Literature summary for 5.3.4.1 extracted from

Serve, O.; Kamiya, Y.; Maeno, A.; Nakano, M.; Murakami, C.; Sasakawa, H.; Yamaguchi, Y.; Harada, T.; Kurimoto, E.; Yagi-Utsumi, M.; Iguchi, T.; Inaba, K.; Kikuchi, J.; Asami, O.; Kajino, T.; Oka, T.; Nakasako, M.; Kato, K.
Redox-dependent domain rearrangement of protein disulfide isomerase coupled with exposure of its substrate-binding hydrophobic surface (2010), J. Mol. Biol., 396, 361-374.

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Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
endoplasmic reticulum	-	Humicola insolens	5783	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Humicola insolens	PDI is a major protein in the endoplasmic reticulum, operating as an essential folding catalyst and molecular chaperone for disulfide-containing proteins by catalyzing the formation, rearrangement, and breakage of their disulfide bridges	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Humicola insolens	P55059	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	PDI is a major protein in the endoplasmic reticulum, operating as an essential folding catalyst and molecular chaperone for disulfide-containing proteins by catalyzing the formation, rearrangement, and breakage of their disulfide bridges	Humicola insolens	?	-	?
additional information	the enzyme has a modular structure with four thioredoxin-like domains, a, b, b', and a', along with a C-terminal extension. The homologous a and a' domains contain one cysteine pair in their active site directly involved in thiol-disulfide exchange reactions, while the b' domain putatively provides a primary binding site for unstructured regions of the substrate polypeptides, mechanistic model of PDI action, overview. The a' domain transfers its own disulfide bond into the unfolded protein accommodated on the hydrophobic surface of the substrate-binding region, which consequently changes into a closed form releasing the oxidized substrate, domain arrangements and redox behaviour, overview	Humicola insolens	?	-	?

Subunits

Subunits	Comment	Organism
More	the enzyme has a modular structure with four thioredoxin-like domains, a, b, b', and a', along with a C-terminal extension. The homologous a and a' domains contain one cysteine pair in their active site directly involved in thiol-disulfide exchange reactions, while the b' domain putatively provides a primary binding site for unstructured regions of the substrate polypeptides, structure determination and analysis by NMR and small-angle X-ray scattering methods, domain arrangements and redox behaviour, overview	Humicola insolens

Synonyms

Synonyms	Comment	Organism
PDI	-	Humicola insolens
protein disulfide isomerase	-	Humicola insolens

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Release 2023.1 (January 2023)