In vitro antibacterial activity of E-0702, a new semisynthetic cephalosporin

  title={In vitro antibacterial activity of E-0702, a new semisynthetic cephalosporin},
  author={Kanemasa Katsu and Kyosuke Kitoh and Matsuhisa Inoue and Susumu Mitsuhashi},
  journal={Antimicrobial Agents and Chemotherapy},
  pages={181 - 185}
E-0702 is an antipseudomonal cephalosporin derivative which has a broad spectrum of antibacterial activity against clinical isolates of gram-positive and gram-negative bacteria. Its in vitro antibacterial activities were less than those of cefoperazone and cefotaxime against Staphylococcus aureus and Staphylococcus epidermidis, but were significantly high against gram-negative bacteria including the Pseudomonas group. It was most characteristic that E-0702 showed high antibacterial activity… 
In vitro antibacterial activity of KP-736, a new cephem antibiotic
KP-736, a new cephen antibiotic with a broad antibacterial spectrum and potent antipseudomonal activity, was evaluated for in vitro antibacterial activity in comparison with ceftazidime, cefotaxime,
Comparative Evaluation of GR 69153, a Catechol-Substituted Cephalosporin
SummaryThe in vitro activity of GR 69153, a new catechol-containing cephalosporin, was compared with other commonly used antibacterial agents against 651 isolates of Enterobacteriaceae, 204 isolates
In vitro evaluation of E1040, a new cephalosporin with potent antipseudomonal activity
E1040 is a new parenteral cephalosporin with a broad antibacterial spectrum and potent antipseudomonal activity and was at least as resistant as ceftazidime and cefmenoxime to hydrolysis by various beta-lactamases and showed high affinities for penicillin-binding protein 3 of both Escherichia coli and P. aeruginosa.
Antimicrobial activity of E-1040, a novel thiadiazolyl cephalosporin compared with other parenteral cephems.
In vitro and in vivo evaluation of Ro 09-1428, a new parenteral cephalosporin with high antipseudomonal activity
The results indicate that Ro 09-1428 is a broad-spectrum cephalosporin with advantages over ceftazidime in its activity against P. aeruginosa, staphylococci, and ceftrazidime-resistant strains of C. freundii and E. cloacae.
E-0702, a new cephalosporin, is incorporated into Escherichia coli cells via the tonB-dependent iron transport system
It is suggested that E-0702 is incorporated into bacterial cells as a chelator of iron via the tonB-dependent iron transport system, after which its strong and rapid bactericidal action is manifested.
Novel cephalosporins having a benzothiopyran group. 2. Synthesis and biological activity of catecholic benzothiopyran group at the C-3 side chain.
These benzothiopyran cephalosporins exhibited broad and good antibacterial activity against both Gram-positive bacteria including Enterococcus faecalis and Gram-negative bacteria including Pseudomonasaeruginosa.
Antibacterial activity of BMS-180680, a new catechol-containing monobactam
BMS-180680 was the only antibiotic evaluated that was active against >90% of the Pseudomonas aeruginosa, Burkholderia cepacia, and Stenotrophomonas maltophilia strains tested.


Purification and properties of a cephalosporinase from Enterobacter cloacae.
The enzyme hydrolyzed cephalosporins much more readily than penicillins, and the enzymological properties of the purified enzyme were compared with those of beta-lactamases derived from other gram-negative enteric bacteria.
Activity of beta-lactamase produced by Bacteroides fragilis against newly introduced cephalosporins
The purified beta-lactamase from Bacteroides fragilis hydrolyzed newly introduced cephalosporins including cefuroxime and HR 756, and was inhibited by 7 alpha-methoxylated cephalosporins such as
Purification and properties of cephalosporinase from Pseudomonas aeruginosa.
Mouse antiserum obtained against the purified enzyme showed no cross-reaction with other types of beta-lactamase in neutralization test, and the enzyme activity was inhibited by iodine, some divalent ions, and some semisynthetic beta- lactam antibiotics, including cephamycin derivatives such as moxalactam and YM09330.
Biochemical Properties of a Penicillin Beta-Lactamase Mediated by R Factor from Bordetella bronchiseptica
The β-lactamase specified by an Rte16 plasmid in Bordetella bronchiseptica was purified 200-fold by carboxymethyl-Sephadex column chromatography and electrofocusing and was highly active against phenethicillin, oxacillin, and propicillin.
Plasmid-Mediated Penicillin Beta-Lactamases in Pseudomonas aeruginosa
It is concluded that this enzyme is a new type of penicillin β-lactamase different from the type I, II, or III R plasmid-mediated PCases reported previously.
Properties of cephalosporinase from Proteus morganii.
The results suggest the possibility that the properties of beta-lactamases may be characterized by measuring the kinetic parameters of the enzyme toward newly-introduced beta-Lactam antibiotics and beta- lactamase inhibitors.
Purification and properties of cephalosporinase in Escherichia coli
The enzyme activity was inhibited by iodine, some divalent metallic ions, semisynthetic penicillins, cefuroxime-type cephalosporins, and cephamycin derivatives.
Purification and Some Properties of a Cephalosporinase from Proteus vulgaris
The purified cephalosporinase from Proteus vulgaris hydrolyzed a variety of cephalosporins, including cefuroxime, at a high level; its activity was inhibited by clavulanic acid.
Purification and biochemical properties of beta-lactamase produced by Proteus rettgeri
beta-Lactamase produced by Proteus rettgeri was found to be a typical cephalosporin beta-lactamase on the basis of its substrate hydrolysis profile. The enzyme activity was enhanced by prior
Purification and Properties of a New β-Lactamase from Pseudomonas cepacia
The f8-lactamase showed a unique substrate profile by hydrolyzing most of the cephalosporins, including cefuroxime, cefotaxime, ampicillin, and penicillin G, at a high rate, and was inhibited by iodine, p-chloromercuribenzoate, clavulanic acid, and cloxacillin.