Nouda H, Sunagawa M: Structure-activity relationships of carbapenem compounds to anti-Haemophilus influenzae activity and affinity for penicillin-binding proteins. Effect of 1 beta-methyl group and C-2 side chain. J Antibiot (Tokyo). 1997 Feb;50(2):162-8. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 2340
Target 2 Name Beta-lactamase PSE-2
Target 2 Synonyms
  1. Beta lactamase OXA-10
  2. Beta-lactamase PSE-2 precursor
  3. EC 3.5.2.6
Target 2 Gene Name pse2
Target 2 Protein Sequence >Beta-lactamase PSE-2 precursor 
MKTFAAYVIIACLSSTALAGSITENTSWNKEFSAEAVNGVFVLCKSSSKSCATNDLARAS
KEYLPASTFKIPNAIIGLETGVIKNEHQVFKWDGKPRAMKQWERDLTLRGAIQVSAVPVF
QQIAREVGEVRMQKYLKKFSYGNQNISGGIDKFWLEGQLRISAVNQVEFLESLYLNKLSA
SKENQLIVKEALVTEAAPEYLVHSKTGFSGVGTESNPGVAWWVGWVEKETEVYFFAFNMD
IDNESKLPLRKSIPTKIMESEGIIGG
Target 2 Number of Residues 270
Target 2 Molecular Weight 29507
Target 2 Theoretical pI 8.03
Target 2 GO Classification
Function
binding
drug binding
penicillin binding
catalytic activity
hydrolase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
beta-lactamase 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)
physiological process
metabolism
cellular metabolism
drug metabolism
antibiotic metabolism
antibiotic catabolism
Component
Not Available
Target 2 General Function Defense mechanisms and antibiotic degradation
Target 2 Specific Function Hydrolyzes both carbenicillin and oxacillin
Target 2 Pathways
Name SMPDB Link KEGG Link
Penicillins and cephalosporins biosynthesis map00311 Link Image
Target 2 Reactions
  • a beta-lactam + H2O = a substituted beta-amino acid
Target 2 Pfam Domain Function
Target 2 Signals
  • 1-20
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Essential
Target 2 GenBank ID Protein 1019897 Link Image
Target 2 UniProtKB/Swiss-Prot ID P14489 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name BLP2_PSEAE Link Image
Target 2 PDB ID 1K6R Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location
  • Cytoplasmic
Target 2 Gene Sequence >801 bp 
ATGAAAACATTTGCCGCATATGTAATTATCGCGTGTCTTTCGAGTACGGCATTAGCTGGT
TCAATTACAGAAAATACGTCTTGGAACAAAGAGTTCTCTGCCGAAGCCGTCAATGGTGTC
TTCGTGCTTTGTAAAAGTAGCAGTAAATCCTGCGCTACCAATGACTTAGCTCGTGCATCA
AAGGAATATCTTCCAGCATCAACATTTAAGATCCCCAACGCAATTATCGGCCTAGAAACT
GGTGTCATAAAGAATGAGCATCAGGTTTTCAAATGGGACGGAAAGCCAAGAGCCATGAAG
CAATGGGAAAGAGACTTGACCTTAAGAGGGGCAATACAAGTTTCAGCTGTTCCCGTATTT
CAACAAATCGCCAGAGAAGTTGGCGAAGTAAGAATGCAGAAATACCTTAAAAAATTTTCC
TATGGCAACCAGAATATCAGTGGTGGCATTGACAAATTCTGGTTGGAAGGCCAGCTTAGA
ATTTCCGCAGTTAATCAAGTGGAGTTTCTAGAGTCTCTATATTTAAATAAATTGTCAGCA
TCTAAAGAAAACCAGCTAATAGTAAAAGAGGCTTTGGTAACGGAGGCGGCACCTGAATAT
CTAGTGCATTCAAAAACTGGTTTTTCTGGTGTGGGAACTGAGTCAAATCCTGGTGTCGCA
TGGTGGGTTGGGTGGGTTGAGAAGGAGACAGAGGTTTACTTTTTCGCCTTTAACATGGAT
ATAGACAACGAAAGTAAGTTGCCGCTAAGAAAATCCATTCCCACCAAAATCATGGAAAGT
GAGGGCATCATTGGTGGCTAA
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. Maveyraud L, Golemi D, Kotra LP, Tranier S, Vakulenko S, Mobashery S, Samama JP: Insights into class D beta-lactamases are revealed by the crystal structure of the OXA10 enzyme from Pseudomonas aeruginosa. Structure. 2000 Dec 15;8(12):1289-98. [PubMed Link Image]
  2. Huovinen P, Huovinen S, Jacoby GA: Sequence of PSE-2 beta-lactamase. Antimicrob Agents Chemother. 1988 Jan;32(1):134-6. [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.