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Literature summary for 3.5.1.11 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.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Escherichia coli

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Temperature Stability [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 8.5
-
 Escherichia coli