Ceftazidime

Overview

Description
An antibiotic given by injection used to treat a variety of serious infections in various parts of the body caused by bacteria.
Description
An antibiotic given by injection used to treat a variety of serious infections in various parts of the body caused by bacteria.
DrugBank ID
DB00438
Type
Small Molecule
US Approved
YES
Other Approved
YES
Clinical Trials
Phase 0
1
Phase 1
12
Phase 2
17
Phase 3
18
Phase 4
20
Therapeutic Categories
  • Cephalosporins
  • Third-Generation Cephalosporins

Identification

Summary

Ceftazidime is an injected broad-spectrum third-generation cephalosporin beta-lactam antibiotic used to treat or prevent a variety of bacterial infections, including pneumonia, gynecological infections, bone and joint infections, and septicemia, among others.

Brand Names
Avycaz, Fortaz, Tazicef, Zavicefta
Generic Name
Ceftazidime
DrugBank Accession Number
DB00438
Background

Bacteria possess a cell wall comprising a glycopeptide polymer commonly known as peptidoglycan, which is synthesized and remodelled through the action of a family of enzymes known as "penicillin-binding proteins" (PBPs).1 β-lactam antibiotics, including cephalosporins, are PBP inhibitors that, through inhibition of essential PBPs, result in impaired cell wall homeostasis, loss of cell integrity, and ultimately bacterial cell death.1,2,3 Ceftazidime is a third-generation cephalosporin with broad-spectrum antibacterial activity, including against some treatment-resistant bacteria such as Pseudomonas aeruginosa.12

Ceftazidime was approved by the FDA on July 19, 1985, and is currently available either alone or in combination with the non-β-lactam β-lactamase inhibitor avibactam to treat a variety of bacterial infections.12,13

Type
Small Molecule
Groups
Approved
Structure
Weight
Average: 546.576
Monoisotopic: 546.099138468
Chemical Formula
C22H22N6O7S2
Synonyms
  • CAZ
  • Ceftazidim
  • Ceftazidima
  • Ceftazidime
  • Ceftazidime anhydrous
  • Ceftazidimum
External IDs
  • GR 20263

Pharmacology

Indication

Ceftazidime is indicated for the treatment of lower respiratory tract infections, skin and skin structure infections, urinary tract infections, bacterial septicemia, bone and joint infections, gynecologic infections, intra-abdominal infections (including peritonitis), and central nervous system infections (including meningitis) caused by susceptible bacteria.12

Ceftazidime is indicated in combination with avibactam to treat infections caused by susceptible Gram-negative organisms, including complicated intra-abdominal infections (cIAI), in conjunction with metronidazole, and complicated urinary tract infections (cUTI), including pyelonephritis, in patients aged three months and older. This combination is also indicated to treat hospital-acquired and ventilator-associated bacterial pneumonia (HABP/VABP) in patients aged 18 years and older.15

In all cases, to mitigate the risk of bacterial resistance and preserve clinical efficacy, ceftazidime should only be used for infections that are confirmed or strongly suspected to be caused by susceptible bacterial strains.12,15

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Associated Conditions
Indication TypeIndicationCombined Product DetailsApproval LevelAge GroupPatient CharacteristicsDose Form
Used in combination to treatBacteremiaCombination Product in combination with: Sodium carbonate (DB09460)•••••••••••••••••••••
Treatment ofBacterial infection••••••••••••
Treatment ofBacterial septicemia•••••••••••••••••••••
Treatment ofBone and joint infections•••••••••••••••••••••
Used in combination to treatBone and joint infectionsCombination Product in combination with: Sodium carbonate (DB09460)•••••••••••••••••••••
Contraindications & Blackbox Warnings
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Pharmacodynamics

Ceftazidime is a semisynthetic, broad-spectrum, third-generation cephalosporin antibiotic that is bactericidal through inhibition of enzymes responsible for cell-wall synthesis, primarily penicillin-binding protein 3 (PBP3).12 Among cephalosporins, ceftazidime is notable for its resistance to numerous β-lactamases and its broad spectrum of activity against Gram-negative bacteria, including Pseudomonas aeruginosa.4 However, it is less active than first- and second-generation cephalosporins against Staphylococcus aureus and other Gram-positive bacteria and also has low activity against anaerobes.4,9 Ceftazidime has confirmed activity against clinically relevant Gram-negative bacteria including Citrobacter spp., Enterobacter spp., Klebsiella spp., Proteus spp., Serratia spp., _Escherichia coli, Haemophilus influenzae, Neisseria meningitidis, Pseudomonas aeruginosa, and some Gram-positive bacteria including Staphylococcus spp. and Streptococcus spp. There are also in vitro data for ceftazidime efficacy against a wide variety of other bacteria, such as Acinetobacter baumannii and Neisseria gonorrhoeae, but no clear clinical studies to support the use of ceftazidime for infections caused by these bacteria.12

Although β-lactam antibiotics like ceftazidime are generally well tolerated, there remains a risk of serious acute hypersensitivity reactions, which is higher in patients with a known allergy to ceftazidime or any other β-lactam antibiotic. As with all antibiotics, ceftazidime may result in the overgrowth of non-susceptible organisms and potentially serious effects including Clostridium difficile-associated diarrhea (CDAD); CDAD should be considered in patients who develop diarrhea and, in confirmed cases, supportive care initiated immediately. Ceftazidime is primarily renally excreted such that high and prolonged serum concentrations can occur in patients with renal insufficiency, leading to seizures, nonconvulsive status epilepticus (NCSE), encephalopathy, coma, asterixis, neuromuscular excitability, and myoclonia. Treatment may lead to the development or induction of resistance with a risk of treatment failure. Periodic susceptibility testing should be considered, and monotherapy failure may necessitate the addition of another antibiotic such as an aminoglycoside. Cephalosporin use may decrease prothrombin activity, which may be improved by exogenous vitamin K. Inadvertent intra-arterial administration of ceftazidime may result in distal necrosis.12

Mechanism of action

The bacterial cell wall, which is located at the periphery of Gram-positive bacteria and within the periplasm of Gram-negative bacteria, comprises a glycopeptide polymer synthesized through cross-linking of glycans to peptide stems on alternating saccharides, which is known commonly as peptidoglycan.1 Cell wall formation, recycling, and remodelling require numerous enzymes, including a family of enzymes with similar active site character despite distinct and sometimes overlapping roles as carboxypeptidases, endopeptidases, transpeptidases, and transglycosylases, known as "penicillin-binding proteins" (PBPs). The number of PBPs differs between bacteria, in which some are considered essential and others redundant. In general, inhibition of one or more essential PBPs results in impaired cell wall homeostasis, loss of cell integrity, and is ultimately bactericidal.1,2,3

Ceftazidime is a semisynthetic third-generation cephalosporin with broad activity against numerous Gram-negative and some Gram-positive bacteria.12 Like other β-lactam antibiotics, ceftazidime exhibits its bactericidal effect primarily through direct inhibition of specific PBPs in susceptible bacteria.4 In vitro experiments in Gram-negative bacteria such as Escherichia coli, Pseudomonas aeruginosa, Acinetobacter baumannii, and Klebsiella pneumoniae suggest that ceftazidime primarily binds to PBP3, with weaker binding to PBP1a/1b and PBP2 as well; although binding to other PBPs, such as PBP4, is detectable, the concentrations required are much greater than those achieved clinically.4,5,6,7,8 Similarly, ceftazidime showed binding to Staphylococcus aureus PBP 1, 2, and 3 with a much lower affinity for PBP4.5 Recent data for Mycobacterium abcessus suggest that ceftazidime can inhibit PonA1, PonA2, and PbpA at intermediate concentrations.3

TargetActionsOrganism
APeptidoglycan synthase FtsI
inhibitor
Escherichia coli (strain K12)
APenicillin-binding protein 1A
inhibitor
Escherichia coli (strain K12)
APenicillin-binding protein 1B
inhibitor
Escherichia coli (strain K12)
APenicillin-binding protein 2
inhibitor
Escherichia coli (strain K12)
UBeta-lactamase Toho-1
substrate
Escherichia coli
Absorption

Ceftazidime administered intravenously in healthy males produced mean Cmax values of between 42 and 170 μg/mL for doses between 500 mg and 2 g, and are reached immediately following the end of the infusion period.12 The Cmax for 1 g of ceftazidime administered intramuscularly is attained approximately one hour following injection and is between 37 and 43 mg/L.4 Following intramuscular administration of 500 mg and 1 g of ceftazidime, the serum concentration remained above 4 μg/mL for six and eight hours, respectively.12

Ceftazidime Cmax and AUC show linear proportionality to the dose over the therapeutic range.4,12 In individuals with normal renal function, ceftazidime given intravenously every eight hours for 10 days as either 1 or 2 g doses showed no accumulation.12

Volume of distribution

Ceftazidime has a volume of distribution of 15-20 L.4

Protein binding

Ceftazidime plasma protein binding ranges from 5-22.8% (typically less than 10%) and is independent of concentration.4,12 Ceftazidime has been shown to bind human serum albumin.10,11

Metabolism

Ceftazidime is not appreciably metabolized.4

Route of elimination

Approximately 80% to 90% of an intramuscular or intravenous dose of ceftazidime is excreted unchanged by the kidneys over a 24-hour period. When administered intravenously, 50% of the dose appears in the urine within two hours, with another 32% of the dose appearing by eight hours post-administration.12

Half-life

Ceftazidime has an elimination half-life of 1.5-2.8 hours in healthy subjects.4,12 As ceftazidime is primarily renally excreted, its half-life is significantly prolonged in patients with renal impairment.12 In patients with creatinine clearance < 12 mL/min, the half-life is prolonged to between 14 and 30 hours.4

Clearance

The mean renal clearance of ceftazidime in healthy subjects ranges from 72 to 141 mL/min while the calculated plasma clearance is approximately 115 mL/min.4,12

Adverse Effects
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Toxicity

Ceftazidime overdosage has occurred in patients with renal failure. Reactions included seizure activity, encephalopathy, asterixis, neuromuscular excitability, and coma. Patients who receive an acute overdosage should be carefully observed and given supportive treatment. In the presence of renal insufficiency, hemodialysis or peritoneal dialysis may aid in the removal of ceftazidime from the body.12

Pathways
Not Available
Pharmacogenomic Effects/ADRs
Not Available

Interactions

Drug Interactions
This information should not be interpreted without the help of a healthcare provider. If you believe you are experiencing an interaction, contact a healthcare provider immediately. The absence of an interaction does not necessarily mean no interactions exist.
DrugInteraction
AbacavirCeftazidime may decrease the excretion rate of Abacavir which could result in a higher serum level.
AbciximabThe therapeutic efficacy of Abciximab can be decreased when used in combination with Ceftazidime.
AceclofenacThe risk or severity of nephrotoxicity can be increased when Ceftazidime is combined with Aceclofenac.
AcemetacinThe risk or severity of nephrotoxicity can be increased when Ceftazidime is combined with Acemetacin.
AcenocoumarolThe risk or severity of bleeding can be increased when Ceftazidime is combined with Acenocoumarol.
Food Interactions
No interactions found.

