disulfide isomerase การใช้

• The PDIA3 protein is a thiol oxidoreductase that has protein disulfide isomerase activity.
• AGR2 is a protein disulfide isomerase, with CXXC active domain motifs for oxidation and reduction reactions.
• This enzyme is also a disulfide isomerase containing two thioredoxin domains that catalyze the formation, breakage and rearrangement of disulfide bonds.
• However, it lacks the thioredoxin motif characteristic of this family, suggesting that this protein does not function as a disulfide isomerase.
• The endosome is moved to the Golgi apparatus, where the A1 protein is recognized by the endoplasmic reticulum chaperon, protein disulfide isomerase.
• This gene encodes the beta subunit of prolyl 4-hydroxylase, a highly abundant multifunctional enzyme that belongs to the protein disulfide isomerase family.
• TTG also has GTPase activity : Besides its transglutaminase activity, tTG is proposed to also act as kinase, and protein disulfide isomerase, and deamidase.
• The A1 chain is then unfolded and delivered to the membrane, where Ero1 triggers the release of the A1 protein by oxidation of protein disulfide isomerase complex.
• Thioredoxin belongs to a structural family that includes glutaredoxin, glutathione peroxidase, bacterial protein disulfide isomerase DsbA, and the N-terminal domain of glutathione transferase.
• Protein disulfide isomerase ( PDI ), a resident foldase of the endoplasmic recticulum, is a multi-functional protein that catalyses the formation and isomerisation of disulfide bonds during protein folding.
• PDI contains 2 redox active domains, near the N-and C-termini, that are similar to thioredoxin : both contribute to disulfide isomerase activity, but are functionally non-equivalent.
• Ero1 is required for the introduction of oxidising equivalents into the ER and their direct transfer to protein disulfide isomerase ( PDI ), thereby ensuring the correct folding and assembly of proteins that contain disulfide bonds in their native state.
• The two cysteines in the first periplasmic domain are in a Cys-X-Y-Cys configuration that is characteristic of the active site of other proteins involved in disulfide bond formation, including DsbA and protein disulfide isomerase.
• MPyV membrane exit is believed to depend on the presence of specific host proteins located in the late ER; for example, the host protein ERp29, a member of the protein disulfide isomerase family, has been shown to disrupt the conformation of VP1.