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Literature summary extracted from

  • Narindrasorasak, S.; Yao, P.; Sarkar, B.
    Protein disulfide isomerase, a multifunctional protein chaperone, shows copper-binding activity (2003), Biochem. Biophys. Res. Commun., 311, 405-414.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.3.4.1 expression Escherichia coli Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
5.3.4.1 endoplasmic reticulum
-
Homo sapiens 5783
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.3.4.1 Ag+ PDI binds Ag+ Homo sapiens
5.3.4.1 Ca2+ major calcium binding protein of the endoplasmic reticulum Homo sapiens
5.3.4.1 Cu2+ PDI binds a maximum of 4 mol Cu2+ and is able to reduce it to Cu+, the bound Cu+ is surface-exposed Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
5.3.4.1 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.3.4.1 recombinant PDI Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.4.1 unfolded RNase A
-
Homo sapiens refolded RNase A
-
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