6-beta-bromopenicillanic acid, a potent beta-lactamase inhibitor.
about
Beta-lactamase inhibitors from laboratory to clinicStructural Basis of the Inhibition of Class A β-Lactamases and Penicillin-Binding Proteins by 6-β-IodopenicillanateInactivation of the thiol RTEM-1 beta-lactamase by 6-beta-bromopenicillanic acid. Identity of the primary active-site nucleophile6-beta-Iodopenicillanate as a probe for the classification of beta-lactamasesInteraction of beta-iodopenicillanate with the beta-lactamases of Streptomyces albus G and Actinomadura R39Substrate selectivity and a novel role in inhibitor discrimination by residue 237 in the KPC-2 beta-lactamase.Chemistry of newer antibiotics directed toward overcoming bacterial resistanceBeta-lactamase inhibitors: evolving compounds for evolving resistance targets.beta-Lactamase-catalyzed hydrolysis of acyclic depsipeptides and acyl transfer to specific amino acid acceptorsOligonucleotide-directed mutagenesis as a general and powerful method for studies of protein function.Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases.Structure-activity relationships amongst beta-lactamase inhibitors.Covalent binding of moxalactam to cephalosporinase of Citrobacter freundii.Penicillinase active sites: labelling of serine-44 in beta-lactamase I by 6beta-bromopenicillanic acid.Antibiotic resistance in pathogenic and producing bacteria, with special reference to beta-lactam antibiotics.Kinetics of inactivation of beta-lactamase I by 6 beta-bromopenicillanic acid.Evidence from a mutant beta-lactamase for the mechanism of beta-lactamase-catalysed depsipeptide aminolysis.Kinetic studies on inactivation of Citrobacter freundii cephalosporinase by sulbactam.Unexpected influence of ionic strength on branched-pathway interactions between beta-lactamases and beta-halogenopenicillanates.A retrospective view of beta-lactamases.beta-Lactamase inhibitory activity of iodopenicillanate and bromopenicillanate.
P2860
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P2860
6-beta-bromopenicillanic acid, a potent beta-lactamase inhibitor.
description
1978 nî lūn-bûn
@nan
1978年の論文
@ja
1978年論文
@yue
1978年論文
@zh-hant
1978年論文
@zh-hk
1978年論文
@zh-mo
1978年論文
@zh-tw
1978年论文
@wuu
1978年论文
@zh
1978年论文
@zh-cn
name
6-beta-bromopenicillanic acid, a potent beta-lactamase inhibitor.
@ast
6-beta-bromopenicillanic acid, a potent beta-lactamase inhibitor.
@en
type
label
6-beta-bromopenicillanic acid, a potent beta-lactamase inhibitor.
@ast
6-beta-bromopenicillanic acid, a potent beta-lactamase inhibitor.
@en
prefLabel
6-beta-bromopenicillanic acid, a potent beta-lactamase inhibitor.
@ast
6-beta-bromopenicillanic acid, a potent beta-lactamase inhibitor.
@en
P2860
P356
P1476
6-beta-bromopenicillanic acid, a potent beta-lactamase inhibitor.
@en
P2093
Loosemore MJ
P2860
P304
P356
10.1073/PNAS.75.9.4145
P407
P577
1978-09-01T00:00:00Z