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Literature summary extracted from
- Molecular cloning and characterization of soybean protein disulfide isomerase family proteins with nonclassic active center motifs (2009), FEBS J., 276, 4130-4141.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.3.4.1 | GmPDIL-3a and GmPDIL-3b isozymes, cloning of mature GmPDIL-3a (Thr24-Leu520) and GmPDIL-3b (Ser27-Leu523), excluding the putative signal peptides, expression in Escherichia coli strain BL21(DE3) | Glycine max |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.3.4.1 | additional information | both GmPDIL-3a and GmPDIL-3b are resistant to protease treatment in the absence of detergent, and are degraded when detergent is added | Glycine max |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 5.3.4.1 | endoplasmic reticulum lumen | GmPDIL-3a and GmPDIL-3b form protein complexes in the endoplasmic reticulum | Glycine max | 5788 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.3.4.1 | Mg2+ | - |
Glycine max |  |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 5.3.4.1 | 130000 | 300000 | GmPDIL-3a-GmPDIL-3b protein complexes | Glycine max |
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 | Glycine max | GmPDIL-1 and GmPDIL-2 function as molecular chaperones, and prevent the aggregation of unfolded rhodanese, while GmPDIL-3a and GmPDIL-3b do not | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.3.4.1 | Glycine max | - |
cv. Jack, isozymes GmPDIL-1, GmPDIL-2, GmPDIL-3a, and GmPDIL-3b | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 5.3.4.1 | recombinant mature GmPDIL-3a (Thr24-Leu520) and GmPDIL-3b (Ser27-Leu523), excluding the putative signal peptides, from Escherichia coli strain BL21(DE3) | Glycine max |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 5.3.4.1 | cotyledon | expression of GmPDIL-3a and GmPDIL-3b in soybean cotyledons during maturation, overview | Glycine max | - |
| 5.3.4.1 | leaf | trifoliolate center leaves | Glycine max | - |
| 5.3.4.1 | additional information | GmPDIL-3a and GmPDIL-3b are ubiquitously expressed in the plant body | Glycine max | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.3.4.1 | additional information | GmPDIL-1 and GmPDIL-2 function as molecular chaperones, and prevent the aggregation of unfolded rhodanese, while GmPDIL-3a and GmPDIL-3b do not | Glycine max | ? | - |
? | |
| 5.3.4.1 | additional information | recombinant GmPDIL-3a and GmPDIL-3b do not function as oxidoreductases or as molecular chaperones in vitro, although a proportion of each protein formed complexes in both thiol-dependent and thiol-independent ways in the endoplasmic reticulum. GmPDIL-3a and GmPDIL-3b have no stimulatory effect on the oxidative refolding of RNase A by GmPDIL-1 and GmPDIL-2 when mixed together, further confirming that the functional properties of GmPDIL-3a and GmPDIL-3b are probably unique | Glycine max | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.3.4.1 | More | GmPDIL-3a and GmPDIL-3b are plant endoplasmic reticulum PDI family proteins containing the nonclassic redox center motif CXXS? C | Glycine max |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.3.4.1 | More | PDI and other PDI family proteins are members of the thioredoxin superfamily | Glycine max |
| 5.3.4.1 | PDI | - |
Glycine max |
| 5.3.4.1 | protein disulfide isomerase | - |
Glycine max |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.3.4.1 | 25 | - |
assay at | Glycine max |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.3.4.1 | 7.5 | - |
assay at | Glycine max |
Expression
| EC Number | Organism | Comment | Expression |
|---|---|---|---|
| 5.3.4.1 | Glycine max | expression of GmPDIL-3a and GmPDIL-3b in the cotyledon increases during seed maturation when synthesis of storage proteins is initiated | up |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 5.3.4.1 | physiological function | PDI and other PDI family proteins are thought to play important roles in disulfide bond formation and isomerization in the endoplasmic reticulum | Glycine max |
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