Ontology highlight
ABSTRACT:
SUBMITTER: De Wals PY
PROVIDER: S-EPMC2708040 | biostudies-literature | 2009 Jan
REPOSITORIES: biostudies-literature
Protein science : a publication of the Protein Society 20090101 1
The diversity in substrate recognition spectra exhibited by various beta-lactamases can result from one or a few mutations in the active-site area. Using Escherichia coli TEM-1 beta-lactamase as a template that efficiently hydrolyses penicillins, we performed site-saturation mutagenesis simultaneously on two opposite faces of the active-site cavity. Residues 104 and 105 as well as 238, 240, and 244 were targeted to verify their combinatorial effects on substrate specificity and enzyme activity a ...[more]