Cloned (Comment) | Organism |
---|---|
recombinant expression of wild-type and mutant enzymes in Escherichia coli. Recombinant PDIp protects the Escherichia coli cells against heat shock and oxidative stress-induced cell death independently of its enzymatic activity | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
additional information | mutation of the cysteine residues in PDIp's active sites, resulting in mutants DELTAC1, DELTAC2 and DELTAC1DELTAC2, completely abolishes its enzymatic activity but does not affect its chaperone activity, the b-b' fragment of PDIp, which does not contain the active sites and is devoid of enzymatic activity, still has chaperone activity | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
iodoacetamide | alkylation of PDIp by iodoacetamide fully abolishes its enzymatic activity while it still retains most of its chaperone activity | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Homo sapiens | PDIp also shows chaperone activity in preventing the aggregation of reduced insulin B chain and denatured D-glyceraldehyde-3-phosphate dehydrogenase, PDIp can form stable complexes with thermal-denatured substrate proteins, e.g. MCF-7 cellular proteins, independently of their enzymatic activity. The b-b' fragment of PDIp, which does not contain the active sites and is devoid of enzymatic activity, still has chaperone activity | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q13087 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and mutant enzymes from Escherichia coli | Homo sapiens |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
pancreas | pancreas-specific enzyme | Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | PDIp also shows chaperone activity in preventing the aggregation of reduced insulin B chain and denatured D-glyceraldehyde-3-phosphate dehydrogenase, PDIp can form stable complexes with thermal-denatured substrate proteins, e.g. MCF-7 cellular proteins, independently of their enzymatic activity. The b-b' fragment of PDIp, which does not contain the active sites and is devoid of enzymatic activity, still has chaperone activity | Homo sapiens | ? | - |
? | |
additional information | formation of active RNase from rRNase and sRNase in the presence of PDIp. The pancreas-specific PDI homolog PDIp can function independently as a chaperone in vitro and in vivo | Homo sapiens | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the two catalytic domains of PDIp, a and a', which contain the WCGHC and WCTHC motifs, respectively, may be responsible for its enzymatic activity, whereas the two non-catalytic domains, b and b', may be involved in substrate-binding | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
More | PDIp is a member of the protein disulfide isomerase PDI family | Homo sapiens |
pancreas-specific protein disulfide isomerase | - |
Homo sapiens |
PDIp | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
isomerase assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
isomerase assay at | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
physiological function | PDI is a multifunctional protein for catalyzing the formation, isomerization, and reduction of disulfide bonds | Homo sapiens |