Electrostatic Perturbations in the Substrate-Binding Pocket of Taurine/α-Ketoglutarate Dioxygenase Determine its Selectivity.

ABSTRACT: Taurine/α-ketoglutarate dioxygenase is an important enzyme that takes part in the cysteine catabolism process in the human body and selectively hydroxylates taurine at the C¹ -position. Recent computational studies showed that in the gas-phase the C² -H bond of taurine is substantially weaker than the C¹ -H bond, yet no evidence exists of 2-hydroxytaurine products. To this end, a detailed computational study on the selectivity patterns in TauD was performed. The calculations show that the second-coordination sphere and the protonation states of residues play a major role in guiding the enzyme to the right selectivity. Specifically, a single proton on an active site histidine residue can change the regioselectivity of the reaction through its electrostatic p

SUBMITTER: Ali HS 

PROVIDER: S-EPMC9304159 | biostudies-literature | 2022 Feb

REPOSITORIES: biostudies-literature