Literature summary for 3.4.22.65 extracted from

Zhang, J.; Hamilton, J.M.; Garrod, D.R.; Robinson, C.
Interactions between mature Der p 1 and its free prodomain indicate membership of a new family of C1 peptidases (2007), Allergy, 62, 1302-1309.

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Cloned(Commentary)

Cloned (Comment)	Organism
the propiece of Der p 1 is PCR cloned and expressed in Escherichia coli	Dermatophagoides pteronyssinus

Inhibitors

Inhibitors	Comment	Organism	Structure
Der p 1 propiece	potent competitive inhibitor of Der p 1. The Der p 1 propiece behaves as a substrate and is fully degraded during this interaction	Dermatophagoides pteronyssinus

Organism

Organism	UniProt	Comment	Textmining
Dermatophagoides pteronyssinus	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	the Der p 1 propiece is a potent competitive inhibitor of Der p 1. The Der p 1 propiece behaves as a substrate and is fully degraded during this interaction. The rapid inactivation of Der p 1 prodomain is a mechanism that may contribute to the potency of this allergen	Dermatophagoides pteronyssinus

Purification (Commentary)

Purification (Comment)	Organism
-	Dermatophagoides pteronyssinus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Der p 1 propiece + H2O	potent competitive inhibitor of Der p 1. The Der p 1 propiece behaves as a substrate and is fully degraded during this interaction. The rapid inactivation of Der p 1 prodomain is a mechanism that may contribute to the potency of this allergen	Dermatophagoides pteronyssinus	?	-	?

Synonyms

Synonyms	Comment	Organism
Der p 1	-	Dermatophagoides pteronyssinus

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Release 2023.1 (January 2023)