Products

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Product Ingredients
IngredientUNIICASInChI Key
Ceftazidime pentahydrate9M416Z9QNR78439-06-2NMVPEQXCMGEDNH-TZVUEUGBSA-N
Ceftazidime sodiumCMC30V039K73547-61-2JEEWDSDYUSEQML-ROMZVAKDSA-M
International/Other Brands
Cefzim (Pharco B International) / Ceptaz / Fortum (GlaxoSmithKline) / Tazidime / Veltadim (Novell)
Brand Name Prescription Products
NameDosageStrengthRouteLabellerMarketing StartMarketing EndRegionImage
Ceftazidime and DextroseInjection, solution1 g/50mLIntravenousB. Braun Medical Inc.2011-06-13Not applicableUS flag
Ceftazidime and DextroseInjection, solution2 g/50mLIntravenousB. Braun Medical Inc.2011-06-13Not applicableUS flag
Ceftazidime for Injection BPPowder, for solution6 g / vialIntravenousSterimax Inc2015-06-08Not applicableCanada flag
Ceftazidime for Injection BPPowder, for solution2 g / vialIntravenousSterimax Inc2015-05-29Not applicableCanada flag
Ceftazidime for Injection BPPowder, for solution1 g / vialIntramuscular; IntravenousSterimax Inc2015-05-28Not applicableCanada flag
Generic Prescription Products
NameDosageStrengthRouteLabellerMarketing StartMarketing EndRegionImage
CeftazidimeInjection, powder, for solution1 g/1Intramuscular; IntravenousPfizer Laboratories, Division of Pfizer Inc2010-05-282012-06-30US flag
CeftazidimeInjection, powder, for solution1 g/1Intramuscular; IntravenousAurobindo Pharma (Italia) S.R.L.2010-05-282012-06-30US flag
CeftazidimeInjection, powder, for solution1 g/1Intramuscular; IntravenousSagent Pharmaceuticals2015-07-012022-01-31US flag
CeftazidimeInjection, powder, for solution2 g/1IntravenousSandoz S.P.A.2008-05-15Not applicableUS flag
CeftazidimeInjection, powder, for solution200 mg/1mLIntravenousAurobindo Pharma (Italia) S.R.L.2010-05-282012-10-31US flag
Mixture Products
NameIngredientsDosageRouteLabellerMarketing StartMarketing EndRegionImage
AvycazCeftazidime pentahydrate (2 g/1) + Avibactam sodium (0.5 g/1)Powder, for solutionIntravenousAllergan, Inc.2014-12-26Not applicableUS flag
CEFAZIME FOR INJECTION 1 g/vialCeftazidime pentahydrate (1 g) + Sodium carbonate (121 mg)InjectionIntramuscular; IntravenousZYFAS MEDICAL CO2001-03-26Not applicableSingapore flag
CEFTAZIDIMA QILUCeftazidime pentahydrate (2 G) + Sodium carbonate (256 mg)Injection, powder, for solutionParenteralQilu Pharma Spain S.L.2019-07-11Not applicableItaly flag
CEFTAZIDIMA QILUCeftazidime pentahydrate (500 MG) + Sodium carbonate (64 mg)Injection, powder, for solutionParenteralQilu Pharma Spain S.L.2019-07-112023-02-09Italy flag
CEFTAZIDIMA QILUCeftazidime pentahydrate (1 G) + Sodium carbonate (128 mg)Injection, powder, for solutionParenteralQilu Pharma Spain S.L.2019-07-11Not applicableItaly flag

Categories

ATC Codes
J01DD02 — Ceftazidime
Drug Categories
Chemical TaxonomyProvided by Classyfire
Description
This compound belongs to the class of organic compounds known as cephalosporins. These are compounds containing a 1,2-thiazine fused to a 2-azetidinone to for a oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid moiety or a derivative thereof.
Kingdom
Organic compounds
Super Class
Organoheterocyclic compounds
Class
Lactams
Sub Class
Beta lactams
Direct Parent
Cephalosporins
Alternative Parents
N-acyl-alpha amino acids and derivatives / 2,4-disubstituted thiazoles / 1,3-thiazines / Pyridinium derivatives / 2-amino-1,3-thiazoles / Dicarboxylic acids and derivatives / Tertiary carboxylic acid amides / Heteroaromatic compounds / Secondary carboxylic acid amides / Amino acids
show 13 more
Substituents
1,3-thiazol-2-amine / 2,4-disubstituted 1,3-thiazole / Alpha-amino acid or derivatives / Amine / Amino acid / Amino acid or derivatives / Aromatic heteropolycyclic compound / Azacycle / Azetidine / Azole
show 28 more
Molecular Framework
Aromatic heteropolycyclic compounds
External Descriptors
cephalosporin, oxime O-ether (CHEBI:3508)
Affected organisms
  • Enteric bacteria and other eubacteria

Chemical Identifiers

UNII
DZR1ENT301
CAS number
72558-82-8
InChI Key
ORFOPKXBNMVMKC-DWVKKRMSSA-N
InChI
InChI=1S/C22H22N6O7S2/c1-22(2,20(33)34)35-26-13(12-10-37-21(23)24-12)16(29)25-14-17(30)28-15(19(31)32)11(9-36-18(14)28)8-27-6-4-3-5-7-27/h3-7,10,14,18H,8-9H2,1-2H3,(H4-,23,24,25,29,31,32,33,34)/b26-13-/t14-,18-/m1/s1
IUPAC Name
1-{[(6R,7R)-7-[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-[(1-carboxy-1-methylethoxy)imino]acetamido]-2-carboxylato-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-en-3-yl]methyl}pyridin-1-ium
SMILES
[O-]C(=O)C1=C(CS[C@]2([H])[C@H](NC(=O)C(=N/OC(C)(C)C(O)=O)\C3=CSC(N)=N3)C(=O)N12)C[N+]1=CC=CC=C1

References

Synthesis Reference

Ronald C. Browning, Melvin G. Pleiss, Jr., "Crystallization process for ceftazidime derivative." U.S. Patent US4659813, issued May, 1982.

