32746-94-4Relevant academic research and scientific papers
Removal of the side chain at the active-site serine by a glycine substitution increases the stability of a wide range of serine β-lactamases by relieving steric strain
Stojanoski, Vlatko,Adamski, Carolyn J.,Hu, Liya,Mehta, Shrenik C.,Sankaran, Banumathi,Zwart, Peter,Prasad, B.V. Venkataram,Palzkill, Timothy
, p. 2479 - 2490 (2016)
Serine β-lactamases are bacterial enzymes that hydrolyze β- lactam antibiotics. They utilize an active-site serine residue as a nucleophile, forming an acyl-enzyme intermediate during hydrolysis. In this study, thermal denaturation experiments as well as
Catalytic single-chain antibodies possessing β-lactamase activity selected from a phage displayed combinatorial library using a mechanism-based inhibitor
Tanaka, Fujie,Almer, Helena,Lerner, Richard A.,Barbas III, Carlos F.
, p. 8063 - 8066 (1999)
Catalytic single-chain antibodies (scFvs) possessing β-lactamase activity were selected from a phage displayed combinatorial antibody library using a penam sulfone mechanism-based inhibitor of β-lactamase. The scFvs FT6 and FT12 catalyzed the hydrolysis o
A Novel metallo-β-lactamase involved in the ampicillin resistance of Streptococcus pneumoniae ATCC 49136 strain
Chang, Chia-Yu,Lin, Hui-Jen,Li, Bor-Ran,Li, Yaw-Kuen
, (2016)
Streptococcus pneumoniae, a penicillin-sensitive bacterium, is recognized as a major cause of pneumonia and is treated clinically with penicillin-based antibiotics. The rapid increase in resistance to penicillin and other antibiotics affects 450 million p
Monitoring bacterial resistance to chloramphenicol and other antibiotics by liquid chromatography electrospray ionization tandem mass spectrometry using selected reaction monitoring
Haag, Anthony M.,Medina, Audrie M.,Royall, Ariel E.,Herzog, Norbert K.,Niesel, David W.
, p. 732 - 739 (2013/07/27)
Antibiotic resistance is a growing problem worldwide. For this reason, clinical laboratories often determine the susceptibility of the bacterial isolate to a number of different antibiotics in order to establish the most effective antibiotic for treatment. Unfortunately, current susceptibility assays are time consuming. Antibiotic resistance often involves the chemical modification of an antibiotic to an inactive form by an enzyme expressed by the bacterium. Selected reaction monitoring (SRM) has the ability to quickly monitor and identify these chemical changes in an unprecedented time scale. In this work, we used SRM as a technique to determine the susceptibility of several different antibiotics to the chemically modifying enzymes β-lactamase and chloramphenicol acetyltransferase, enzymes used by bacteria to confer resistance to major classes of commonly used antibiotics. We also used this technique to directly monitor the effects of resistant bacteria grown in a broth containing a specific antibiotic. Because SRM is highly selective and can also identify chemical changes in a multitude of antibiotics in a single assay, SRM has the ability to detect organisms that are resistant to multiple antibiotics in a single assay. For these reasons, the use of SRM greatly reduces the time it takes to determine the susceptibility or resistance of an organism to a multitude of antibiotics by eliminating the time-consuming process found in other currently used methods. Copyright 2013 John Wiley & Sons, Ltd. Copyright
