High resolution crystal structures of the trans-enamine intermediates formed by sulbactam and clavulanic acid and E166A SHV-1 {beta}-lactamase.
about
Three decades of beta-lactamase inhibitorsSulbactam forms only minimal amounts of irreversible acrylate-enzyme with SHV-1 beta-lactamaseCrystal Structure of a Preacylation Complex of the β-Lactamase Inhibitor Sulbactam Bound to a Sulfenamide Bond-Containing Thiol-β-lactamasePenam Sulfones and β-Lactamase Inhibition: SA2-13 and the Importance of the C2 Side Chain Length and CompositionCrystal Structure of the Extended-Spectrum -Lactamase PER-2 and Insights into the Role of Specific Residues in the Interaction with -Lactams and -Lactamase InhibitorsInvestigations on recyclisation and hydrolysis in avibactam mediated serine β-lactamase inhibitionKinetic crystallography by Raman microscopy.Effect of the inhibitor-resistant M69V substitution on the structures and populations of trans-enamine beta-lactamase intermediates.Why the extended-spectrum beta-lactamases SHV-2 and SHV-5 are "hypersusceptible" to mechanism-based inhibitorsDetecting a quasi-stable imine species on the reaction pathway of SHV-1 β-lactamase and 6β-(hydroxymethyl)penicillanic acid sulfoneDifferent intermediate populations formed by tazobactam, sulbactam, and clavulanate reacting with SHV-1 beta-lactamases: Raman crystallographic evidenceThe enzymes of β-lactam biosynthesis.Synergy within structural biology of single crystal optical spectroscopy and X-ray crystallography.Avibactam and inhibitor-resistant SHV β-lactamasesInhibition of Klebsiella β-Lactamases (SHV-1 and KPC-2) by Avibactam: A Structural Study.The antibiotic CJ-15,801 is an antimetabolite that hijacks and then inhibits CoA biosynthesis.Mutation of the active site carboxy-lysine (K70) of OXA-1 beta-lactamase results in a deacylation-deficient enzyme.The road to avibactam: the first clinically useful non-β-lactam working somewhat like a β-lactam.Raman spectra of interchanging β-lactamase inhibitor intermediates on the millisecond time scale.Rational design of a beta-lactamase inhibitor achieved via stabilization of the trans-enamine intermediate: 1.28 A crystal structure of wt SHV-1 complex with a penam sulfoneIrreversible inhibition of the Mycobacterium tuberculosis beta-lactamase by clavulanate.Following drug uptake and reactions inside Escherichia coli cells by Raman microspectroscopy.Exploring Additional Dimensions of Complexity in Inhibitor Design for Serine β-Lactamases: Mechanistic and Intra- and Inter-molecular Chemistry Approaches.
P2860
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P2860
High resolution crystal structures of the trans-enamine intermediates formed by sulbactam and clavulanic acid and E166A SHV-1 {beta}-lactamase.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh-hant
name
High resolution crystal struct ...... E166A SHV-1 {beta}-lactamase.
@en
High resolution crystal struct ...... E166A SHV-1 {beta}-lactamase.
@nl
type
label
High resolution crystal struct ...... E166A SHV-1 {beta}-lactamase.
@en
High resolution crystal struct ...... E166A SHV-1 {beta}-lactamase.
@nl
prefLabel
High resolution crystal struct ...... E166A SHV-1 {beta}-lactamase.
@en
High resolution crystal struct ...... E166A SHV-1 {beta}-lactamase.
@nl
P2093
P2860
P356
P1476
High resolution crystal struct ...... E166A SHV-1 {beta}-lactamase.
@en
P2093
Focco van den Akker
Marianne P Carey
Marion S Helfand
Monica A Totir
Paul R Carey
Pius S Padayatti
P2860
P304
34900-34907
P356
10.1074/JBC.M505333200
P407
P577
2005-07-29T00:00:00Z