Substrate-activated Zinc Binding of Metallo-β-lactamases
نویسندگان
چکیده
منابع مشابه
Metallo-β-Lactamases and Aptamer-Based Inhibition
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 hydrolysis of the β-lactam bond of this class of antibiotics, by pathogenic bacteria such as Bacillus cereus, are rendering them useless. Some inh...
متن کاملA variety of roles for versatile zinc in metallo-β-lactamases.
Metallo-β-lactamases are important as a major source of resistance of pathogenic bacteria to the widely used β-lactam antibiotics. They show considerable diversity in terms of sequence and are grouped into three subclasses, B1, B2 and B3, which share a common overall fold. In each case the active enzyme has binding sites for two zinc ions in close proximity, although the amino-acid residues whi...
متن کاملThe Mechanisms of Catalysis by Metallo β-Lactamases
Class B beta-lactamases or metallo-beta-lactamases (MBLs) require zinc ions to catalyse the hydrolysis of beta-lactam antibiotics such as penicillins, cephalosporins, carbapenems, and cephamycins. There are no clinically useful inhibitors against MBLs which are responsible for the resistance of some bacteria to antibiotics. There are two metal-ion binding sites that have different zinc ligands ...
متن کاملInteraction of Avibactam with Class B Metallo-β-Lactamases
β-Lactamases are the most important mechanisms of resistance to the β-lactam antibacterials. There are two mechanistic classes of β-lactamases: the serine β-lactamases (SBLs) and the zinc-dependent metallo-β-lactamases (MBLs). Avibactam, the first clinically useful non-β-lactam β-lactamase inhibitor, is a broad-spectrum SBL inhibitor, which is used in combination with a cephalosporin antibiotic...
متن کاملEmergence of metallo-β-lactamases in Enterobacteriaceae from Argentina.
Carbapenem susceptibility in Enterobacteriaceae (M9921, M9959) revealed the presence of MBLs bla(VIM-2) (M9959) and bla(IMP-8) (M9921), both as first cassettes of class-1-integrons. ESBL bla(PER-2) was detected in both strains and M9921 also harboured qnrB10, aac(6')-Ib and aac(6')-Ib-cr. This is the first report of MBLs in Enterobacteriaceae from Argentina.
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2002
ISSN: 0021-9258
DOI: 10.1074/jbc.m202467200