Literature summary for 3.5.1.11 extracted from

Ignatova, Z.; Mahsunah, A.; Georgieva, M.; Kasche, V.
Improvement of posttranslational bottlenecks in the production of penicillin amidase in recombinant Escherichia coli strains (2003), Appl. Environ. Microbiol., 69, 1237-1245.

Cloned(Commentary)

Cloned (Comment)	Organism
expression levels in various Escherichia coli host cells. Intracellular proteolytic degradation of the newly synthesized penicillin amidase precursor and translocation through the plasma membrane are determined to be the main posttranslational processes limiting enzyme production. The production of mature active penicillin amidase is increased up to 10fold when the protease deficient strain Escherichia coli BL21 (DE3) is cultivated in medium without a proteinaceous substrate. Simultaneous coexpression of the OmpT pac gene with some proteins of the Sec export machinery of the cell results in up to threefold-enhanced penicillin amidase production	Escherichia coli

Cloned (Comment)

Organism

expression levels in various Escherichia coli host cells. Intracellular proteolytic degradation of the newly synthesized penicillin amidase precursor and translocation through the plasma membrane are determined to be the main posttranslational processes limiting enzyme production. The production of mature active penicillin amidase is increased up to 10fold when the protease deficient strain Escherichia coli BL21 (DE3) is cultivated in medium without a proteinaceous substrate. Simultaneous coexpression of the OmpT pac gene with some proteins of the Sec export machinery of the cell results in up to threefold-enhanced penicillin amidase production

Escherichia coli

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
periplasm	-	Escherichia coli	-	-

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	ATCC 11105	-

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Release 2023.1 (January 2023)