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Literature summary extracted from

  • Hashimoto, S.; Okada, K.; Imaoka, S.
    Interaction between bisphenol derivatives and protein disulphide isomerase (PDI) and inhibition of PDI functions: requirement of chemical structure for binding to PDI (2008), J. Biochem., 144, 335-342.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.3.4.1
-
Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
5.3.4.1 C398A/C401A 90% residual isomerase activity Rattus norvegicus
5.3.4.1 C54A/C57A 30% residual isomerase activity Rattus norvegicus
5.3.4.1 C54A/C57A/C398A/C401A 15% residual isomerase activity Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.3.4.1 1,1-bis(4-hydroxyphenyl)ethane i.e.bisphenol E, 15% inhibition at 0.0125 mM Rattus norvegicus
5.3.4.1 1,3-diphenylpropane 8% inhibition at 0.0125 mM Rattus norvegicus
5.3.4.1 2,2-bis(4-hydroxyphenyl)propane i.e. bisphenol A, 30% inhibition at 0.0125 mM Rattus norvegicus
5.3.4.1 3,3',5-triiodo-L-thyronine 30% inhibition at 0.0125 mM Rattus norvegicus
5.3.4.1 4,4'-methylenebisphenol 12% inhibition at 0.0125 mM Rattus norvegicus
5.3.4.1 4-alpha-cumylphenol 18% inhibition at 0.0125 mM Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
5.3.4.1 Rattus norvegicus
-
-
-