Ontology highlight
ABSTRACT:
SUBMITTER: Desjardins M
PROVIDER: S-EPMC6641618 | biostudies-literature | 2017 Jul
REPOSITORIES: biostudies-literature
Desjardins Morgan M Mak Wai Shun WS O'Brien Terrence E TE Carlin Dylan Alexander DA Tantillo Dean J DJ Siegel Justin B JB
ACS omega 20170707 7
Enzymes have been through millions of years of evolution during which their active-site microenvironments are fine-tuned. Active-site residues are commonly conserved within protein families, indicating their importance for substrate recognition and catalysis. In this work, we systematically mutated active-site residues of l-threonine dehydrogenase from <i>Thermoplasma volcanium</i> and characterized the mutants against a panel of substrate analogs. Our results demonstrate that only a subset of t ...[more]