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Literature summary for 5.3.4.1 extracted from

  • Gruber, C.W.; Cemazar, M.; Heras, B.; Martin, J.L.; Craik, D.J.
    Protein disulfide isomerase: the structure of oxidative folding (2006), Trends Biochem. Sci., 31, 455-464.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
Chlamydomonas reinhardtii 9507
-
chloroplast
-
Arabidopsis thaliana 9507
-
endoplasmic reticulum
-
Chlamydomonas reinhardtii 5783
-
endoplasmic reticulum
-
Arabidopsis thaliana 5783
-
endoplasmic reticulum
-
Homo sapiens 5783
-
endoplasmic reticulum
-
Saccharomyces cerevisiae 5783
-
membrane
-
Escherichia coli 16020
-
periplasm
-
Escherichia coli
-
-
thylakoid membrane
-
Arabidopsis thaliana 42651
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli PDI oxidizes pairs of cysteines to form disulfide bonds and can also shuffle incorrect disulfides into their correct pairings, function and mechanism of PDI, bacterial machinery for disulfide formation and oxidative protein folding, overview ?
-
?
additional information Chlamydomonas reinhardtii structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview ?
-
?
additional information Arabidopsis thaliana structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview ?
-
?
additional information Homo sapiens structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview ?
-
?
additional information Saccharomyces cerevisiae structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview ?
-
?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-
Chlamydomonas reinhardtii
-
-
-
Escherichia coli
-
-
-
Homo sapiens P07237
-
-
Saccharomyces cerevisiae P17967
-
-

Reaction

Reaction Comment Organism Reaction ID
catalyses the rearrangement of -S-S- bonds in proteins substrate binding and catalytic mechanism Chlamydomonas reinhardtii
catalyses the rearrangement of -S-S- bonds in proteins substrate binding and catalytic mechanism Escherichia coli
catalyses the rearrangement of -S-S- bonds in proteins substrate binding and catalytic mechanism Arabidopsis thaliana
catalyses the rearrangement of -S-S- bonds in proteins substrate binding and catalytic mechanism Homo sapiens
catalyses the rearrangement of -S-S- bonds in proteins substrate binding and catalytic mechanism Saccharomyces cerevisiae

Source Tissue

Source Tissue Comment Organism Textmining
pancreas PDIp Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information PDI oxidizes pairs of cysteines to form disulfide bonds and can also shuffle incorrect disulfides into their correct pairings, function and mechanism of PDI, bacterial machinery for disulfide formation and oxidative protein folding, overview Escherichia coli ?
-
?
additional information structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview Chlamydomonas reinhardtii ?
-
?
additional information structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview Arabidopsis thaliana ?
-
?
additional information structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview Homo sapiens ?
-
?
additional information structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview Saccharomyces cerevisiae ?
-
?
additional information PDI has the ability to catalyze dithiol-disulfide exchange reactions, chaperone activity and propensity to form subunits of multi-enzyme complexes, overview Escherichia coli ?
-
?
additional information PDI oxidizes pairs of cysteines to form disulfide bonds and can also shuffle incorrect disulfides into their correct pairings, function and mechanism of PDI, PDI has the ability to catalyze dithiol-disulfide exchange reactions, chaperone activity and propensity to form subunits of multi-enzyme complexes, overview Chlamydomonas reinhardtii ?
-
?
additional information PDI oxidizes pairs of cysteines to form disulfide bonds and can also shuffle incorrect disulfides into their correct pairings, function and mechanism of PDI, PDI has the ability to catalyze dithiol-disulfide exchange reactions, chaperone activity and propensity to form subunits of multi-enzyme complexes, overview Arabidopsis thaliana ?
-
?
additional information PDI oxidizes pairs of cysteines to form disulfide bonds and can also shuffle incorrect disulfides into their correct pairings, function and mechanism of PDI, PDI has the ability to catalyze dithiol-disulfide exchange reactions, chaperone activity and propensity to form subunits of multi-enzyme complexes, overview Homo sapiens ?
-
?
additional information PDI oxidizes pairs of cysteines to form disulfide bonds and can also shuffle incorrect disulfides into their correct pairings, function and mechanism of PDI, PDI has the ability to catalyze dithiol-disulfide exchange reactions, chaperone activity and propensity to form subunits of multi-enzyme complexes, overview Saccharomyces cerevisiae ?
-
?

Subunits

Subunits Comment Organism
More PDI domain structure, overview Chlamydomonas reinhardtii
More PDI domain structure, overview Escherichia coli
More PDI domain structure, overview Arabidopsis thaliana
More PDI domain structure, overview Homo sapiens
More PDI domain structure, overview Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
Dsb
-
Escherichia coli
ERp28
-
Homo sapiens
ERp57
-
Homo sapiens
ERp72
-
Homo sapiens
More the enzyme belongs to the Dsb family Escherichia coli
PDI
-
Chlamydomonas reinhardtii
PDI
-
Escherichia coli
PDI
-
Arabidopsis thaliana
PDI
-
Homo sapiens
PDI
-
Saccharomyces cerevisiae
PDIp
-
Homo sapiens
protein disulfide isomerase
-
Chlamydomonas reinhardtii
protein disulfide isomerase
-
Escherichia coli
protein disulfide isomerase
-
Arabidopsis thaliana
protein disulfide isomerase
-
Homo sapiens
protein disulfide isomerase
-
Saccharomyces cerevisiae
RB60
-
Chlamydomonas reinhardtii