Literature summary for 3.5.1.11 extracted from

Kasche, V.; Lummer, K.; Nurk, A.; Piotraschke, E.; Rieks, A.; Stoeva, S.; Voelter, W.
Intramolecular autoproteolysis initiates the maturation of penicillin amidase from Escherichia coli (1999), Biochim. Biophys. Acta, 1433, 76-86.

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Protein Variants

Protein Variants	Comment	Organism
T263G	slowly processing mutant enzyme	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	enzyme form PA7.0 and enzyme form PA6.7	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	intramolecular autoproteolysis initiates the maturation of penicillin amidase from Escherichia coli. The Gly263-Ser264 bond is hydrolysed first in the free and immobilized mutant proenzyme T263G, this bond is hydrolyzed by intramolecular autoproteolysis	Escherichia coli

Purification (Commentary)

Purification (Comment)	Organism
mutant proenzyme T263G, expressed in Escherichia coli	Escherichia coli

pI Value

Organism	Comment	pI Value Maximum	pI Value
Escherichia coli	enzyme form PA6.7	-	6.7
Escherichia coli	enzyme form PA7.0	-	7

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Release 2023.1 (January 2023)