Non-allosteric enzyme switches possess larger effector-induced changes in thermodynamic stability than their non-switch analogs.

ABSTRACT: The ability to regulate cellular protein activity offers a broad range of biotechnological and biomedical applications. Such protein regulation can be achieved by modulating the specific protein activity or through processes that regulate the amount of protein in the cell. We have previously demonstrated that the nonhomologous recombination of the genes encoding maltose binding protein (MBP) and TEM1 β-lactamase (BLA) can result in genes that confer maltose-dependent resistance to β-lactam antibiotics even though the encoded proteins are not allosteric enzymes. We showed that these phenotypic switches-named based on their conferral of a switching phenotype to cells-resulted from a specific interaction with maltose in the cell that increased the switches cellular accumulation. Since phenoty

SUBMITTER: Choi JH 

PROVIDER: S-EPMC3610053 | biostudies-literature | 2013 Apr

REPOSITORIES: biostudies-literature