Role of Aspartate 42 and Histidine 79 in the aiPLA2 activity and oligomeric status of Prdx6 at low pH.

ABSTRACT: Peroxiredoxin 6 (Prdx6), a unique non-seleno peroxidase, is a bifunctional protein with GSH peroxidase at pH 7.4 and calcium independent phospholipase A₂ (aiPLA₂) activities at pH 4.0. Changes in pH brings about alteration in the conformational and thermodynamic stability of Prdx6. For instance, under acidic condition (pH 4.0), Prdx6 forms higher oligomers with concommittant gain in aiPLA₂ activity that is resistant to thermal denaturation. However, there has been no molecular level understanding of how low pH induces formation of oligomers. In the present study, site directed mutagenesis of two conserved amino acid residues, Asp42 and His79, was used to study the molecular basis for the influence of pH on the oligomeric state of Prdx6. We observed that mut

SUBMITTER: Kakchingtabam P 

PROVIDER: S-EPMC11703348 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature