[HTML][HTML] Reconstitution of human Ero1-Lα/protein-disulfide isomerase oxidative folding pathway in vitro: position-dependent differences in role between the a and a …
L Wang, S Li, A Sidhu, L Zhu, Y Liang… - Journal of biological …, 2009 - ASBMB
Protein-disulfide isomerase (PDI), a critical enzyme responsible for oxidative protein folding
in the eukaryotic endoplasmic reticulum, is composed of four thioredoxin domains a, b, b′,
a′, and a linker x between b′ and a′. Ero1-Lα, an oxidase for human PDI (hPDI), has
been determined to have one molecular flavin adenine dinucleotide (FAD) as its prosthetic
group. Oxygen consumption assays with purified recombinant Ero1-Lα revealed that it
utilizes oxygen as a terminal electron acceptor producing one disulfide bond and one …
in the eukaryotic endoplasmic reticulum, is composed of four thioredoxin domains a, b, b′,
a′, and a linker x between b′ and a′. Ero1-Lα, an oxidase for human PDI (hPDI), has
been determined to have one molecular flavin adenine dinucleotide (FAD) as its prosthetic
group. Oxygen consumption assays with purified recombinant Ero1-Lα revealed that it
utilizes oxygen as a terminal electron acceptor producing one disulfide bond and one …