US4659813
General References
  1. Fisher JF, Mobashery S: Constructing and deconstructing the bacterial cell wall. Protein Sci. 2020 Mar;29(3):629-646. doi: 10.1002/pro.3737. Epub 2019 Nov 20. [Article]
  2. Bush K, Bradford PA: beta-Lactams and beta-Lactamase Inhibitors: An Overview. Cold Spring Harb Perspect Med. 2016 Aug 1;6(8). pii: cshperspect.a025247. doi: 10.1101/cshperspect.a025247. [Article]
  3. Sayed ARM, Shah NR, Basso KB, Kamat M, Jiao Y, Moya B, Sutaria DS, Lang Y, Tao X, Liu W, Shin E, Zhou J, Werkman C, Louie A, Drusano GL, Bulitta JB: First Penicillin-Binding Protein Occupancy Patterns for 15 beta-Lactams and beta-Lactamase Inhibitors in Mycobacterium abscessus. Antimicrob Agents Chemother. 2020 Dec 16;65(1). pii: AAC.01956-20. doi: 10.1128/AAC.01956-20. Print 2020 Dec 16. [Article]
  4. Richards DM, Brogden RN: Ceftazidime. A review of its antibacterial activity, pharmacokinetic properties and therapeutic use. Drugs. 1985 Feb;29(2):105-61. doi: 10.2165/00003495-198529020-00002. [Article]
  5. Hayes MV, Orr DC: Mode of action of ceftazidime: affinity for the penicillin-binding proteins of Escherichia coli K12, Pseudomonas aeruginosa and Staphylococcus aureus. J Antimicrob Chemother. 1983 Aug;12(2):119-26. [Article]
  6. Davies TA, Shang W, Bush K, Flamm RK: Affinity of doripenem and comparators to penicillin-binding proteins in Escherichia coli and Pseudomonas aeruginosa. Antimicrob Agents Chemother. 2008 Apr;52(4):1510-2. doi: 10.1128/AAC.01529-07. Epub 2008 Feb 4. [Article]
  7. Penwell WF, Shapiro AB, Giacobbe RA, Gu RF, Gao N, Thresher J, McLaughlin RE, Huband MD, DeJonge BL, Ehmann DE, Miller AA: Molecular mechanisms of sulbactam antibacterial activity and resistance determinants in Acinetobacter baumannii. Antimicrob Agents Chemother. 2015 Mar;59(3):1680-9. doi: 10.1128/AAC.04808-14. Epub 2015 Jan 5. [Article]
  8. Sutaria DS, Moya B, Green KB, Kim TH, Tao X, Jiao Y, Louie A, Drusano GL, Bulitta JB: First Penicillin-Binding Protein Occupancy Patterns of beta-Lactams and beta-Lactamase Inhibitors in Klebsiella pneumoniae. Antimicrob Agents Chemother. 2018 May 25;62(6). pii: AAC.00282-18. doi: 10.1128/AAC.00282-18. Print 2018 Jun. [Article]
  9. Shirley M: Ceftazidime-Avibactam: A Review in the Treatment of Serious Gram-Negative Bacterial Infections. Drugs. 2018 Apr;78(6):675-692. doi: 10.1007/s40265-018-0902-x. [Article]
  10. Nerli B, Romanini D, Pico G: Structural specificity requirements in the binding of beta lactam antibiotics to human serum albumin. Chem Biol Interact. 1997 May 2;104(2-3):179-202. [Article]
  11. Siddiqi MK, Alam P, Chaturvedi SK, Nusrat S, Ajmal MR, Abdelhameed AS, Khan RH: Probing the interaction of cephalosporin antibiotic-ceftazidime with human serum albumin: A biophysical investigation. Int J Biol Macromol. 2017 Dec;105(Pt 1):292-299. doi: 10.1016/j.ijbiomac.2017.07.036. Epub 2017 Jul 8. [Article]
  12. FDA Approved Drug Products: FORTAZ (ceftazidime) injection [Link]
  13. FDA Approved Drug Products: AVYCAZ (ceftazidime and avibactam) injection [Link]
  14. Cayman Chemical: ceftazidime MSDS [Link]
  15. FDA Approved Drug Products: AVYCAZ (ceftazidime and avibactam) injection for intravenous use (December 2022) [Link]
Human Metabolome Database
HMDB0014582
KEGG Drug
D07654
KEGG Compound
C06889
PubChem Compound
5481173
PubChem Substance
46506143
ChemSpider
4587145
BindingDB
50420259
RxNav
1545984
ChEBI
3508
ChEMBL
CHEMBL44354
Therapeutic Targets Database
DAP000433
PharmGKB
PA448861
RxList
RxList Drug Page
Drugs.com
Drugs.com Drug Page
Wikipedia
Ceftazidime
FDA label
Download (360 KB)
MSDS
Download (28 KB)

Clinical Trials

Clinical Trials
Clinical Trial & Rare Diseases Add-on Data Package
Explore 4,000+ rare diseases, orphan drugs & condition pairs, clinical trial why stopped data, & more. Preview package
PhaseStatusPurposeConditionsCountStart DateWhy Stopped100+ additional columns
Not AvailableActive Not RecruitingNot AvailableSevere Sepsis1somestatusstop reasonjust information to hide
Not AvailableCompletedNot AvailableAcute Kidney Injury (AKI) / Haemodiafiltration / Sepsis1somestatusstop reasonjust information to hide
Not AvailableCompletedNot AvailableBacterial Infections1somestatusstop reasonjust information to hide
Not AvailableCompletedNot AvailableBacterial Keratitis / Fungal infections of the cornea / Microbial Keratitis / Mixed Bacterial and Fungal Keratitis1somestatusstop reasonjust information to hide
Not AvailableCompletedNot AvailableCarbapenem Resistant Enterobacteriaceae Infection1somestatusstop reasonjust information to hide

