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- W2495804868 abstract "isa potentinhibitor ofa broad range ofbacterial P-lactamases, including theplasmid-mediated TEM, SHV,OXA, andstaphylococcal enzymes,aswell asthechromosomally mediated enzymes ofBacteroides, Enterobacter, Citrobacter, Serratia, Morganella, Escherichia, Klebsiella, andProteus species. Theconcentration ofBRL42715needed toreduce the initial rateofhydrolysis ofmostP-lactamase enzymes by50% was 128to2,ug/ml inthepresenceof1 jigofBRL42715 perml,whereas 5 jigofclavulanic acid permlbrought theMIC5. downto8jig/ml. Among these 412strains were 73Citrobacter andEnterobacter strains, and1,ig ofBRL42715 permlreduced the M1C50 ofamoxicillin from>128to2,ug/mI forthe48cefotaxime-susceptible strains andfrom>128to8,ig/ml forthe25cefotaxime-resistant strains. The,B-lactamase enzymes formalarge anddiverse group (3,19)andarerecognized asamajorcauseofbacterial resistance toP-lactam antibiotics (14). Thisresistance can often beovercome either byusing P-lactam antibiotics that arestable tohydrolysis byP-lactamases orbycombining labile 3-lactams withenzymeinhibitors whichmaynot themselves beuseful antibacterial agents butwhich havethe ability toinactivate P-lactamases. Thefirst ,-lactamase inhibitor tohaveclinical application wasclavulanic acid (8, 16), andformulations ofamoxicillin plus clavulanic acid and ofticarcillin plusclavulanic acid areavailable whichprotect theantibiotics amoxicillin andticarcillin fromhydrolysis by manyP-lactamase-producing organisms. Morerecently described P-lactamase inhibitors include sulbactam (5)and tazobactam (YTR830;1).Clavulanic acidishighly active against a broadrangeofP-lactamases, including theIc enzymesproduced byProteus vulgaris andBacteroides fragilis, butisonlyweaklyactive against other class I enzymes. Sulbactam isgenerally less potent thanclavulanic acid(9), although itdoeshavesomeactivity against most class Ienzymes, while tazobactam issimilar inpotency to clavulanic acidandalsohasmoderate activity against the class Ienzymes. Studies doneinourlaboratories onthestructural modification ofthepenemnucleus culminated inthesynthesis of compounds containing analkylidene moiety attheC6positionofthepenemringsystem (I.S.Bennett, G.Brooks, N.J.P.Broom, K.Coleman, S.Coulton, R.A.Edmundson,D.R.J.Griffin, J.B.Harbridge, N.F.Osborne, I. Stirling-Francois," @default.
- W2495804868 created "2016-08-23" @default.
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- W2495804868 date "1989-01-01" @default.
- W2495804868 modified "2023-09-24" @default.
- W2495804868 title "InVitro Evaluation ofBRL 42715, a Novel3-Lactamase Inhibitor" @default.
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