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Article

A triple mutant in the Ω-loop of TEM-1 β-lactamase changes the substrate profile via a large conformational change and an altered general base for catalysis.

The Journal of biological chemistry - 17 Apr 2015

Stojanoski Vlatko, Chow Dar-Chone, Hu Liya, Sankaran Banumathi, Gilbert Hiram F, Prasad B V Venkataram, Palzkill Timothy

Abstract excerpt

β-Lactamases are bacterial enzymes that hydrolyze β-lactam antibiotics. TEM-1 is a prevalent plasmid-encoded β-lactamase in Gram-negative bacteria that efficiently catalyzes the hydrolysis of penicillins and early cephalosporins but not oxyimino-cephalosporins. A previous random mutagenesis study identified a W165Y/E166Y/P167G triple mutant that displays greatly altered substrate specificity with increased...

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Identifiers

PMID: 25713062
DOI: 10.1074/jbc.M114.633438
PMCID: PMC4400348

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A triple mutant in the Ω-loop of TEM-1 β-lactamase changes the substrate profile via a large conformational change and an altered general base for catalysis.PMID 25713062Read ↗

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