Pharmacoeconomics

Manufacturers
  • Acs dobfar spa
  • Aurobindo pharma ltd
  • Wockhardt ltd
  • Glaxosmithkline
  • Hospira inc
  • Eli lilly and co
  • Baxter healthcare corp
Packagers
  • Antibioticos Ltd.
  • Aurobindo Pharma Ltd.
  • Baxter International Inc.
  • BMH Ltd.
  • Cardinal Health
  • GlaxoSmithKline Inc.
  • Hospira Inc.
  • Medisca Inc.
  • Sagent Pharmaceuticals
  • Sandoz
  • Wockhardt Ltd.
Dosage Forms
FormRouteStrength
SolutionParenteral1000 mg
Powder, for solutionIntravenous
InjectionIntramuscular; Intravenous1 gr
InjectionIntramuscular; Intravenous2 gr
Injection, powder, for solutionIntramuscular; Intravenous
InjectionIntramuscular; Intravenous1 g
Injection1 g
Injection, powder, for solutionParenteral1 g
Injection, powder, for solutionParenteral
Injection, powder, for solutionParenteral2 g
Injection, powder, for solutionParenteral500 mg
SolutionParenteral1.165 g
Injection, powder, for solutionIntramuscular1 G/3ML
Injection, powder, for solutionIntramuscular250 MG/1ML
Injection, powder, for solutionIntramuscular500 MG/1.5ML
Injection, powder, for solutionIntravenous1 G/10ML
Powder, for solutionParenteral2 G
Injection, powder, for solutionIntramuscular; Parenteral1 G/3ML
Injection, powder, for solutionIntramuscular; Parenteral250 MG/1ML
Injection, powder, for solutionIntramuscular; Parenteral500 MG/1.5ML
Injection, powder, for solutionIntravenous; Parenteral1 G/10ML
Injection, powder, for solution1000 MG
Injection, powder, for solution2000 MG
Injection, powder, for solutionIntramuscular250 MG/ML
Injection, powder, for solutionIntramuscular; Parenteral250 MG/ML
Injection, powder, for solutionParenteral
Injection, powder, for solutionIntramuscular; Parenteral1 G
Injection, powder, for solutionIntravenous; Parenteral1 G
Powder, for solution2 G
Injection, powder, for solutionIntramuscular; Intravenous1 g/1
Injection, powder, for solutionIntramuscular; Intravenous1000 mg
Injection, powder, for solutionIntramuscular; Intravenous500 mg/1
Injection, powder, for solutionIntravenous2 g/1
Injection, powder, for solutionIntravenous200 mg/1mL
Injection, powder, for solutionIntravenous6 g/30mL
Injection, powder, for solutionIntravenous6 g/100mL
Injection, powder, for solutionIntramuscular; Intravenous1.0 g
Injection, solutionIntravenous1 g/50mL
Injection, solutionIntravenous2 g/50mL
Powder, for solutionIntravenous3 g / vial
Powder, for solutionIntravenous6 g / vial
Injection, powder, for solutionIntramuscular; Intravenous1000 mgvial
Injection, powder, for solutionIntravenous2000 mg
Injection, powder, for solution1 g
Injection, powder, for solution1.34 g
Injection, powder, for solutionParenteral1.0 g
Injection
Injection, powder, for solution500 mg
Injection, powder, for solution
Powder, for solutionIntravenous10 g / vial
Powder, for solutionIntramuscular; Intravenous1 g / vial
Powder, for solutionIntravenous2 g / vial
SolutionParenteral1.000 g
SolutionIntravenous2.000 mL
Injection, powder, for solutionIntramuscular; Intravenous100 mg/1mL
Injection, powder, for solutionIntramuscular; Intravenous111 mg/1mL
Injection, powder, for solutionIntramuscular; Intravenous170 mg/1mL
Injection, powder, for solutionIntramuscular; Intravenous20 mg/1mL
Injection, powder, for solutionIntramuscular; Intravenous200 mg/1mL
Injection, powder, for solutionIntramuscular; Intravenous56 mg/1mL
Injection, powder, lyophilized, for solutionIntramuscular; Intravenous1 g/1
Injection, powder, lyophilized, for solutionIntramuscular; Intravenous2 g/1
Injection, solutionIntravenous20 mg/1mL
Injection, solutionIntravenous40 mg/1mL
Powder, for solutionIntramuscular; Intravenous500 mg / vial
Injection, powder, for solution1212 mg
Injection, powder, for solutionIntramuscular; Intravenous1 g
Injection, powder, for solutionIntravenous2 g
InjectionIntramuscular; Intravenous1 g
InjectionIntramuscular; Intravenous
PowderIntramuscular250 MG/1ML
PowderIntravenous1 G/10ML
Powder, for solution1 G/100ML
Powder, for solution1 G
Powder, for solution2 G/100ML
InjectionIntravenous0.5 g
InjectionIntravenous1 g
InjectionIntravenous2 g
Injection, powder, for solutionIntramuscular
Injection, powder, for solutionIntramuscular; Intravenous500 mg
Injection, powder, for solutionIntravenous
Powder, for solution
Injection, powder, for solutionIntravenous1 g
Injection, powder, for solutionParenteral1 G/3ML
Injection, powder, for solutionParenteral250 MG/1ML
Injection, powder, for solutionParenteral500 MG/1.5ML
Injection, powder, for solutionIntravenous1 g/1
Injection, powder, for solutionIntravenous6 g/1
Powder, for solutionIntravenous1 g / vial
PowderIntramuscular; Intravenous500 mg / vial
Injection, powder, for solutionIntramuscular; Intravenous1 g/vial
Injection, powder, for solution
Injection, powder, for solutionIntravenous
Injection, powder, for solutionIntravenous; Parenteral
Powder, for solutionIntravenous0.5 g
SolutionIntravenous
Injection, powder, for solutionIntramuscular; Intravenous0.5 g
Injection, solutionIntravenous2 g
Powder500 mg/1vial
Prices
Unit descriptionCostUnit
Fortaz 6 g/vial150.11USD vial
Ceftazidime 6 gm vial97.05USD vial
Fortaz 6 gm vial82.8USD vial
Fortaz 2 g/vial50.01USD vial
Tazicef 6 gram vial29.88USD vial
Fortaz 2 gm add-vantage vial28.93USD vial
Fortaz 2 gm vial28.45USD vial
Fortaz 1 g/vial25.44USD vial
Ceftazidime 2 gm vial19.97USD vial
Fortaz 1 gm add-vantage vial14.71USD vial
Fortaz 1 gm vial14.23USD vial
Tazicef 2 gram vial10.66USD vial
Ceftazidime 1 gm vial10.46USD vial
Ceftazidime-sodium carb powder6.27USD g
Tazicef 1 gram vial4.57USD vial
Fortaz-iso-osmot 2 gm/50 ml0.62USD ml
Fortaz-iso-osmotic 1 gm/50 ml0.34USD ml
DrugBank does not sell nor buy drugs. Pricing information is supplied for informational purposes only.
Patents
Patent NumberPediatric ExtensionApprovedExpires (estimated)Region
US7112592No2006-09-262022-02-24US flag
US8178554No2012-05-152021-07-24US flag
US7612087No2009-11-032026-11-12US flag
US8471025No2013-06-252031-08-12US flag
US8835455No2014-09-162030-10-08US flag
US8969566No2015-03-032032-06-15US flag
US9284314No2016-03-152032-06-15US flag
US9695122No2017-07-042032-06-15US flag

