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Literature summary for 5.3.4.1 extracted from

  • Okada, K.; Hashimoto, S.; Imaoka, S.
    Biological functions of protein disulfide isomerase as a target of phenolic endocrine-disrupting chemicals (2010), J. Health Sci., 56, 1-13.
No PubMed abstract available
Search for more literature for 5.3.4.1

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of PDI in GH3 cells, that release growth hormone via the T3-receptor, leads to reduced T3-induced GH release in the cells, mechanism, overview Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
3,3',5-triiodo-L-thyronine inhibits PDI isomerase activity Homo sapiens
3,3',5-triiodo-L-thyronine inhibits PDI isomerase activity Mus musculus
3,3',5-triiodo-L-thyronine inhibits PDI isomerase activity Rattus norvegicus
3,4-dichlorophenol inhibits PDI 3,3',5-triiodo-L-thyronine binding activity Homo sapiens
3,4-dichlorophenol inhibits PDI 3,3',5-triiodo-L-thyronine binding activity Mus musculus
3,4-dichlorophenol inhibits PDI 3,3',5-triiodo-L-thyronine binding activity Rattus norvegicus
4-nonylphenol inhibits PDI 3,3',5-triiodo-L-thyronine binding activity Homo sapiens
4-nonylphenol inhibits PDI 3,3',5-triiodo-L-thyronine binding activity Mus musculus
4-nonylphenol inhibits PDI 3,3',5-triiodo-L-thyronine binding activity Rattus norvegicus
4-octylphenol inhibits PDI 3,3',5-triiodo-L-thyronine binding activity Homo sapiens
4-octylphenol inhibits PDI 3,3',5-triiodo-L-thyronine binding activity Mus musculus
4-octylphenol inhibits PDI 3,3',5-triiodo-L-thyronine binding activity Rattus norvegicus
bisphenol A i.e. 2,2-bis(4-hydroxyphenyl)propane, an endocrine disrupting chemical, inhibiting the enzyme's 3,3',5-triiodo-L-thyronine binding activity, its chaperone activity, and its isomerase activity, structural requirements, overview. Inhibits also PDI family members ERp57 and ERp72 Homo sapiens
bisphenol A i.e. 2,2-bis(4-hydroxyphenyl)propane, an endocrine disrupting chemical, inhibiting the enzyme's 3,3',5-triiodo-L-thyronine binding activity, its chaperone activity, and its isomerase activity, structural requirements, overview Mus musculus
bisphenol A i.e. 2,2-bis(4-hydroxyphenyl)propane, an endocrine disrupting chemical, inhibiting the enzyme's 3,3',5-triiodo-L-thyronine binding activity, its chaperone activity, and its isomerase activity, structural requirements, overview Rattus norvegicus
Pentachlorophenol inhibits PDI 3,3',5-triiodo-L-thyronine binding activity Homo sapiens
Pentachlorophenol inhibits PDI 3,3',5-triiodo-L-thyronine binding activity Mus musculus
Pentachlorophenol inhibits PDI 3,3',5-triiodo-L-thyronine binding activity Rattus norvegicus
tetrabromobisphenyl A TBBPA, inhibits PDI 3,3',5-triiodo-L-thyronine binding activity Homo sapiens
tetrabromobisphenyl A TBBPA, inhibits PDI 3,3',5-triiodo-L-thyronine binding activity Mus musculus
tetrabromobisphenyl A TBBPA, inhibits PDI 3,3',5-triiodo-L-thyronine binding activity Rattus norvegicus
tetrachlorobisphenyl A TCBPA, inhibits PDI 3,3',5-triiodo-L-thyronine binding activity Homo sapiens
tetrachlorobisphenyl A TCBPA, inhibits PDI 3,3',5-triiodo-L-thyronine binding activity Mus musculus
tetrachlorobisphenyl A TCBPA, inhibits PDI 3,3',5-triiodo-L-thyronine binding activity Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
 Mus musculus 5783
-
endoplasmic reticulum
-
 Homo sapiens 5783
-
endoplasmic reticulum
-
 Rattus norvegicus 5783
-
membrane associated Mus musculus 16020
-
membrane associated Homo sapiens 16020
-
membrane associated Rattus norvegicus 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ possibly bound at the C-terminal extension Mus musculus
Ca2+ possibly bound at the C-terminal extension Homo sapiens
Ca2+ possibly bound at the C-terminal extension Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mus musculus PDI specifically binds 3,3',5-triiodo-L-thyronine ?
-
 ?
additional information Homo sapiens PDI specifically binds 3,3',5-triiodo-L-thyronine ?
-
 ?
additional information Rattus norvegicus PDI specifically binds 3,3',5-triiodo-L-thyronine ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Mus musculus
-
-
-
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Rattus norvegicus
-
GH3 cell a pituitary carcinoma celll line Rattus norvegicus
-
pituitary gland
-
 Mus musculus
-
pituitary gland
-
 Homo sapiens
-
pituitary gland
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information PDI specifically binds 3,3',5-triiodo-L-thyronine Mus musculus ?
-
 ?
additional information PDI specifically binds 3,3',5-triiodo-L-thyronine Homo sapiens ?
-
 ?
additional information PDI specifically binds 3,3',5-triiodo-L-thyronine Rattus norvegicus ?
-
 ?
additional information the enzyme's isomerase activity comprises disulfide reduction, refolding, and oxidation of thiols requiring all four thioredoxin-folded domains in tandem link plus the C-terminal acidic extension Mus musculus ?
-
 ?
additional information the enzyme's isomerase activity comprises disulfide reduction, refolding, and oxidation of thiols requiring all four thioredoxin-folded domains in tandem link plus the C-terminal acidic extension Homo sapiens ?
-
 ?
additional information the enzyme's isomerase activity comprises disulfide reduction, refolding, and oxidation of thiols requiring all four thioredoxin-folded domains in tandem link plus the C-terminal acidic extension Rattus norvegicus ?
-
 ?

