d-Alanine–d-alanine ligase as a model for the activation of ATP-grasp enzymes by monovalent cations
Jordan L. Pederick, Andrew Thompson, Stephen G. Bell, John B. Bruning
Abstract
Ddl revealed no evident conformational change on MVC binding. Of note, the identified MVC binding site is structurally conserved within the ATP-grasp superfamily. We propose that MVCs activate Ddl by altering the charge distribution of its active site. These findings provide insight into the catalytic mechanism of ATP-grasp enzymes.
Topics & Concepts
Thermus thermophilusDNA ligaseEnzymeAlanineActive siteBiochemistryChemistryEnzyme activatorStereochemistryBiophysicsAmino acidBiologyEscherichia coliGeneAmino Acid Enzymes and MetabolismEnzyme Structure and FunctionPolyamine Metabolism and Applications