Results 41 to 50 of about 52,332 (219)

Conformational Changes in the Metallo-β-lactamase ImiS During the Catalytic Reaction: An EPR Spectrokinetic Study of Co(II)-Spin Label Interactions [PDF]

, 2008
Metallo-β-lactamases are responsible for conferring antibiotic resistance on certain pathogenic bacteria. In consequence, the search for inhibitors that may be useful in combating antibiotic resistance has fueled much study of the active sites of these ...
Bennett, Brian, Crowder, Michael W., Hu, Zhenxin, Sharma, Narayan   +3 more
core   +2 more sources

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

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

Nature Communications, 2022
Metallo-β-lactamases cleave β-lactam moiety of many broadly used antibiotics. Here the authors captured mechanistic details of the enzyme catalyzed reaction using time-resolved xray synchrotron serial crystallography.
M. Wilamowski, D. A. Sherrell, Y. Kim, A. Lavens, R. W. Henning, K. Lazarski, A. Shigemoto, M. Endres, N. Maltseva, G. Babnigg, S. C. Burdette, V. Srajer, A. Joachimiak   +12 more
doaj   +1 more source

The reaction mechanism of metallo-beta-lactamases is tuned by the conformation of an active site mobile loop [PDF]

, 2018
Carbapenems are "last resort" β-lactam antibiotics used to treat serious and life-threatening health care-associated infections caused by multidrug-resistant Gram-negative bacteria.
Alzari, Pedro M., Bethel, Christopher R., Bonomo, Robert A., Giannini, Estefanía, Klinke, Sebastian, Llarrull, Leticia Irene, Mojica, María F., Otero, Lisandro Horacio, Palacios, Antonela Rocio, Taracila, Magdalena A., Vila, Alejandro Jose   +10 more
core   +1 more source

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

NDM Metallo-β-Lactamases and Their Bacterial Producers in Health Care Settings

Clinical Microbiology Reviews, 2019
New Delhi metallo-β-lactamase (NDM) is a metallo-β-lactamase able to hydrolyze almost all β-lactams. Twenty-four NDM variants have been identified in >60 species of 11 bacterial families, and several variants have enhanced carbapenemase activity. SUMMARY
Wenjing Wu, Yu Feng, G. Tang, F. Qiao, A. McNally, Z. Zong   +5 more
semanticscholar   +1 more source

Occurrence of a new metallo-β-lactamase IMP-4 carried on a conjugative plasmid inCitrobacter youngaefrom the People's Republic of China [PDF]

FEMS Microbiology Letters, 2001
During the course of an antimicrobial resistance surveillance programme in Guangzhou, the People's Republic of China, single strains of Citrobacter youngae and Pseudomonas aeruginosa were identified which were resistant to imipenem and found to carry the carbapenemase gene bla(IMP).
P M, Hawkey, J, Xiong, H, Ye, H, Li, F H, M'Zali   +4 more
openaire   +2 more sources

Biochemical characterization of the carbapenem-hydrolyzing β-lactamase AsbM1 fromAeromonas sobriaAER 14M: a member of a novel subgroup of metallo-β-lactamases [PDF]

FEMS Microbiology Letters, 1996
AsbM1, a carbapenem-hydrolyzing beta-lactamase produced by Aeromonas sobria AER 14M, was purified chromatographically, with anion exchange chromatography performed in the absence of Zn2+. The molecular mass of AsbM1 was approximately 34,000; the isoelectric point was 9.1.
Y, Yang, K, Bush
openaire   +2 more sources

Metallo-β-Lactamases and Aptamer-Based Inhibition

Pharmaceuticals, 2011
An evolution of antibiotic-resistant bacteria has resulted in the need for new antibiotics. β-Lactam based drugs are the most predominantly prescribed antibiotics to combat bacterial infections; however, production of β-lactamases, which catalyze the ...
Sung-Kun Kim, Taylor O. Foster, Mieke J. Lahousse, Sara R. Schlesinger   +3 more
doaj   +1 more source

Prevalence and detection of Stenotrophomonas maltophilia carrying metallo-β-lactamase blaL1 in Beijing, China [PDF]

Frontiers in Microbiology, 2014
Intrinsic β-lactam resistance in Stenotrophomonas maltophilia is caused by bla L1 and/or bla L2, a kind of metallo-β-lactamase with a broad substrate spectrum including carbapenems. A rapid and sensitive molecular method for the detection of bla L1 in clinical samples is needed to guide therapeutic treatment. In present study, we first described a loop-
Zhan eYang, Wei eLiu, Qian eCui, Qian eCui, Wen Kai Niu, Huan eLi, Xiang Na Zhao, Xiao eWei, Xue Song Wang, Si Mo Huang, De Rong Dong, Si Jing Lu, Chang Qing Bai, Yan eLi, Liu Yu Huang, Jing eYuan   +15 more
openaire   +3 more sources