Subunits

Subunits Comment Organism
More the enzyme molecule has four domains a,a', b, and b', each possessing a thioredoxin fold, the domain a and a' show catalytic sites with the Cys-Gly-His-Cys motif, the b and b' domains possess substrate binding sites, domains b' and a' are linked via linker x, and the enbzyme also posseses a C-terminal acidic alpha-helix containing the endoplasmic reticulum retention signal, domain structure, overview Mus musculus
More the enzyme molecule has four domains a,a', b, and b', each possessing a thioredoxin fold, the domain a and a' show catalytic sites with the Cys-Gly-His-Cys motif, the b and b' domains possess substrate binding sites, domains b' and a' are linked via linker x, and the enbzyme also posseses a C-terminal acidic alpha-helix containing the endoplasmic reticulum retention signal, domain structure, overview Homo sapiens
More the enzyme molecule has four domains a,a', b, and b', each possessing a thioredoxin fold, the domain a and a' show catalytic sites with the Cys-Gly-His-Cys motif, the b and b' domains possess substrate binding sites, domains b' and a' are linked via linker x, and the enzyme also posseses a C-terminal acidic alpha-helix containing the endoplasmic reticulum retention signal, domain structure, overview Rattus norvegicus

Synonyms

Synonyms Comment Organism
ERp28
-
 Homo sapiens
ERp44
-
 Homo sapiens
ERp57
-
 Homo sapiens
ERp72
-
 Homo sapiens
P5
-
 Homo sapiens
PDI
-
 Homo sapiens
PDI
-
 Rattus norvegicus
PDIp
-
 Homo sapiens
PDIr
-
 Homo sapiens

General Information

General Information Comment Organism
physiological function PDI is a key enzyme involved in formation of correct pattern of disulfide bonds in proteins. PDI also plays an important role in the hypothalamic-pituitary-thyroid axis, mechanism, overview Mus musculus
physiological function PDI is a key enzyme involved in formation of correct pattern of disulfide bonds in proteins. PDI also plays an important role in the hypothalamic-pituitary-thyroid axis, mechanism, overview Homo sapiens
physiological function PDI is a key enzyme involved in formation of correct pattern of disulfide bonds in proteins. PDI also plays an important role in the hypothalamic-pituitary-thyroid axis, mechanism, overview Rattus norvegicus