Literature summary for 3.5.1.11 extracted from

Abian, O.; Grazu, V.; Hermoso, J.; Gonzalez, R.; Garcia, J.L.; Fernandez-Lafuente, R.; Guisan, J.M.
Stabilization of penicillin G acylase from Escherichia coli: site-directed mutagenesis of the protein surface to increase multipoint covalent attachment (2004), Appl. Environ. Microbiol., 70, 1249-1251.

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Protein Variants

Protein Variants	Comment	Organism
D13K	mutation in beta-subunit, no change in enzyme stability or kinetic properties, but improved stability after immobilization on glyoxyl-agarose	Escherichia coli
E272K	mutation in beta-subunit, no change in enzyme stability or kinetic properties, but improved stability after immobilization on glyoxyl-agarose	Escherichia coli
R276K	mutation in beta-subunit, no change in enzyme stability or kinetic properties, but improved stability after immobilization on glyoxyl-agarose	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

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Release 2023.1 (January 2023)