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Literature summary extracted from

  • Marschall, R.; Tudzynski, P.
    The protein disulfide isomerase of Botrytis cinerea an ER protein involved in protein folding and redox homeostasis influences NADPH oxidase signaling processes (2017), Front. Microbiol., 8, 960 .
    View publication on PubMedView publication on EuropePMC

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
5.3.4.1 endoplasmic reticulum
-
 Botrytis cinerea 5783
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.3.4.1 NADPH oxidase A Botrytis cinerea
-
 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
5.3.4.1 Botrytis cinerea
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
5.3.4.1 phosphoprotein
-
 Botrytis cinerea

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.4.1 NADPH oxidase A
-
 Botrytis cinerea ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
5.3.4.1 PDI1
-
 Botrytis cinerea
5.3.4.1 protein disulfide isomerase
-
 Botrytis cinerea

General Information

EC Number General Information Comment Organism
5.3.4.1 physiological function the enzyme affects the redox homeostasis and unfolded protein response-related genes. The enzyme is involved in all major developmental processes, such as the formation of sclerotia, conidial anastomosis tubes and infection cushions, is involved in oxidative and osmotic stress resistance, and needed for full virulence Botrytis cinerea