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Reduction-reoxidation cycles contribute to catalysis of disulfide isomerization by protein-disulfide isomerase.
Schwaller M, Wilkinson B, Gilbert HF. Schwaller M, et al. J Biol Chem. 2003 Feb 28;278(9):7154-9. doi: 10.1074/jbc.M211036200. Epub 2002 Dec 15. J Biol Chem. 2003. PMID: 12486139 Free article.
This led to the proposal that the second active site cysteine provides an escape mechanism, preventing PDI from becoming trapped with substrates that isomerize slowly (Walker, K. W., and Gilbert, H. F. (1997) J. Biol. Chem. 272, 8845-8848). Escape also reduces the s …
This led to the proposal that the second active site cysteine provides an escape mechanism, preventing PDI from becoming trapped with substr …
A structural disulfide of yeast protein-disulfide isomerase destabilizes the active site disulfide of the N-terminal thioredoxin domain.
Wilkinson B, Xiao R, Gilbert HF. Wilkinson B, et al. J Biol Chem. 2005 Mar 25;280(12):11483-7. doi: 10.1074/jbc.M414203200. Epub 2005 Jan 13. J Biol Chem. 2005. PMID: 15649885 Free article.
., Solovyov, A., Winther, J. R., Holmgren, A., Lundstrom-Ljung, J., and Gilbert, H. F. (2004) J. Biol. Chem. 279, 49780-49786) suggest that the internal cysteines exist as a disulfide in the endoplasmic reticulum of Saccharomyces cerevisiae. ...
., Solovyov, A., Winther, J. R., Holmgren, A., Lundstrom-Ljung, J., and Gilbert, H. F. (2004) J. Biol. Chem. 279, 49780-49786) …
955 results