[HTML][HTML] Succinic acids as potent inhibitors of plasmid-borne IMP-1 metallo-β-lactamase

JH Toney, GG Hammond, PMD Fitzgerald… - Journal of Biological …, 2001 - ASBMB
IMP-1 metallo-β-lactamase (class B) is a plasmid-borne zinc metalloenzyme that efficiently
hydrolyzes β-lactam antibiotics, including carbapenems, rendering them ineffective …

Analysis of the context dependent sequence requirements of active site residues in the metallo-β-lactamase IMP-1

IC Materon, Z Beharry, W Huang, C Perez… - Journal of molecular …, 2004 - Elsevier
The metallo-β-lactamase IMP-1 catalyzes the hydrolysis of a broad range of β-lactam
antibiotics to provide bacterial resistance to these compounds. In this study, 29 amino acid …

N-Arylsulfonyl Hydrazones as Inhibitors of IMP-1 Metallo-β-Lactamase

S Siemann, DP Evanoff, L Marrone… - Antimicrobial agents …, 2002 - Am Soc Microbiol
Members of a family of N-arylsulfonyl hydrazones have been identified as novel inhibitors of
IMP-1, a metallo-β-lactamase of increasing prevalence. Structure-activity relationship …

Structural and kinetic studies on metallo-β-lactamase IMP-1

DH Griffin, TK Richmond, C Sanchez, AJ Moller… - Biochemistry, 2011 - ACS Publications
In an effort to probe for metal binding to metallo-β-lactamase (MβL) IMP-1, the enzyme was
overexpressed, purified, and characterized. The resulting enzyme was shown to bind 2 …

Inhibition of IMP-1 metallo-β-lactamase and sensitization of IMP-1-producing bacteria by thioester derivatives

GG Hammond, JL Huber, ML Greenlee… - FEMS microbiology …, 1999 - academic.oup.com
Abstract IMP-1 metallo-β-lactamase is a transferable carbapenem-hydrolyzing enzyme
found in some clinical isolates of Pseudomonas aeruginosa, Serratia marcescens and …

[HTML][HTML] Probing the role of Asp-120 (81) of metallo-β-lactamase (IMP-1) by site-directed mutagenesis, kinetic studies, and X-ray crystallography

Y Yamaguchi, T Kuroki, H Yasuzawa, T Higashi… - Journal of Biological …, 2005 - ASBMB
Metallo-β-lactamase IMP-1 is a di-Zn (II) metalloenzyme that efficiently hydrolyzes β-lactam
antibiotics. Wild-type (WT) IMP-1 has a conserved Asp-120 (81) in the active site, which …

Synthesis and SAR of thioester and thiol inhibitors of IMP-1 metallo-β-lactamase

ML Greenlee, JB Laub, JM Balkovec… - Bioorganic & medicinal …, 1999 - Elsevier
SYNTHESIS AND SAR OF THIOESTER AND THIOL INHIBITORS OF IMP-1 METALLO-~-LACTAMASE
Page 1 BIOORGANIC & MEDICINAL CHEMISTRY LETTERS Pergamon Bioorganic & Medicinal …

Crystal Structure of the IMP-1 Metallo β-Lactamase from Pseudomonas aeruginosa and Its Complex with a Mercaptocarboxylate Inhibitor:  Binding Determinants of a Potent …

NO Concha, CA Janson, P Rowling, S Pearson… - Biochemistry, 2000 - ACS Publications
Metallo β-lactamase enzymes confer antibiotic resistance to bacteria by catalyzing the
hydrolysis of β-lactam antibiotics. This relatively new form of resistance is spreading …

Identification of residues critical for metallo‐β‐lactamase function by codon randomization and selection

IC Materon, T Palzkill - Protein Science, 2001 - Wiley Online Library
IMP‐1 β‐lactamase is a zinc metallo‐enzyme encoded by the transferable blaIMP‐1 gene,
which confers resistance to virtually all β‐lactam antibiotics including carbapenems. To …

Amino acid substitutions in a variant of IMP-1 metallo-β-lactamase

S Iyobe, H Kusadokoro, J Ozaki… - Antimicrobial Agents …, 2000 - Am Soc Microbiol
In the course of surveying for the carbapenem-hydrolyzing metallo-β-lactamase gene bla
IMP in pathogenic bacteria by the PCR method, we detected a gene encoding a variant …