Lipoprotein-associated phospholipase A₂: A paradigm for allosteric regulation by membranes.

ABSTRACT: Lipoprotein-associated phospholipase A₂ (Lp-PLA₂) associates with low- and high-density lipoproteins in human plasma and specifically hydrolyzes circulating oxidized phospholipids involved in oxidative stress. The association of this enzyme with the lipoprotein's phospholipid monolayer to access its substrate is the most crucial first step in its catalytic cycle. The current study demonstrates unequivocally that a significant movement of a major helical peptide region occurs upon membrane binding, resulting in a large conformational change upon Lp-PLA₂ binding to a phospholipid surface. This allosteric regulation of an enzyme's activity by a large membrane-like interface inducing a conformational change in the catalytic site defines a unique dimension of al

SUBMITTER: Mouchlis VD 

PROVIDER: S-EPMC8764669 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature