Literature summary extracted from

Niersbach, H.; Kuhne, A.; Tischer, W.; Weber, M.; Wedekind F.; Plapp, R.
Improvement of the catalytic properties of penicillin G acylase from Escherichia coli ATCC 11105 by selection of a new substrate specificity (1995), Appl. Microbiol. Biotechnol., 43, 679-684.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
3.5.1.11	expression in Escherichia coli	Escherichia coli

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
3.5.1.11	additional information	-	additional information	further values of mutants	Escherichia coli
3.5.1.11	0.025	-	penicillin G	-	Escherichia coli
3.5.1.11	4.22	-	penicillin G	immobilized enzyme	Escherichia coli

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.5.1.11	Escherichia coli	-	-	-

Specific Activity [micromol/min/mg]

EC Number	Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
3.5.1.11	additional information	-	further values of mutants	Escherichia coli
3.5.1.11	1.64	-	penicillin G	Escherichia coli
3.5.1.11	2.35	-	cephalosporin G	Escherichia coli

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3.5.1.11	cephalosporin + H2O	-	Escherichia coli	7-aminocephalosporanic acid + an amino acid	-	?
3.5.1.11	penicillin G + H2O	-	Escherichia coli	6-aminopenicillanate + phenylacetic acid	-	r

Temperature Stability [°C]

EC Number	Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
3.5.1.11	50	-	loss of stability	Escherichia coli

pH Optimum

EC Number	pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
3.5.1.11	7	8.5	-	Escherichia coli

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Release 2023.1 (January 2023)