Literature summary for 3.4.22.65 extracted from

Takahashi, K.; Takai, T.; Yasuhara, T.; Yuuki, T.; Ohtake, Y.; Yokota, T.; Okumura, Y.
Production of enzymatically and immunologically active Der f1 in Escherichia coli (2000), Int. Arch. Allergy Immunol., 122, 108-114.

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Cloned(Commentary)

Cloned (Comment)	Organism
construction of an isopropyl-beta-D-thiogalactopyranoside-inducible expression plasmid to produce the pro-form of Der f1 in Escherichia coli	Dermatophagoides farinae

Organism

Organism	UniProt	Comment	Textmining
Dermatophagoides farinae	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	the removal of the pro-sequence is necessary for the cysteine protease activity. Acid treatment of the renatured pro Der f1 results in the autocatalytic removal of the pro-sequence. The obtained mature form of Der f1 binds IgE in patient sera and induces the release of histamine from peripheral blood leukocytes equally to native Der f1	Dermatophagoides farinae

Source Tissue

Source Tissue	Comment	Organism	Textmining
feces	-	Dermatophagoides farinae	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O	more efficiently hydrolyzed than N-succinyl-Ala-Pro-Ala-7-amido-4-methylcoumarin	Dermatophagoides farinae	butyloxycarbonyl-Val-Leu-Lys + 7-amino-4-methylcoumarin	-	?
additional information	mature recombinant enzyme shows the same IgE binding activity as the native enzyme	Dermatophagoides farinae	?	-	?
N-succinyl-Ala-Pro-Ala-7-amido-4-methylcoumarin	-	Dermatophagoides farinae	N-succinyl-Ala-Pro-Ala + 7-amino-4-methylcoumarin	-	?
N-succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin	more efficiently hydrolyzed than N-succinyl-Ala-Pro-Ala-7-amido-4-methylcoumarin	Dermatophagoides farinae	N-succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin	-	?

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Release 2023.1 (January 2023)