DrugBank: Cefonicid (DB01328)

targets (5) carriers (1)

Identification

Name

Cefonicid

Accession Number

DB01328

Type

small molecule

Groups

approved

Description

A second-generation cephalosporin administered intravenously or intramuscularly. Its bactericidal action results from inhibition of cell wall synthesis. It is used for urinary tract infections, lower respiratory tract infections, and soft tissue and bone infections. [PubChem]

Structure

Download: MOL | SDF | SMILES | InChI
Display: 2D Structure | 3D Structure

Synonyms

Cefonicido [inn-spanish]
Cefonicidum [inn-latin]

Brand names

Monocid
Praticef

Brand name mixtures

Not Available

Categories

Anti-Bacterial Agents
Antibacterial Agents
Cephalosporins

CAS number

61270-58-4

Weight

Average: 542.566
Monoisotopic: 542.034823652

Chemical Formula

C₁₈H₁₈N₆O₈S₃

InChI Key

InChIKey=DYAIAHUQIPBDIP-UJBKNGIVSA-N

InChI

InChI=1S/C18H18N6O8S3/c25-13(9-4-2-1-3-5-9)14(26)19-11-15(27)24-12(17(28)29)10(6-33-16(11)24)7-34-18-20-21-22-23(18)8-35(30,31)32/h1-5,11,13,16,25H,6-8H2,(H,19,26)(H,28,29)(H,30,31,32)/t11-,13?,16-/m1/s1

Plain Text

IUPAC Name

(6R,7R)-7-(2-hydroxy-2-phenylacetamido)-8-oxo-3-({[1-(sulfomethyl)-1H-1,2,3,4-tetrazol-5-yl]sulfanyl}methyl)-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid

SMILES

[H][C@]12SCC(CSC3=NN=NN3CS(O)(=O)=O)=C(N1C(=O)[C@H]2NC(=O)C(O)C1=CC=CC=C1)C(O)=O

Plain Text

Mass Spec

Not Available

Taxonomy

Kingdom

Organic

Classes

Benzyl Alcohols and Derivatives
Phenethylamines
Cephalosporins

Substructures

Ethers
Hydroxy Compounds
Benzyl Alcohols and Derivatives
Acetates
Amino Ketones
Carboxylic Acids and Derivatives
Sulfonyls
Benzene and Derivatives
Aliphatic and Aryl Amines
Sulfonic Acids and Derivatives
Beta Lactams
Enamines
Tetrazoles
Phenethylamines
Heterocyclic compounds
Aromatic compounds
Carboxamides and Derivatives
Cephalosporins
Lactams
Azetidines
Cyanamides
Alcohols and Polyols

Pharmacology

Indication

For the treatment of bacterial infections caused by susceptible microorganisms.

Pharmacodynamics

Cefonicid is a second-generation cephalosporin administered intravenously or intramuscularly. Its bactericidal action results from inhibition of cell wall synthesis. It is used for urinary tract infections, lower respiratory tract infections, and soft tissue and bone infections.

Mechanism of action

Cefonicid, like the penicillins, is a beta-lactam antibiotic. By binding to specific penicillin-binding proteins (PBPs) located inside the bacterial cell wall, it 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.

Absorption

Not Available

Volume of distribution

Not Available

Protein binding

98% bound to plasma proteins.

Metabolism

Not metabolized.

Route of elimination

Not Available

Half life

4.5 hours

Clearance

Not Available

Toxicity

Not Available

Affected organisms

Enteric bacteria and other eubacteria

Pathways

Not Available

Pharmacoeconomics

Manufacturers

Glaxosmithkline

Packagers

Not Available

Dosage forms

Form	Route	Strength
Solution	Intramuscular
Solution	Intravenous

Prices

Not Available

Patents

Not Available

Properties

State

solid

Melting point

Not Available

Experimental Properties

Not Available

Predicted Properties

Property	Value	Source
water solubility	8.95e-01 g/l	ALOGPS
logP	-0.71	ALOGPS
logP	-2.53	ChemAxon Molconvert
logS	-2.78	ALOGPS
pKa	3.11	ChemAxon Molconvert
hydrogen acceptor count	11	ChemAxon Molconvert
hydrogen donor count	4	ChemAxon Molconvert
polar surface area	204.91	ChemAxon Molconvert
rotatable bond count	9	ChemAxon Molconvert
refractivity	136.58	ChemAxon Molconvert
polarizability	48.64	ChemAxon Molconvert

