Literature summary extracted from
Wilkinson, B.; Xiao, R.; Gilbert, H.F.
A structural disulfide of yeast protein-disulfide isomerase destabilizes the active site disulfide of the N-terminal thioredoxin domain (2005), J. Biol. Chem., 280, 11483-11487.
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
5.3.4.1 |
GSH |
required for activity |
Saccharomyces cerevisiae |
|
5.3.4.1 |
GSSG |
required for activity |
Saccharomyces cerevisiae |
|
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
5.3.4.1 |
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) |
Saccharomyces cerevisiae |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
5.3.4.1 |
C90A |
site-directed mutagenesis, mutation of a non-active site cysteine residue, reduced oxidase and isomerase activities compared to the wild-type enzyme |
Saccharomyces cerevisiae |
5.3.4.1 |
C90A/C97A |
site-directed mutagenesis, mutation of both non-active site cysteine residues, 60% and 80% reduced oxidase and isomerase activities, respectively, compared to the wild-type enzyme |
Saccharomyces cerevisiae |
5.3.4.1 |
C97A |
site-directed mutagenesis, mutation of a non-active site cysteine residue, reduced oxidase and isomerase activities compared to the wild-type enzyme |
Saccharomyces cerevisiae |
KM Value [mM]
EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Comment |
Organism |
Structure |
---|
5.3.4.1 |
additional information |
- |
additional information |
redox equilibrium measurements of wild-type and mutant C90A/C97A enzymes, determination of oxidase and isomerase activities |
Saccharomyces cerevisiae |
|
Localization
EC Number |
Localization |
Comment |
Organism |
GeneOntology No. |
Textmining |
---|
5.3.4.1 |
endoplasmic reticulum |
- |
Saccharomyces cerevisiae |
5783 |
- |
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
5.3.4.1 |
additional information |
Saccharomyces cerevisiae |
the enzyme is an essential catalyst of disulfide formation with two cysteines in the active site facilitating thiol-disulfide exchange |
? |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
5.3.4.1 |
Saccharomyces cerevisiae |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
5.3.4.1 |
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography |
Saccharomyces cerevisiae |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
5.3.4.1 |
catalyses the rearrangement of -S-S- bonds in proteins |
active site structure |
Saccharomyces cerevisiae |
|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
5.3.4.1 |
additional information |
the enzyme is an essential catalyst of disulfide formation with two cysteines in the active site facilitating thiol-disulfide exchange |
Saccharomyces cerevisiae |
? |
- |
? |
|
5.3.4.1 |
additional information |
non-active site cysteines form a disulfide bridges which destabilizes the N-terminal active site disulfide rendering it a 18fold better oxidant by this way |
Saccharomyces cerevisiae |
? |
- |
? |
|
5.3.4.1 |
ribonuclease |
refolding of ribonuclease, isomerase activity, renaturation of reduced ribonuclease, in presence of GSH and GSSG |
Saccharomyces cerevisiae |
? |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
5.3.4.1 |
More |
non-active site cysteines form a disulfide bridge that is stable even under very reducing environment destabilizing the N-terminal active site disulfide which becomes a 18fold better oxidant by this way |
Saccharomyces cerevisiae |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
5.3.4.1 |
PDI |
- |
Saccharomyces cerevisiae |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
5.3.4.1 |
25 |
- |
assay at |
Saccharomyces cerevisiae |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
5.3.4.1 |
8 |
- |
assay at |
Saccharomyces cerevisiae |