The disease-associated mutation of the mitochondrial sulphydryl oxidase Erv1 impairs cofactor binding during its catalytic reaction

In this study, we use yeast Erv1 as a model to provide clear evidence for a progressive functional defect in the catalytic activity of the corresponding Erv1 R182H mutant. We show that the FAD cofactor was released from Erv1 R182H during its catalytic cycle, which led to the inactivation of the enzyme. We also characterised the effects of the mutation on the folding and stability of Erv1, and tested our in vitro findings in vivo using a yeast genetic approach. The results of this study allows us to provide a model for the functional defect in Erv1 R182H, which could potentially be extended to human ALR R194H, and provides insights into the molecular basis of autosomal recessive myopathy.
Source: BJ Energy - Category: Biochemistry Authors: Tags: BJ Biomolecules Source Type: research