Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
endoplasmic reticulum | lumen | Streptomyces sp. | 5783 | - |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
55000 | - |
x * 55000 | Streptomyces sp. |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
alkaline protease inhibitor | Streptomyces sp. | folding and rearrangement of alkaline protease inhibitor | ? | - |
? | |
alkaline protease inhibitor | Streptomyces sp. NCIM 5127 | folding and rearrangement of alkaline protease inhibitor | ? | - |
? | |
additional information | Streptomyces sp. | both chaperone and isomerase functions of PDI are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitor API, PDI acts as isomerase/chaperone for a few monomeric proteins assisting in disulfide bond formation and rearrangement of secreted proteins | ? | - |
? | |
additional information | Streptomyces sp. NCIM 5127 | both chaperone and isomerase functions of PDI are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitor API, PDI acts as isomerase/chaperone for a few monomeric proteins assisting in disulfide bond formation and rearrangement of secreted proteins | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Streptomyces sp. | - |
NCIM 5127 | - |
Streptomyces sp. NCIM 5127 | - |
NCIM 5127 | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
- |
Streptomyces sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
alkaline protease inhibitor | folding and rearrangement of alkaline protease inhibitor | Streptomyces sp. | ? | - |
? | |
alkaline protease inhibitor | folding and rearrangement of alkaline protease inhibitor, PDI contains 2 cysteine residues in the active site which are involved in rearrangement of disulfide bonds by function in thiol/disulfide exchange | Streptomyces sp. | ? | - |
? | |
alkaline protease inhibitor | folding and rearrangement of alkaline protease inhibitor | Streptomyces sp. NCIM 5127 | ? | - |
? | |
alkaline protease inhibitor | folding and rearrangement of alkaline protease inhibitor, PDI contains 2 cysteine residues in the active site which are involved in rearrangement of disulfide bonds by function in thiol/disulfide exchange | Streptomyces sp. NCIM 5127 | ? | - |
? | |
additional information | both chaperone and isomerase functions of PDI are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitor API, PDI acts as isomerase/chaperone for a few monomeric proteins assisting in disulfide bond formation and rearrangement of secreted proteins | Streptomyces sp. | ? | - |
? | |
additional information | both chaperone and isomerase functions of PDI are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitor API, PDI acts as isomerase/chaperone for a few monomeric proteins assisting in disulfide bond formation and rearrangement of secreted proteins | Streptomyces sp. NCIM 5127 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 55000 | Streptomyces sp. |
Synonyms | Comment | Organism |
---|---|---|
PDI | - |
Streptomyces sp. |
protein disulfide isomerase | - |
Streptomyces sp. |