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Literature summary for 5.3.4.1 extracted from
- Protein disulfide isomerase-P5, down-regulated in the final stage of boar epididymal sperm maturation, catalyzes disulfide formation to inhibit protein function in oxidative refolding of reduced denatured lysozyme (2010), Biochim. Biophys. Acta, 1804, 1272-1284.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| isozymes PDIA3 and PDI-P5 precursors, DNA and amino acid sequence determination and analysis, expression of His-tagged mature isozymes in Escherichia coli strain HMS174 (DE3) | Sus scrofa |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | - |
Sus scrofa |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 48074 | - |
x * 48074, PDI-P5, sequence calculation, x * 56859, PDIA3, sequence calculation | Sus scrofa |
| 56859 | - |
x * 48074, PDI-P5, sequence calculation, x * 56859, PDIA3, sequence calculation | Sus scrofa |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Sus scrofa | PDIA3 shows chaperone activity to promote oxidative refolding of reduced denatured lysozyme, meanwhile PDI-P5 exhibits anti-chaperone activity to inhibit oxidative refolding of lysozyme at an equimolar ratio | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Sus scrofa | E1CAJ6 | PDI-P5; isozymes PDIA3 and PDI-P5 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged mature isozymes PDIA3 and PDI-P5 from Escherichia coli strain HMS174 (DE3) by nickel affinity chromatography and anion exchange chromatography, the His-tag of PDI-P5 is cleaved off | Sus scrofa |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| spermatozoon | epididymal caput, corpus, and cauda sperm, isozymes PDIA3 and PDI-P5. PDI-P5 is downregulated from the epididymal corpus to cauda sperm, while PDIA3 is constitutively expressed | Sus scrofa | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | PDIA3 shows chaperone activity to promote oxidative refolding of reduced denatured lysozyme, meanwhile PDI-P5 exhibits anti-chaperone activity to inhibit oxidative refolding of lysozyme at an equimolar ratio | Sus scrofa | ? | - |
? | |
| additional information | the isozymes catalyze refolding of reduced and denatured lysozyme | Sus scrofa | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 48074, PDI-P5, sequence calculation, x * 56859, PDIA3, sequence calculation | Sus scrofa |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PDI-P5 | - |
Sus scrofa |
| PDIA3 | - |
Sus scrofa |
| protein disulfide isomerase-P5 | - |
Sus scrofa |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Sus scrofa |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.6 | - |
assay at | Sus scrofa |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | physiological roles of PDIA3 and PDI-P5 in sperm maturation and fertilization, overview | Sus scrofa |
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Release 2023.1 (January 2023)
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