Properties

State
Solid
Experimental Properties
PropertyValueSource
melting point (°C)103-113O'Callaghan, C.H., Livermore, D.G.H. and Newall, C.E.; British Patent 2,025,398; January 23, 1980; assigned to Glaxo Group Ltd.
logP-1.60HANSCH,C ET AL. (1995)
Predicted Properties
PropertyValueSource
Water Solubility0.00573 mg/mLALOGPS
logP-1.2ALOGPS
logP-4.2Chemaxon
logS-5ALOGPS
pKa (Strongest Acidic)2.42Chemaxon
pKa (Strongest Basic)4.02Chemaxon
Physiological Charge-1Chemaxon
Hydrogen Acceptor Count10Chemaxon
Hydrogen Donor Count3Chemaxon
Polar Surface Area191.22 Å2Chemaxon
Rotatable Bond Count9Chemaxon
Refractivity143.88 m3·mol-1Chemaxon
Polarizability51.03 Å3Chemaxon
Number of Rings4Chemaxon
Bioavailability1Chemaxon
Rule of FiveNoChemaxon
Ghose FilterNoChemaxon
Veber's RuleNoChemaxon
MDDR-like RuleYesChemaxon
Predicted ADMET Features
PropertyValueProbability
Human Intestinal Absorption-0.8406
Blood Brain Barrier-0.9857
Caco-2 permeable-0.7235
P-glycoprotein substrateSubstrate0.8593
P-glycoprotein inhibitor INon-inhibitor0.8782
P-glycoprotein inhibitor IIInhibitor0.6684
Renal organic cation transporterNon-inhibitor0.8311
CYP450 2C9 substrateNon-substrate0.8404
CYP450 2D6 substrateNon-substrate0.8155
CYP450 3A4 substrateSubstrate0.5897
CYP450 1A2 substrateNon-inhibitor0.8112
CYP450 2C9 inhibitorNon-inhibitor0.7396
CYP450 2D6 inhibitorNon-inhibitor0.8758
CYP450 2C19 inhibitorNon-inhibitor0.7009
CYP450 3A4 inhibitorNon-inhibitor0.8354
CYP450 inhibitory promiscuityLow CYP Inhibitory Promiscuity0.7222
Ames testNon AMES toxic0.7979
CarcinogenicityNon-carcinogens0.8252
BiodegradationNot ready biodegradable0.9951
Rat acute toxicity1.6048 LD50, mol/kg Not applicable
hERG inhibition (predictor I)Weak inhibitor0.9938
hERG inhibition (predictor II)Non-inhibitor0.659
ADMET data is predicted using admetSAR, a free tool for evaluating chemical ADMET properties. (23092397)

Spectra

Mass Spec (NIST)
Not Available
Spectra
SpectrumSpectrum TypeSplash Key
Predicted GC-MS Spectrum - GC-MSPredicted GC-MSsplash10-0fb9-9681160000-8d070b22df5da67959c7
LC-MS/MS Spectrum - LC-ESI-QFT , negativeLC-MS/MSsplash10-0udi-1900000000-35c537be0b49e8347500
LC-MS/MS Spectrum - LC-ESI-QFT , negativeLC-MS/MSsplash10-0udi-3900000000-f8108350d09aeabb208f
LC-MS/MS Spectrum - LC-ESI-QFT , negativeLC-MS/MSsplash10-0pb9-9600000000-3a117de626550cd6bd1e
LC-MS/MS Spectrum - LC-ESI-QFT , negativeLC-MS/MSsplash10-0a4i-9200000000-42d1f87964b083915995
LC-MS/MS Spectrum - LC-ESI-QFT , negativeLC-MS/MSsplash10-0a4i-9100000000-9b08b7904165504611b6
LC-MS/MS Spectrum - LC-ESI-QFT , positiveLC-MS/MSsplash10-014j-0115900000-d76de6ad1809c0528b8c
LC-MS/MS Spectrum - LC-ESI-QFT , positiveLC-MS/MSsplash10-0006-1910000000-cb7ea1c7b4b139a7336e
LC-MS/MS Spectrum - LC-ESI-QFT , positiveLC-MS/MSsplash10-01tl-3900000000-07fadc61e1b566ec14ba
LC-MS/MS Spectrum - LC-ESI-QFT , positiveLC-MS/MSsplash10-004i-5900000000-e92b85ec9fabd9a4c1fe
LC-MS/MS Spectrum - LC-ESI-QFT , positiveLC-MS/MSsplash10-004i-7900000000-548213f534e499ba783b
Chromatographic Properties
Collision Cross Sections (CCS)
AdductCCS Value (Å2)Source typeSource
[M-H]-214.267802
predicted
DarkChem Lite v0.1.0
[M-H]-218.78352
predicted
DeepCCS 1.0 (2019)
[M+H]+213.063202
predicted
DarkChem Lite v0.1.0
[M+H]+220.71751
predicted
DeepCCS 1.0 (2019)
[M+Na]+214.182702
predicted
DarkChem Lite v0.1.0
[M+Na]+226.45793
predicted
DeepCCS 1.0 (2019)

Targets

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Kind
Protein
Organism
Escherichia coli (strain K12)
Pharmacological action
Yes
Actions
Inhibitor
Curator comments
The above was chosen as a representative target protein in a representative bacterium, and does not encompass all proteins/bacteria affected by this agent.
General Function
Essential cell division protein that catalyzes cross-linking of the peptidoglycan cell wall at the division septum (PubMed:1103132, PubMed:3531167, PubMed:6450748, PubMed:7030331, PubMed:9614966). Required for localization of FtsN (PubMed:9282742).
Specific Function
penicillin binding
Gene Name
ftsI
Uniprot ID
P0AD68
Uniprot Name
Peptidoglycan synthase FtsI
Molecular Weight
63876.925 Da
References
  1. Hayes MV, Orr DC: Mode of action of ceftazidime: affinity for the penicillin-binding proteins of Escherichia coli K12, Pseudomonas aeruginosa and Staphylococcus aureus. J Antimicrob Chemother. 1983 Aug;12(2):119-26. [Article]
  2. Richards DM, Brogden RN: Ceftazidime. A review of its antibacterial activity, pharmacokinetic properties and therapeutic use. Drugs. 1985 Feb;29(2):105-61. doi: 10.2165/00003495-198529020-00002. [Article]
  3. Davies TA, Shang W, Bush K, Flamm RK: Affinity of doripenem and comparators to penicillin-binding proteins in Escherichia coli and Pseudomonas aeruginosa. Antimicrob Agents Chemother. 2008 Apr;52(4):1510-2. doi: 10.1128/AAC.01529-07. Epub 2008 Feb 4. [Article]
  4. Penwell WF, Shapiro AB, Giacobbe RA, Gu RF, Gao N, Thresher J, McLaughlin RE, Huband MD, DeJonge BL, Ehmann DE, Miller AA: Molecular mechanisms of sulbactam antibacterial activity and resistance determinants in Acinetobacter baumannii. Antimicrob Agents Chemother. 2015 Mar;59(3):1680-9. doi: 10.1128/AAC.04808-14. Epub 2015 Jan 5. [Article]
  5. Sutaria DS, Moya B, Green KB, Kim TH, Tao X, Jiao Y, Louie A, Drusano GL, Bulitta JB: First Penicillin-Binding Protein Occupancy Patterns of beta-Lactams and beta-Lactamase Inhibitors in Klebsiella pneumoniae. Antimicrob Agents Chemother. 2018 May 25;62(6). pii: AAC.00282-18. doi: 10.1128/AAC.00282-18. Print 2018 Jun. [Article]
Kind
Protein
Organism
Escherichia coli (strain K12)
Pharmacological action
Yes
Actions
Inhibitor
Curator comments
The above was chosen as a representative target protein in a representative bacterium, and does not encompass all proteins/bacteria affected by this agent.
General Function
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).
Specific Function
penicillin binding
Gene Name
mrcA
Uniprot ID
P02918
Uniprot Name
Penicillin-binding protein 1A
Molecular Weight
93635.545 Da
References
  1. Hayes MV, Orr DC: Mode of action of ceftazidime: affinity for the penicillin-binding proteins of Escherichia coli K12, Pseudomonas aeruginosa and Staphylococcus aureus. J Antimicrob Chemother. 1983 Aug;12(2):119-26. [Article]
  2. Richards DM, Brogden RN: Ceftazidime. A review of its antibacterial activity, pharmacokinetic properties and therapeutic use. Drugs. 1985 Feb;29(2):105-61. doi: 10.2165/00003495-198529020-00002. [Article]
  3. Davies TA, Shang W, Bush K, Flamm RK: Affinity of doripenem and comparators to penicillin-binding proteins in Escherichia coli and Pseudomonas aeruginosa. Antimicrob Agents Chemother. 2008 Apr;52(4):1510-2. doi: 10.1128/AAC.01529-07. Epub 2008 Feb 4. [Article]
  4. Penwell WF, Shapiro AB, Giacobbe RA, Gu RF, Gao N, Thresher J, McLaughlin RE, Huband MD, DeJonge BL, Ehmann DE, Miller AA: Molecular mechanisms of sulbactam antibacterial activity and resistance determinants in Acinetobacter baumannii. Antimicrob Agents Chemother. 2015 Mar;59(3):1680-9. doi: 10.1128/AAC.04808-14. Epub 2015 Jan 5. [Article]
  5. Sutaria DS, Moya B, Green KB, Kim TH, Tao X, Jiao Y, Louie A, Drusano GL, Bulitta JB: First Penicillin-Binding Protein Occupancy Patterns of beta-Lactams and beta-Lactamase Inhibitors in Klebsiella pneumoniae. Antimicrob Agents Chemother. 2018 May 25;62(6). pii: AAC.00282-18. doi: 10.1128/AAC.00282-18. Print 2018 Jun. [Article]
Kind
Protein
Organism
Escherichia coli (strain K12)
Pharmacological action
Yes
Actions
Inhibitor
Curator comments
The above was chosen as a representative target protein in a representative bacterium, and does not encompass all proteins/bacteria affected by this agent.
General Function
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).
Specific Function
penicillin binding
Gene Name
mrcB
Uniprot ID
P02919
Uniprot Name
Penicillin-binding protein 1B
Molecular Weight
94291.875 Da
References
  1. Hayes MV, Orr DC: Mode of action of ceftazidime: affinity for the penicillin-binding proteins of Escherichia coli K12, Pseudomonas aeruginosa and Staphylococcus aureus. J Antimicrob Chemother. 1983 Aug;12(2):119-26. [Article]
  2. Richards DM, Brogden RN: Ceftazidime. A review of its antibacterial activity, pharmacokinetic properties and therapeutic use. Drugs. 1985 Feb;29(2):105-61. doi: 10.2165/00003495-198529020-00002. [Article]
  3. Davies TA, Shang W, Bush K, Flamm RK: Affinity of doripenem and comparators to penicillin-binding proteins in Escherichia coli and Pseudomonas aeruginosa. Antimicrob Agents Chemother. 2008 Apr;52(4):1510-2. doi: 10.1128/AAC.01529-07. Epub 2008 Feb 4. [Article]
  4. Penwell WF, Shapiro AB, Giacobbe RA, Gu RF, Gao N, Thresher J, McLaughlin RE, Huband MD, DeJonge BL, Ehmann DE, Miller AA: Molecular mechanisms of sulbactam antibacterial activity and resistance determinants in Acinetobacter baumannii. Antimicrob Agents Chemother. 2015 Mar;59(3):1680-9. doi: 10.1128/AAC.04808-14. Epub 2015 Jan 5. [Article]
  5. Sutaria DS, Moya B, Green KB, Kim TH, Tao X, Jiao Y, Louie A, Drusano GL, Bulitta JB: First Penicillin-Binding Protein Occupancy Patterns of beta-Lactams and beta-Lactamase Inhibitors in Klebsiella pneumoniae. Antimicrob Agents Chemother. 2018 May 25;62(6). pii: AAC.00282-18. doi: 10.1128/AAC.00282-18. Print 2018 Jun. [Article]
Kind
Protein
Organism
Escherichia coli (strain K12)
Pharmacological action
Yes
Actions
Inhibitor
Curator comments
The above was chosen as a representative target protein in a representative bacterium, and does not encompass all proteins/bacteria affected by this agent.
General Function
Catalyzes cross-linking of the peptidoglycan cell wall (PubMed:3009484). Responsible for the determination of the rod shape of the cell (PubMed:1103132). Is probably required for lateral peptidoglycan synthesis and maintenance of the correct diameter during lateral and centripetal growth (PubMed:12519203).
Specific Function
penicillin binding
Gene Name
mrdA
Uniprot ID
P0AD65
Uniprot Name
Penicillin-binding protein 2
Molecular Weight
70856.1 Da
References
  1. Hayes MV, Orr DC: Mode of action of ceftazidime: affinity for the penicillin-binding proteins of Escherichia coli K12, Pseudomonas aeruginosa and Staphylococcus aureus. J Antimicrob Chemother. 1983 Aug;12(2):119-26. [Article]
  2. Richards DM, Brogden RN: Ceftazidime. A review of its antibacterial activity, pharmacokinetic properties and therapeutic use. Drugs. 1985 Feb;29(2):105-61. doi: 10.2165/00003495-198529020-00002. [Article]
  3. Davies TA, Shang W, Bush K, Flamm RK: Affinity of doripenem and comparators to penicillin-binding proteins in Escherichia coli and Pseudomonas aeruginosa. Antimicrob Agents Chemother. 2008 Apr;52(4):1510-2. doi: 10.1128/AAC.01529-07. Epub 2008 Feb 4. [Article]
  4. Penwell WF, Shapiro AB, Giacobbe RA, Gu RF, Gao N, Thresher J, McLaughlin RE, Huband MD, DeJonge BL, Ehmann DE, Miller AA: Molecular mechanisms of sulbactam antibacterial activity and resistance determinants in Acinetobacter baumannii. Antimicrob Agents Chemother. 2015 Mar;59(3):1680-9. doi: 10.1128/AAC.04808-14. Epub 2015 Jan 5. [Article]
  5. Sutaria DS, Moya B, Green KB, Kim TH, Tao X, Jiao Y, Louie A, Drusano GL, Bulitta JB: First Penicillin-Binding Protein Occupancy Patterns of beta-Lactams and beta-Lactamase Inhibitors in Klebsiella pneumoniae. Antimicrob Agents Chemother. 2018 May 25;62(6). pii: AAC.00282-18. doi: 10.1128/AAC.00282-18. Print 2018 Jun. [Article]
Kind
Protein
Organism
Escherichia coli
Pharmacological action
Unknown
Actions
Substrate
General Function
Has strong cefotaxime-hydrolyzing activity.
Specific Function
beta-lactamase activity
Gene Name
bla
Uniprot ID
Q47066
Uniprot Name
Beta-lactamase Toho-1
Molecular Weight
31446.6 Da
References
  1. Ishii Y, Ohno A, Taguchi H, Imajo S, Ishiguro M, Matsuzawa H: Cloning and sequence of the gene encoding a cefotaxime-hydrolyzing class A beta-lactamase isolated from Escherichia coli. Antimicrob Agents Chemother. 1995 Oct;39(10):2269-75. [Article]