References

Synthesis Reference

Not Available

General Reference

Not Available

External Links

Resource	Link
KEGG Compound	C06882
PubChem Compound	43592
PubChem Substance	46505699
ChemSpider	39732
ChEBI	3491
ChEMBL	3491
Therapeutic Targets Database	DAP001173
PharmGKB	PA448847
Drug Product Database	0

ATC Codes

J01DC06

AHFS Codes

Not Available

PDB Entries

Not Available

FDA label

Not Available

MSDS

Not Available

Interactions

Drug Interactions

Not Available

Food Interactions

Not Available

Targets
1. Penicillin-binding protein 1A Pharmacological action: yes Actions: inhibitor Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits) Organism class: bacterial UniProt ID: P02918 Gene: mrcA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report References: Rake JB, Newman DJ, Actor P: Affinity of cefonicid, a long-acting cephalosporin, for the penicillin-binding proteins of Escherichia coli K-12. J Antibiot (Tokyo). 1984 May;37(5):572-6. Pubmed 2. Peptidoglycan synthetase ftsI Pharmacological action: yes Actions: inhibitor Cell wall formation. Essential for the formation of a septum of the murein sacculus. Synthesis of cross-linked peptidoglycan from the lipid intermediates Organism class: bacterial UniProt ID: P0AD68 Gene: ftsI Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report References: Rake JB, Newman DJ, Actor P: Affinity of cefonicid, a long-acting cephalosporin, for the penicillin-binding proteins of Escherichia coli K-12. J Antibiot (Tokyo). 1984 May;37(5):572-6. Pubmed 3. Penicillin-binding protein 1B Pharmacological action: yes Actions: inhibitor Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits) Organism class: bacterial UniProt ID: P02919 Gene: mrcB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report References: Rake JB, Newman DJ, Actor P: Affinity of cefonicid, a long-acting cephalosporin, for the penicillin-binding proteins of Escherichia coli K-12. J Antibiot (Tokyo). 1984 May;37(5):572-6. Pubmed 4. Penicillin-binding protein 4 Pharmacological action: yes Actions: inhibitor Not involved in transpeptidation but exclusively catalyzes a DD-carboxypeptidase and DD-endopeptidase reaction Organism class: bacterial UniProt ID: P24228 Gene: dacB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report References: Rake JB, Newman DJ, Actor P: Affinity of cefonicid, a long-acting cephalosporin, for the penicillin-binding proteins of Escherichia coli K-12. J Antibiot (Tokyo). 1984 May;37(5):572-6. Pubmed 5. Penicillin-binding protein 2 Pharmacological action: yes Actions: inhibitor Cell wall formation; PBP-2 is responsible for the determination of the rod shape of the cell. Its synthesize cross- linked peptidoglycan from the lipid intermediates Organism class: bacterial UniProt ID: P0AD65 Gene: mrdA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report References: Rake JB, Newman DJ, Actor P: Affinity of cefonicid, a long-acting cephalosporin, for the penicillin-binding proteins of Escherichia coli K-12. J Antibiot (Tokyo). 1984 May;37(5):572-6. Pubmed

Targets

1. Penicillin-binding protein 1A

Pharmacological action: yes
Actions: inhibitor

Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits)

Organism class: bacterial
UniProt ID: P02918 Link_out

Gene: mrcA
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:

Rake JB, Newman DJ, Actor P: Affinity of cefonicid, a long-acting cephalosporin, for the penicillin-binding proteins of Escherichia coli K-12. J Antibiot (Tokyo). 1984 May;37(5):572-6. Pubmed

