Systematic identification of allosteric effectors in <i>Escherichia coli</i> metabolism.

ABSTRACT: Recent physical binding screens suggest that protein-metabolite interactions are more extensive than previously recognized. To elucidate the functional relevance of these interactions, we developed a mass spectrometry-based screening method for higher throughput in vitro enzyme assays. By systematically quantifying the effects of 79 metabolites on the activity of 20 central Escherichia coli enzymes, we not only assess functional relevance but also gauge the depth of the current understanding of regulatory interactions within one of the best-characterized networks. Our identification of 50 inhibitors and 14 activators not only expands the range of known input signals but also uncovers novel regulatory logic. For instance, we observed that AMP inhibits malic enzyme to safeguard the cy

SUBMITTER: Gruber CH 

PROVIDER: S-EPMC11912433 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature