protein disulfide isomerase.
The observation of multiple disulfide bonds in the recombinant form of the enzyme suggests the need for further investigations into whether the intracellular environment of P. aerophilum, and possibly other hyperthermophiles, may be compatible with protein disulfide bond formation.
Protein disulfide isomerases (PDIs), a family of structurally related enzymes, aid in protein folding by catalyzing disulfide bonds formation, breakage, or isomerization in newly synthesized proteins and thus.
The 55 kDa protein was identified as protein disulfide isomerase (PDI 11 (OsPDIL1 1; Os11g0199200) (Table 1).
Protein disulfide isomerase (spots LU14, LU15), an enzyme located in the endoplasmic reticulum, catalyzes the folding of many disulfide-bonded proteins (Freedman, 1984).
As discussed above, tissue factor is activated by protein disulfide isomerases (PDI) [56, 100 104].
Protein disulfide isomerase (PDI), a member of thioredoxin-superfamily, plays a key role in catalyzing disulfide bond formation, reduction, and isomerization.
Protein disulfide isomerases (PDIs) are eukaryotic oxidoreductases essential for oxidative protein folding.
Additional members include tryparedoxin of Trypanosomes, the protein disulfide isomerase and a few bacterial disulfide bondforming proteins.
Protein Disulfide Isomerase (PDI) is a multifunctional enzyme that primarily catalyzes disulfide bond formation, breakage, and rearrangement [8].
