Literature summary for 5.3.4.1 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.

Search for more literature for 5.3.4.1

Cloned(Commentary)

Cloned (Comment)	Organism
-	Rattus norvegicus

Protein Variants

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

Inhibitors

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

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

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Release 2023.1 (January 2023)