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Literature summary for 5.3.4.1 extracted from

  • Markus, M.; Benezra, R.
    Two isoforms of protein disulfide isomerase alter the dimerization status of E2A proteins by a redox mechanism (1999), J. Biol. Chem., 274, 1040-1049.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
57000
-
x * 57000, SDS-PAGE, immunoprecipitation Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
E2A homodimer Homo sapiens PDI I and PDI II foster heterodimer formation between E proteins, i.e. basic-loop-helix proteins of the E2A gene products, by a redox mechanism E2A-basic helix-loop-helix protein heterodimer
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
E2A homodimer PDI I and PDI II foster heterodimer formation between E proteins, i.e. basic-loop-helix proteins of the E2A gene products, by a redox mechanism Homo sapiens E2A-basic helix-loop-helix protein heterodimer
-
?

Subunits

Subunits Comment Organism
? x * 57000, SDS-PAGE, immunoprecipitation Homo sapiens

Synonyms

Synonyms Comment Organism
PDI I
-
Homo sapiens
PDI II
-
Homo sapiens