Literature summary for 5.3.4.1 extracted from

Wang, L.; Li, S.J.; Sidhu, A.; Zhu, L.; Liang, Y.; Freedman, R.B.; Wang, C.C.
Reconstitution of human Ero1-Lalpha/protein-disulfide isomerase oxidative folding pathway in vitro: position-dependent difference in role between the a and a' domains of protein disulfide isomerase (2009), J. Biol. Chem., 284, 199-206.

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
RNase A	reconstitution of the Ero1-Lalpha/protein disulfide isomerase oxidative folding system in vitro. The a' domain of protein disulfide isomerase is much more active than the a domain in Ero1-Lalpha-mediated folding. The minimal element for binding to Ero1-Lalpha are core element b, linker x and the a domain	Homo sapiens	?	-	?

Subunits

Subunits	Comment	Organism
More	reconstitution of the Ero1-Lalpha/protein disulfide isomerase oxidative folding system in vitro. The a' domain of protein disulfide isomerase is much more active than the a domain in Ero1-Lalpha-mediated folding. The minimal element for binding to Ero1-Lalpha are core element b, linker x and the a domain	Homo sapiens

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Release 2023.1 (January 2023)