ArticleAntimicrobial agents and chemotherapy2008
The Lys234Arg substitution in the enzyme SHV-72 is a determinant for resistance to clavulanic acid inhibition.
Article in Antimicrobial agents and chemotherapy, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 1 of them a synthesis that pooled it.
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Who cites it
18 citing papers in PubMed, 1 synthesis or guideline pooled it, 27 citations in OpenAlex.
- Diversity, functional classification and genotyping of SHV β-lactamases inMicrobial genomics · 2024Pooled it
- Two β-Lactamase Variants with Reduced Clavulanic Acid Inhibition Display Different Millisecond Dynamics.Antimicrobial agents and chemotherapy · 2021Article
- A drug-resistant β-lactamase variant changes the conformation of its active-site proton shuttle to alter substrate specificity and inhibitor potency.The Journal of biological chemistry · 2020Article
- Outbreak of KPC-2-producingEuro surveillance : bulletin Europeen sur les maladies transmissibles = European communicable disease bulletin · 2020Article
- Detection in two hospitals of transferable ceftazidime-avibactam resistance inEuro surveillance : bulletin Europeen sur les maladies transmissibles = European communicable disease bulletin · 2020Article
- Combinatorial active-site variants confer sustained clavulanate resistance in BlaC β-lactamase from Mycobacterium tuberculosis.Protein science : a publication of the Protein Society · 2015Article
- Penam sulfones and β-lactamase inhibition: SA2-13 and the importance of the C2 side chain length and composition.PloS one · 2014Article
- Detection of resistance to beta-lactamase inhibitors in strains with CTX-M beta-lactamases: a multicenter external proficiency study using a well-defined collection of Escherichia coli strains.Journal of clinical microbiology · 2014Article
- The evolutionary histories of clinical and environmental SHV β-lactamases are intertwined.Journal of molecular evolution · 2013Article
- Design and exploration of novel boronic acid inhibitors reveals important interactions with a clavulanic acid-resistant sulfhydryl-variable (SHV) β-lactamase.Journal of medicinal chemistry · 2013Article
- Substitutions at position 105 in SHV family β-lactamases decrease catalytic efficiency and cause inhibitor resistance.Antimicrobial agents and chemotherapy · 2012Article
- Characterization of the inhibitor-resistant SHV β-lactamase SHV-107 in a clinical Klebsiella pneumoniae strain coproducing GES-7 enzyme.Antimicrobial agents and chemotherapy · 2012Article
- In vitro selection of variants resistant to beta-lactams plus beta-lactamase inhibitors in CTX-M beta-lactamases: predicting the in vivo scenario?Antimicrobial agents and chemotherapy · 2011Article
- Role of SHV β-lactamase variants in resistance of clinical Klebsiella pneumoniae strains to β-lactams in an Algerian hospital.Journal of medical microbiology · 2011Article
- Enzymatic analysis of the effect of naturally occurring Leu138Pro mutation identified in SHV β-lactamase on hydrolysis of penicillin and ampicillin.BMC microbiology · 2011Article
- Biochemical study of a new inhibitor-resistant beta-lactamase, SHV-84, produced by a clinical Escherichia coli strain.Antimicrobial agents and chemotherapy · 2010Article
- Three decades of beta-lactamase inhibitors.Clinical microbiology reviews · 2010Review
- Biochemical characterization of SHV-55, an extended-spectrum class A beta-lactamase from Klebsiella pneumoniae.Antimicrobial agents and chemotherapy · 2008Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The new beta-lactamase SHV-72 was isolated from clinical Klebsiella pneumoniae INSRA1229, which exhibited the unusual association of resistance to the amoxicillin-clavulanic acid combination (MIC, 64 microg/ml) and susceptibility to cephalosporins, aztreonam, and imipenem. SHV-72 (pI 7.6) harbored the three amino acid substitutions Ile8Phe, Ala146Val, and Lys234Arg. SHV-72 had high catalytic efficiency against penicillins (k(cat)/K(m), 35 to 287 microM(-1) x s(-1)) and no activity against oxyimino beta-lactams. The concentration of clavulanic acid necessary to inhibit the enzyme activity by 50% was 10-fold higher for SHV-72 than for SHV-1. Molecular-dynamics simulation suggested that the Lys234Arg substitution in SHV-72 stabilized an atypical conformation of the Ser130 side chain, which moved the O gamma atom of Ser130 around 3.5 A away from the key O gamma atom of the reactive serine (Ser70). This movement may therefore decrease the susceptibility to clavulanic acid by preventing cross-linking between Ser130 and Ser70.
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