2. Peptidoglycan synthetase ftsI

Pharmacological action: yes
Actions: inhibitor

Cell wall formation. Essential for the formation of a septum of the murein sacculus. Synthesis of cross-linked peptidoglycan from the lipid intermediates

Organism class: bacterial
UniProt ID: P0AD68 Link_out

Gene: ftsI
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:

Rake JB, Newman DJ, Actor P: Affinity of cefonicid, a long-acting cephalosporin, for the penicillin-binding proteins of Escherichia coli K-12. J Antibiot (Tokyo). 1984 May;37(5):572-6. Pubmed

3. Penicillin-binding protein 1B

Pharmacological action: yes
Actions: inhibitor

Organism class: bacterial
UniProt ID: P02919 Link_out

Gene: mrcB
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:

Rake JB, Newman DJ, Actor P: Affinity of cefonicid, a long-acting cephalosporin, for the penicillin-binding proteins of Escherichia coli K-12. J Antibiot (Tokyo). 1984 May;37(5):572-6. Pubmed

4. Penicillin-binding protein 4

Pharmacological action: yes
Actions: inhibitor

Not involved in transpeptidation but exclusively catalyzes a DD-carboxypeptidase and DD-endopeptidase reaction

Organism class: bacterial
UniProt ID: P24228 Link_out

Gene: dacB
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:

Rake JB, Newman DJ, Actor P: Affinity of cefonicid, a long-acting cephalosporin, for the penicillin-binding proteins of Escherichia coli K-12. J Antibiot (Tokyo). 1984 May;37(5):572-6. Pubmed

5. Penicillin-binding protein 2

Pharmacological action: yes
Actions: inhibitor

Cell wall formation; PBP-2 is responsible for the determination of the rod shape of the cell. Its synthesize cross- linked peptidoglycan from the lipid intermediates

Organism class: bacterial
UniProt ID: P0AD65 Link_out

Gene: mrdA Link_out

Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:

Rake JB, Newman DJ, Actor P: Affinity of cefonicid, a long-acting cephalosporin, for the penicillin-binding proteins of Escherichia coli K-12. J Antibiot (Tokyo). 1984 May;37(5):572-6. Pubmed

Carriers
1. Serum albumin Actions: other/unknown Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood UniProt ID: P02768 Gene: ALB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report References: Rodriguez CA, Smith DE: Influence of the unbound concentration of cefonicid on its renal elimination in isolated perfused rat kidneys. Antimicrob Agents Chemother. 1991 Nov;35(11):2395-400. Pubmed Robertson A, Fink S, Karp W: Effect of cephalosporins on bilirubin-albumin binding. J Pediatr. 1988 Feb;112(2):291-4. Pubmed Benson JM, Boudinot FD, Pennell AT, Cunningham FE, DiPiro JT: In vitro protein binding of cefonicid and cefuroxime in adult and neonatal sera. Antimicrob Agents Chemother. 1993 Jun;37(6):1343-7. Pubmed

Carriers

1. Serum albumin

Actions: other/unknown

Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood

UniProt ID: P02768 Link_out

Gene: ALB

Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:

Rodriguez CA, Smith DE: Influence of the unbound concentration of cefonicid on its renal elimination in isolated perfused rat kidneys. Antimicrob Agents Chemother. 1991 Nov;35(11):2395-400. Pubmed
Robertson A, Fink S, Karp W: Effect of cephalosporins on bilirubin-albumin binding. J Pediatr. 1988 Feb;112(2):291-4. Pubmed
Benson JM, Boudinot FD, Pennell AT, Cunningham FE, DiPiro JT: In vitro protein binding of cefonicid and cefuroxime in adult and neonatal sera. Antimicrob Agents Chemother. 1993 Jun;37(6):1343-7. Pubmed

Comments

Drug created on June 30, 2007 11:48 / Updated on April 19, 2011 15:09

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.