Results 21 to 30 of about 58,396 (229)

The flavonoid galangin inhibits the L1 metallo-β-lactamase fromStenotrophomonas maltophilia [PDF]

FEMS Microbiology Letters, 2002
The flavonoid galangin inhibits the partially purified metallo-beta-lactamase from Stenotrophomonas maltophilia. The effect was not reversed by the addition of ZnCl(2) suggesting that the inhibitory effect is not related to metal chelation. The flavonoid quercetin also has some inhibitory effect against the enzyme.
Brian J, Denny, Peter A, Lambert, Patrick W J, West   +2 more
openaire   +2 more sources

Computationally designed peptide macrocycle inhibitors of New Delhi metallo-β-lactamase 1

Proceedings of the National Academy of Sciences of the United States of America, 2021
Significance Peptide macrocycles are a promising class of drugs, but their weakness is conformational flexibility: target affinity can be limited by an unfavorable transition from a disordered unbound state to an ordered bound state. We introduce general
V. Mulligan, S. Workman, T. Sun, Stephen A. Rettie, Xinting Li, L. Worrall, Timothy W. Craven, D. King, P. Hosseinzadeh, A. Watkins, P. Renfrew, Sharon L. Guffy, Jason W. Labonte, Rocco Moretti, Richard Bonneau, N. Strynadka, D. Baker   +16 more
semanticscholar   +1 more source

Time-resolved β-lactam cleavage by L1 metallo-β-lactamase

Nature Communications, 2022
Serial x-ray crystallography can uncover binding events, and subsequent chemical conversions occurring during enzymatic reaction. Here, we reveal the structure, binding and cleavage of moxalactam antibiotic bound to L1 metallo-β-lactamase (MBL) from ...
M. Wilamowski, D. Sherrell, Y. Kim, A. Lavens, R. Henning, K. Lazarski, A. Shigemoto, M. Endres, N. Maltseva, G. Babnigg, S. Burdette, V. Šrajer, A. Joachimiak   +12 more
semanticscholar   +1 more source

Isolation and partial purification of a carbapenem-hydrolysing metallo-β-lactamase fromPseudomonas cepacia [PDF]

FEMS Microbiology Letters, 1994
A metallo-beta-lactamase has been isolated from a clinical strain of Pseudomonas cepacia and partially purified using Cibacron blue F3GA coupled agarose. The resulting preparation showed a single band of beta-lactamase activity (pI 8.45) after analytical isoelectric focusing.
I A, Baxter, P A, Lambert
openaire   +2 more sources

A rapid method for detecting and distinguishing metallo-β-lactamase-and serine carbapenemase-producing Enterobacteriales using MALDI-TOF MS

Frontiers in Microbiology, 2023
IntroductionCarbapenemase-producing Enterobacteriales (CPE) are a major health threat worldwide, and therefore the development of rapid detection methods is needed.
Xiaopeng Jing, Yanyan Hu, Tingting Wu, Xing Zhang, Shaofeng Luo, Wei Wang, Xiaochun Min, Ruiling Sun, Ji Zeng   +8 more
doaj   +1 more source

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

FEMS Microbiology Letters, 1999
IMP-1 metallo-beta-lactamase is a transferable carbapenem-hydrolyzing enzyme found in some clinical isolates of Pseudomonas aeruginosa, Serratia marcescens and Klebsiella pneumoniae. Bacteria that express IMP-1 show significantly reduced sensitivity to carbapenems and other beta-lactam antibiotics.
G G, Hammond, J L, Huber, M L, Greenlee, J B, Laub, K, Young, L L, Silver, J M, Balkovec, K D, Pryor, J K, Wu, B, Leiting, D L, Pompliano, J H, Toney   +11 more
openaire   +2 more sources

Occurrences of Metalo-β-lactamase Producing Pseudomonas aeruginosa among Clinical Samples in Kwara state, Nigeria

Journal of Applied Sciences and Environmental Management, 2022
Pseudomonas aeruginosa is a frequent nosocomial pathogen that causes severe disease in many clinical and community settings. The objective of this paper was to isolate Pseudomonas aeruginosa from clinical samples and to investigate the occurrence of ...
O.C. Adekunle, A. Mustapha, G. Odewale , R.O. Ojedele   +3 more
doaj   +1 more source

Characterization of the active-site residues asparagine 167 and lysine 161 of the IMP-1 metallo β-lactamase [PDF]

FEMS Microbiology Letters, 2001
The roles of lysine at position 161 and asparagine at position 167 in IMP-1 metallo beta-lactamase were studied by site-directed mutagenesis. These residues are highly conserved in metallo beta-lactamases and are thought to be present in the active-site cavity.
S, Haruta, E T, Yamamoto, Y, Eriguchi, T, Sawai   +3 more
openaire   +2 more sources

Motion of the Zinc Ions in Catalysis by a Dizinc Metallo-β-Lactamase [PDF]

, 2009
We report rapid-freeze-quench X-ray absorption spectroscopy of a dizinc metallo-β-lactamase (MβL) reaction intermediate. The Zn(II) ions in the dinuclear active site of the S.
Bennett, Brian, Breece, Robert M., Crowder, Michael W., Hu, Zhenxin, Tierney, David L.   +4 more
core   +2 more sources

Novel IMP-1 metallo-β-lactamase inhibitors can reverse meropenem resistance inEscherichia coliexpressing IMP-1 [PDF]

FEMS Microbiology Letters, 2005
IMP-1 metallo-beta-lactamase is a zinc metalloenzyme that confers antibiotic resistance to bacteria through the hydrolysis of beta-lactam antibiotics. Pathogens that express the enzyme show reduced susceptibility to carbapenems, such as meropenem and imipenem.
Joseph G, Moloughney, Janice, D Thomas, Jeffrey H, Toney   +2 more
openaire   +2 more sources