Electrostatic fingerprints of catalytically active amino acids in enzymes.

ABSTRACT: The computed electrostatic and proton transfer properties are studied for 20 enzymes that represent all six major enzyme commission classes and a variety of different folds. The properties of aspartate, glutamate, and lysine residues that have been previously experimentally determined to be catalytically active are reported. The catalytic aspartate and glutamate residues studied here are strongly coupled to at least one other aspartate or glutamate residue and often to multiple other carboxylate residues with intrinsic pK_a differences less than 1 pH unit. Sometimes these catalytic acidic residues are also coupled to a histidine residue, such that the intrinsic pK_a of the acidic residue is higher than that of the histidine. All catalytic lysine residues studied here ar

SUBMITTER: Iyengar SM 

PROVIDER: S-EPMC8994506 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature