Compounds > phenylacetyl 7-aminodesacetoxycephalosporanic acid
Page last updated: 2024-11-08

phenylacetyl 7-aminodesacetoxycephalosporanic acid

Description Research Excerpts Clinical Trials Roles Classes Pathways Study Profile Bioassays Related Drugs Related Conditions Protein Interactions Research Growth Market Indicators

Cross-References

ID SourceID
PubMed CID168674
CHEMBL ID115860
SCHEMBL ID8024475
MeSH IDM0091910

Synonyms (18)

Synonym
(6r-trans)-3-methyl-8-oxo-7-(phenylacetamido)-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
CHEMBL115860
(6r,7r)-3-methyl-8-oxo-7-[(2-phenylacetyl)amino]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
A818980
27255-72-7
phenylacetyl 7-aminodesacetoxycephalosporanic acid
(6r-trans)-3-methyl-8-oxo-7-(phenylacetamido)-5-thia-1-azabicyclo(4.2.0)oct-2-ene-2-carboxylic acid
5-thia-1-azabicyclo(4.2.0)oct-2-ene-2-carboxylic acid, 3-methyl-8-oxo-7-((phenylacetyl)amino)-, (6r-trans)-
einecs 248-379-3
AKOS015955755
(6r,7r)-3-methyl-8-oxo-7-(2-phenylacetamido)-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
CIPQGGYPCPIDBB-IUODEOHRSA-N
(6r, 7r)-3-methyl-7-phenylacetamidoceph-3-em-4-carboxylic acid
(6r,7r)-3-methyl-7-phenylacetamidoceph-3-em-4-carboxylic acid
SCHEMBL8024475
W-109199
DTXSID00181707
5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid,3-methyl-8-oxo-7-[(phenylacetyl)amino]-, (6r,7r)-
[information is derived through text-mining from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Bioassays (41)

Assay IDTitleYearJournalArticle
AID1812388Inhibition of Metallo-beta-lactamase NDM-1 in Escherichia coli clinical isolate assessed as fold reduction in meropenem MIC at 64 ug/ml2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID205978In Vitro minimal inhibitory concentration against Staphylococcus aureus (FDA 209P)1998Journal of medicinal chemistry, Nov-19, Volume: 41, Issue:24
Syntheses of new isodethiaazacephems as potent antibacterial agents.
AID1812380Inhibition of Metallo-beta-lactamase IMP-1 in Enterobacter cloacae clinical isolate assessed as fold reduction in meropenem MIC at 128 ug/ml2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID1812349Inhibition of Metallo-beta-lactamase IMP-28 in Klebsiella pneumoniae clinical isolate assessed as MIC for meropenem antibacterial activity at 64 ug/ml (Rvb = 2 ug/ml)2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID1812360Antibacterial activity against beta-lactamase VIM2 producing Escherichia coli clinical isolate measured upto 128 ug/ml2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID1812359Antibacterial activity against beta-lactamase IMP-28 producing Klebsiella pneumoniae clinical isolate measured upto 128 ug/ml2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID1812333Inhibition of Metallo-beta-lactamase IMP-1 in Enterobacter cloacae clinical isolate assessed as MIC for meropenem antibacterial activity at 32 ug/ml (Rvb =16 ug/ml)2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID44090Second order rate constant for metallo-beta-lactamase hydrolysis at pH 7.022004Bioorganic & medicinal chemistry letters, Apr-05, Volume: 14, Issue:7
The inhibition of metallo-beta-lactamase by thioxo-cephalosporin derivatives.
AID1812361Inhibition of Enterobacter cloacae IMP-1 using nitrocefin chromogenic substrate measured after 15 to 60 min at 25 degC by microplate reader2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID1812382Inhibition of Metallo-beta-lactamase IMP-28 in Klebsiella pneumoniae clinical isolate assessed as fold reduction in meropenem MIC at 64 ug/ml2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID1812358Antibacterial activity against beta-lactamase IMP1 producing Enterobacter cloacae clinical isolate measured upto 128 ug/ml2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID1812373Substrate activity at Klebsiella pneumoniae beta-lactamase IMP-28 assessed as compound hydrolysis by measuring Kcat/Km by Michaelis-Menten analysis2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID1812389Inhibition of Metallo-beta-lactamase NDM-1 in Escherichia coli clinical isolate assessed as fold reduction in meropenem MIC at 128 ug/ml2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID1812386Inhibition of Metallo-beta-lactamase VIM-2 in Escherichia coli clinical isolate assessed as fold reduction in meropenem MIC at 128 ug/ml2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID1812342Inhibition of Metallo-beta-lactamase NDM-1 in Escherichia coli clinical isolate assessed as MIC for meropenem antibacterial activity at 32 ug/ml (Rvb = 32 ug/ml)2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID1812379Inhibition of Metallo-beta-lactamase IMP-1 in Enterobacter cloacae clinical isolate assessed as fold reduction in meropenem MIC at 64 ug/ml2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID1812348Inhibition of Metallo-beta-lactamase IMP-28 in Klebsiella pneumoniae clinical isolate assessed as MIC for meropenem antibacterial activity at 32 ug/ml (Rvb = 2 ug/ml)2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID1812364Inhibition of Escherichia coli beta-lactamase VIM-2 using nitrocefin chromogenic substrate measured after 15 to 60 min at 25 degC by microplate reader2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID1812343Inhibition of Metallo-beta-lactamase NDM-1 in Escherichia coli clinical isolate assessed as MIC for meropenem antibacterial activity at 64 ug/ml (Rvb = 32 ug/ml)2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID200682In Vitro minimal inhibitory concentration against Salmonella typhi (O-901)1998Journal of medicinal chemistry, Nov-19, Volume: 41, Issue:24
Syntheses of new isodethiaazacephems as potent antibacterial agents.
AID1812381Inhibition of Metallo-beta-lactamase IMP-28 in Klebsiella pneumoniae clinical isolate assessed as fold reduction in meropenem MIC at 32 ug/ml2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID1812370Substrate activity at Klebsiella pneumoniae beta-lactamase IMP-28 assessed as compound hydrolysis by measuring Kcat by Michaelis-Menten analysis2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID164883In Vitro minimal inhibitory concentration against Pseudomonas aeruginosa (1101-75)1998Journal of medicinal chemistry, Nov-19, Volume: 41, Issue:24
Syntheses of new isodethiaazacephems as potent antibacterial agents.
AID1812362Inhibition of Klebsiella pneumoniae beta-lactamase IMP-28 using nitrocefin chromogenic substrate measured after 15 to 60 min at 25 degC by microplate reader2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID1812353Inhibition of Metallo-beta-lactamase VIM-2 in Escherichia coli clinical isolate assessed as MIC for meropenem antibacterial activity at 128 ug/ml (Rvb = 4 ug/ml)2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID1812363Inhibition of Escherichia coli beta-lactamase NDM-1 using nitrocefin chromogenic substrate measured after 15 to 60 min at 25 degC by microplate reader2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID1812344Inhibition of Metallo-beta-lactamase NDM-1 in Escherichia coli clinical isolate assessed as MIC for meropenem antibacterial activity at 128 ug/ml (Rvb = 32 ug/ml)2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID96241In Vitro minimal inhibitory concentration against Klebsiella pneumoniae (NCTC 418)1998Journal of medicinal chemistry, Nov-19, Volume: 41, Issue:24
Syntheses of new isodethiaazacephems as potent antibacterial agents.
AID1812378Inhibition of Metallo-beta-lactamase IMP-1 in Enterobacter cloacae clinical isolate assessed as fold reduction in meropenem MIC at 32 ug/ml2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID1812351Inhibition of Metallo-beta-lactamase VIM-2 in Escherichia coli clinical isolate assessed as MIC for meropenem antibacterial activity at 32 ug/ml (Rvb = 4 ug/ml)2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID70750In Vitro minimal inhibitory concentration against Escherichia coli (ATCC 39188)1998Journal of medicinal chemistry, Nov-19, Volume: 41, Issue:24
Syntheses of new isodethiaazacephems as potent antibacterial agents.
AID1812384Inhibition of Metallo-beta-lactamase VIM-2 in Escherichia coli clinical isolate assessed as fold reduction in meropenem MIC at 32 ug/ml2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID1812352Inhibition of Metallo-beta-lactamase VIM-2 in Escherichia coli clinical isolate assessed as MIC for meropenem antibacterial activity at 64 ug/ml (Rvb = 4 ug/ml)2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID1812334Inhibition of Metallo-beta-lactamase IMP-1 in Enterobacter cloacae clinical isolate assessed as MIC for meropenem antibacterial activity at 64 ug/ml (Rvb =16 ug/ml)2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID1812335Inhibition of Metallo-beta-lactamase IMP-1 in Enterobacter cloacae clinical isolate assessed as MIC for meropenem antibacterial activity at 128 ug/ml (Rvb =16 ug/ml)2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID1812383Inhibition of Metallo-beta-lactamase IMP-28 in Klebsiella pneumoniae clinical isolate assessed as fold reduction in meropenem MIC at 128 ug/ml2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID1812385Inhibition of Metallo-beta-lactamase VIM-2 in Escherichia coli clinical isolate assessed as fold reduction in meropenem MIC at 64 ug/ml2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID1812390Antibacterial activity against beta-lactamase NDM1 producing Escherichia coli clinical isolate measured upto 128 ug/ml2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID1812350Inhibition of Metallo-beta-lactamase IMP-28 in Klebsiella pneumoniae clinical isolate assessed as MIC for meropenem antibacterial activity at 128 ug/ml (Rvb = 2 ug/ml)2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID1812367Substrate activity at Klebsiella pneumoniae beta-lactamase IMP-28 assessed as compound hydrolysis by measuring Km by Michaelis-Menten analysis2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
AID1812387Inhibition of Metallo-beta-lactamase NDM-1 in Escherichia coli clinical isolate assessed as fold reduction in meropenem MIC at 32 ug/ml2021Journal of medicinal chemistry, 07-08, Volume: 64, Issue:13
Novel Cephalosporin Conjugates Display Potent and Selective Inhibition of Imipenemase-Type Metallo-β-Lactamases.
[information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023]

Research

Studies (5)

TimeframeStudies, This Drug (%)All Drugs %
pre-19902 (40.00)18.7374
1990's1 (20.00)18.2507
2000's1 (20.00)29.6817
2010's0 (0.00)24.3611
2020's1 (20.00)2.80
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Market Indicators

Research Demand Index: 12.46

According to the monthly volume, diversity, and competition of internet searches for this compound, as well the volume and growth of publications, there is estimated to be weak demand-to-supply ratio for research on this compound.

MetricThis Compound (vs All)
Research Demand Index12.46 (24.57)
Research Supply Index1.79 (2.92)
Research Growth Index4.25 (4.65)
Search Engine Demand Index0.00 (26.88)
Search Engine Supply Index0.00 (0.95)

This Compound (12.46)

All Compounds (24.57)

Study Types

Publication TypeThis drug (%)All Drugs (%)
Trials0 (0.00%)5.53%
Reviews0 (0.00%)6.00%
Case Studies0 (0.00%)4.05%
Observational0 (0.00%)0.25%
Other5 (100.00%)84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]
SubstanceRelationship StrengthStudiesTrialsClassesRoles
penicillin g
Penicillin G: 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.. benzylpenicillin : A penicillin in which the substituent at position 6 of the penam ring is a phenylacetamido group.		2.3920penicillin allergen;
penicillin		antibacterial drug;
drug allergen;
epitope
ampicillin
Ampicillin: Semi-synthetic derivative of penicillin that functions as an orally active broad-spectrum antibiotic.. ampicillin : A penicillin in which the substituent at position 6 of the penam ring is a 2-amino-2-phenylacetamido group.		1.9710beta-lactam antibiotic;
penicillin allergen;
penicillin		antibacterial drug
dipicolinic acid
dipicolinic acid : A pyridinedicarboxylic acid carrying two carboxy groups at positions 2 and 6.		2.3110pyridinedicarboxylic acidbacterial metabolite
cephalexin
Cephalexin: A semisynthetic cephalosporin antibiotic with antimicrobial activity similar to that of CEPHALORIDINE or CEPHALOTHIN, but somewhat less potent. It is effective against both gram-positive and gram-negative organisms.. cephalexin : A semisynthetic first-generation cephalosporin antibiotic having methyl and beta-(2R)-2-amino-2-phenylacetamido groups at the 3- and 7- of the cephem skeleton, respectively. It is effective against both Gram-negative and Gram-positive organisms, and is used for treatment of infections of the skin, respiratory tract and urinary tract.		1.9710beta-lactam antibiotic allergen;
cephalosporin;
semisynthetic derivative		antibacterial drug
cephalosporin c
cephalosporin C: RN given refers to parent cpd; structure in Merck, 9th ed, #1937. cephalosporin C : A cephalosporin antibiotic carrying a 3-acetoxymethyl substituent and a 6-oxo-N(6)-L-lysino group at position 7.		2.3720cephalosporinfungal metabolite
cefaloram
cefaloram: RN given refers to parent cpd; structure given in first source. cefaloram : A cephalosporin derivative with potent antibacterial activity which binds to and inactivates penicillin-binding proteins (PBPs) located on the inner membrane of the bacterial cell wall. PBPs are enzymes involved in the terminal stages of assembling the bacterial cell wall and in reshaping the cell wall during growth and division, inactivation of which interferes with the cross-linkage of peptidoglycan chains necessary for bacterial cell wall strength and rigidity, resulting in the weakening of the bacterial cell wall and causing cell lysis.		2.4320cephalosporinantibacterial drug
cefotaxime
Cefotaxime: Semisynthetic broad-spectrum cephalosporin.. cefotaxime : A cephalosporin compound having acetoxymethyl and [2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino side groups.		2.39201,3-thiazoles;
cephalosporin;
oxime O-ether		antibacterial drug;
drug allergen
ConditionIndicatedRelationship StrengthStudiesTrials