Racemases and epimerases operating through a 1,1-proton transfer mechanism: reactivity, mechanism and inhibition.

ABSTRACT: Racemases and epimerases catalyse changes in the stereochemical configurations of chiral centres and are of interest as model enzymes and as biotechnological tools. They also occupy pivotal positions within metabolic pathways and, hence, many of them are important drug targets. This review summarises the catalytic mechanisms of PLP-dependent, enolase family and cofactor-independent racemases and epimerases operating by a deprotonation/reprotonation (1,1-proton transfer) mechanism and methods for measuring their catalytic activity. Strategies for inhibiting these enzymes are reviewed, as are specific examples of inhibitors. Rational design of inhibitors based on substrates has been extensively explored but there is considerable scope for development of transition-state mimics and covalent i

SUBMITTER: Lloyd MD 

PROVIDER: S-EPMC8142540 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature