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- W1965743559 abstract "The mechanism of hydrolysis of cefepime, a novel cephalosporin, by the class A TEMpUC19 β-lactamase has been investigated. Models for the active-site binding of this antibiotic indicate severe steric interactions between the active site of the enzyme and the C7β function of cefepime. Specific interactions with the side-chain functions of Pro-167 and Asn-170, amino acids present in the Ω-loop spanning residues 164−179, have been singled out as important in the interactions with the antibiotic. These interactions displace the hydrolytic water (Wat-712) from its preferred position for the deacylation step. These observations are consistent with experimental evidence that deacylation is the rate-limiting step in the turnover of cefepime by this β-lactamase. Furthermore, it has been shown in circular-dichroic measurements that hydrolysis of cefepime by this β-lactamase is accompanied by an unprecedented relaxation of the structure of the enzyme in order to accommodate the bulky C7β side chain of the antibiotic..." @default.
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- W1965743559 title "Evidence for Structural Elasticity of Class A β-Lactamases in the Course of Catalytic Turnover of the Novel Cephalosporin Cefepime" @default.
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- W1965743559 doi "https://doi.org/10.1021/ja9529753" @default.
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