Results 11 to 20 of about 9,673 (155)

Dynamically chiral phosphonic acid-type metallo-β-lactamase inhibitors

Communications Chemistry
Antibiotic resistance is a growing global health threat that risks the lives of millions. Among the resistance mechanisms, that mediated by metallo-β-lactamases is of particular concern as these bacterial enzymes dismantle most β-lactam antibiotics ...
Kinga Virág Gulyás, Liping Zhou, Daniel Salamonsen, Andreas Prester, Kim Bartels, Robert Bosman, Paul Haffke, Jintian Li, Viola Tamási, Fritz Deufel, Johannes Thoma, Anna Andersson Rasmussen, Miklós Csala, Hanna-Kirsti Schroder Leiros, Zhijian Xu, Mikael Widersten, Holger Rohde, Eike C. Schulz, Weiliang Zhu, Máté Erdélyi   +19 more
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Novel metallo β-lactamase mediated by aShigella flexneriplasmid [PDF]

FEMS Microbiology Letters, 1998
Novel carbapenem-hydrolyzing beta-lactamase (newly named MET-1) encoded on a transferable plasmid pMS390 from Shigella flexneri JS19622 was purified. The molecular weight was 28,000 by SDS-PAGE and the isoelectric point was higher than 9.3. This beta-lactamase favorably hydrolyzed classical cephalosporins and oxyimino-cephalosporins rather than ...
K, O'Hara, S, Haruta, T, Sawai, M, Tsunoda, S, Iyobe   +4 more
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Multi-Drug-Resistant Gram-Negative Microorganisms: Epidemiology, Treatment and Alternative Approach

Antibiotics, 2022
The presence of enzymes such as Extended-Spectrum β-lactamase (ESBL) and carbapenemases (KPCs, Metallo β-lactamases and OXA) constitutes the principal resistance mechanism to antibiotics [...]
Maria Teresa Mascellino
doaj   +1 more source

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
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Identification and characterization of a novel metallo β-lactamase, SZM-1, in Shenzhen Bay, South China

Frontiers in Microbiology, 2022
Metallo β-Lactamases (MBLs) degrade most clinical β-lactam antibiotics, especially Carbapenem, posing a huge threat to global health. Studies on environmental MBLs are important for risk assessment of the MBLs transmission among connected habitats, and ...
Lingxu Fang, Zongbao Liu, Zhongyi Lu, Zhongyi Lu, Rongzhong Huang, Rong Xiang   +5 more
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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
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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
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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
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Cefiderocol: An Overview of Its in-vitro and in-vivo Activity and Underlying Resistant Mechanisms

Frontiers in Medicine, 2021
Treatment of multidrug-resistant (MDR) Gram-negative bacteria (GNB) infections has led to a global public health challenging due to the bacterial resistance and limited choices of antibiotics.
Jiahui Yao, Jin Wang, Mengli Chen, Yun Cai   +3 more
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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
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