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Literature summary for 5.3.4.1 extracted from

  • Fu, X.M.; Zhu, B.T.
    Human pancreas-specific protein disulfide isomerase (PDIp) can function as a chaperone independently of its enzymatic activity by forming stable complexes with denatured substrate proteins (2010), Biochem. J., 429, 157-169.
    View publication on PubMed

Cloned(Commentary)

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

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

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/ Products (Substrates)

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 ?
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?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q13087
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-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
pancreas pancreas-specific enzyme Homo sapiens
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Substrates and Products (Substrate)

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 ?
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?
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 ?
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?

Subunits

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

Synonyms Comment Organism
More PDIp is a member of the protein disulfide isomerase PDI family Homo sapiens
pancreas-specific protein disulfide isomerase
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Homo sapiens
PDIp
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Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
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isomerase assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
isomerase assay at Homo sapiens

General Information

General Information Comment Organism
physiological function PDI is a multifunctional protein for catalyzing the formation, isomerization, and reduction of disulfide bonds Homo sapiens