Carriers

Kind
Protein
Organism
Humans
Pharmacological action
No
Actions
Binder
General Function
Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs (Probable). Its main function is the regulation of the colloidal osmotic pressure of blood (Probable). Major zinc transporter in plasma, typically binds about 80% of all plasma zinc (PubMed:19021548). Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (By similarity). Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (By similarity). The shared binding site between zinc and calcium at residue Asp-273 suggests a crosstalk between zinc and calcium transport in the blood (By similarity). The rank order of affinity is zinc > calcium > magnesium (By similarity). Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli from ferric transferrin, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli (PubMed:6234017). Does not prevent iron uptake by the bacterial siderophore aerobactin (PubMed:6234017)
Specific Function
antioxidant activity
Gene Name
ALB
Uniprot ID
P02768
Uniprot Name
Albumin
Molecular Weight
69365.94 Da
References
  1. Nerli B, Romanini D, Pico G: Structural specificity requirements in the binding of beta lactam antibiotics to human serum albumin. Chem Biol Interact. 1997 May 2;104(2-3):179-202. [Article]
  2. Siddiqi MK, Alam P, Chaturvedi SK, Nusrat S, Ajmal MR, Abdelhameed AS, Khan RH: Probing the interaction of cephalosporin antibiotic-ceftazidime with human serum albumin: A biophysical investigation. Int J Biol Macromol. 2017 Dec;105(Pt 1):292-299. doi: 10.1016/j.ijbiomac.2017.07.036. Epub 2017 Jul 8. [Article]

Transporters

Kind
Protein
Organism
Humans
Pharmacological action
Unknown
Actions
Inhibitor
Curator comments
A study using cloned rat OAT1 transporter expressed in oocytes suggested that ceftazidime could inhibit OAT1, yet prescribing information for avibactam/ceftazidime states that ceftazidime is not a clinically relevant OAT1 inhibitor.
General Function
Secondary active transporter that functions as a Na(+)-independent organic anion (OA)/dicarboxylate antiporter where the uptake of one molecule of OA into the cell is coupled with an efflux of one molecule of intracellular dicarboxylate such as 2-oxoglutarate or glutarate (PubMed:11669456, PubMed:11907186, PubMed:14675047, PubMed:22108572, PubMed:23832370, PubMed:28534121, PubMed:9950961). Mediates the uptake of OA across the basolateral side of proximal tubule epithelial cells, thereby contributing to the renal elimination of endogenous OA from the systemic circulation into the urine (PubMed:9887087). Functions as a biopterin transporters involved in the uptake and the secretion of coenzymes tetrahydrobiopterin (BH4), dihydrobiopterin (BH2) and sepiapterin to urine, thereby determining baseline levels of blood biopterins (PubMed:28534121). Transports prostaglandin E2 (PGE2) and prostaglandin F2-alpha (PGF2-alpha) and may contribute to their renal excretion (PubMed:11907186). Also mediates the uptake of cyclic nucleotides such as cAMP and cGMP (PubMed:26377792). Involved in the transport of neuroactive tryptophan metabolites kynurenate (KYNA) and xanthurenate (XA) and may contribute to their secretion from the brain (PubMed:22108572, PubMed:23832370). May transport glutamate (PubMed:26377792). Also involved in the disposition of uremic toxins and potentially toxic xenobiotics by the renal organic anion secretory pathway, helping reduce their undesired toxicological effects on the body (PubMed:11669456, PubMed:14675047). Uremic toxins include the indoxyl sulfate (IS), hippurate/N-benzoylglycine (HA), indole acetate (IA), 3-carboxy-4- methyl-5-propyl-2-furanpropionate (CMPF) and urate (PubMed:14675047, PubMed:26377792). Xenobiotics include the mycotoxin ochratoxin (OTA) (PubMed:11669456). May also contribute to the transport of organic compounds in testes across the blood-testis-barrier (PubMed:35307651)
Specific Function
alpha-ketoglutarate transmembrane transporter activity
Gene Name
SLC22A6
Uniprot ID
Q4U2R8
Uniprot Name
Solute carrier family 22 member 6
Molecular Weight
61815.78 Da
References
  1. Jariyawat S, Sekine T, Takeda M, Apiwattanakul N, Kanai Y, Sophasan S, Endou H: The interaction and transport of beta-lactam antibiotics with the cloned rat renal organic anion transporter 1. J Pharmacol Exp Ther. 1999 Aug;290(2):672-7. [Article]
  2. FDA Approved Drug Products: AVYCAZ (ceftazidime and avibactam) injection [Link]

Drug created at June 13, 2005 13:24 / Updated at November 09, 2024 06:19