Structure of a phosphonate-inhibited beta-lactamase. An analog of the tetrahedral transition state/intermediate of beta-lactam hydrolysis
about
Three decades of beta-lactamase inhibitorsThe complexed structure and antimicrobial activity of a non-β-lactam inhibitor of AmpC β-lactamaseRe-examining the role of Lys67 in class C β-lactamase catalysisThe deacylation mechanism of AmpC beta-lactamase at ultrahigh resolution.Directed evolution of protein switches and their application to the creation of ligand-binding proteins.The role of a second-shell residue in modifying substrate and inhibitor interactions in the SHV beta-lactamase: a study of ambler position Asn276.Kinship and diversification of bacterial penicillin-binding proteins and beta-lactamases.Exploring sequence requirements for C₃/C₄ carboxylate recognition in the Pseudomonas aeruginosa cephalosporinase: Insights into plasticity of the AmpC β-lactamase.Protonation of the beta-lactam nitrogen is the trigger event in the catalytic action of class A beta-lactamasesExtended-spectrum and inhibitor-resistant TEM-type beta-lactamases: mutations, specificity, and three-dimensional structure.Development of new drugs for an old target: the penicillin binding proteins.Substitution of Asp for Asn at position 132 in the active site of TEM beta-lactamase. Activity toward different substrates and effects of neighboring residues.Structural and mechanistic insights into the inhibition of class C β-lactamases through the adenylylation of the nucleophilic serine.Catalytic properties of class A beta-lactamases: efficiency and diversity.Hydrogen bonding and protein perturbation in beta-lactam acyl-enzymes of Streptococcus pneumoniae penicillin-binding protein PBP2x.Site-saturation mutagenesis of Tyr-105 reveals its importance in substrate stabilization and discrimination in TEM-1 beta-lactamase.Structural and Kinetic Studies of the Potent Inhibition of Metallo-β-lactamases by 6-Phosphonomethylpyridine-2-carboxylates.A new TEM beta-lactamase double mutant with broadened specificity reveals substrate-dependent functional interactions.
P2860
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P2860
Structure of a phosphonate-inhibited beta-lactamase. An analog of the tetrahedral transition state/intermediate of beta-lactam hydrolysis
description
1993 nî lūn-bûn
@nan
1993 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
Structure of a phosphonate-inh ...... iate of beta-lactam hydrolysis
@ast
Structure of a phosphonate-inh ...... iate of beta-lactam hydrolysis
@en
Structure of a phosphonate-inh ...... iate of beta-lactam hydrolysis
@nl
type
label
Structure of a phosphonate-inh ...... iate of beta-lactam hydrolysis
@ast
Structure of a phosphonate-inh ...... iate of beta-lactam hydrolysis
@en
Structure of a phosphonate-inh ...... iate of beta-lactam hydrolysis
@nl
prefLabel
Structure of a phosphonate-inh ...... iate of beta-lactam hydrolysis
@ast
Structure of a phosphonate-inh ...... iate of beta-lactam hydrolysis
@en
Structure of a phosphonate-inh ...... iate of beta-lactam hydrolysis
@nl
P2093
P356
P1476
Structure of a phosphonate-inh ...... iate of beta-lactam hydrolysis
@en
P2093
P304
P356
10.1006/JMBI.1993.1571
P577
1993-11-01T00:00:00Z