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Literature summary for 3.5.1.11 extracted from

  • Kasche, V.; Galunsky, B.; Ignatova, Z.
    Fragments of pro-peptide activate mature penicillin amidase of Alcaligenes faecalis (2003), Eur. J. Biochem., 270, 4721-4728.
    View publication on PubMed
Search for more literature for 3.5.1.11

Activating Compound

Activating Compound Comment Organism Structure
additional information addition of chemically synthesized fragments of the pro-peptide to purified mature enzyme increases its specific activity up to 2.3fold Alcaligenes faecalis

Protein Variants

Protein Variants Comment Organism
T206G specific activity of the mutant enzyme is 60% higher compared to the wild-type enzyme, pI is 5.5 Alcaligenes faecalis
T206G/G213G mutant enzyme with 1.9fold increased specific activity compared to completely processed wild-type enzyme, mutation stabilizes the precursor form, pI value is 5.6 Alcaligenes faecalis
T206G/S213G/T219G mutant enzyme with 2.3fold increased specific activity compared to completely processed wild-type enzyme Alcaligenes faecalis
T206P mutant undergoes normal proteolytic processing leading to a completely processed enzyme with pI 5.3 Alcaligenes faecalis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0065
-
 benzylpenicillin pH 7.5, 25°C, mutant enzyme T206G/S213G/T219G Alcaligenes faecalis
0.007
-
 benzylpenicillin pH 7.5, 25°C, mutant enzyme T206G//S213G Alcaligenes faecalis
0.008
-
 benzylpenicillin pH 7.5, 25°C, mutant enzyme T206G and wild-type enzyme Alcaligenes faecalis

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ catalytically active enzyme contains one tightly bound Ca2+ Alcaligenes faecalis

Organism

Organism UniProt Comment Textmining
Alcaligenes faecalis
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the enzyme is maturated in vivo from an inactive precursor into the catalytically active enzyme, via a complex post-translational autocatalytic processing with a multi-step excision of a small internal pro-peptide Alcaligenes faecalis

Purification (Commentary)

Purification (Comment) Organism
wild-type enzyme and pro-peptide mutants T206G, T206P, T206G/G213G and T206G/S213G/T219G Alcaligenes faecalis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzylpenicillin + H2O
-
 Alcaligenes faecalis phenylacetic acid + 6-aminopenicillanate
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
80
-
 benzylpenicillin pH 7.5, 25°C, wild-type enzyme Alcaligenes faecalis
120
-
 benzylpenicillin pH 7.5, 25°C, mutant enzyme T206G Alcaligenes faecalis
140
-
 benzylpenicillin pH 7.5, 25°C, mutant enzyme T206G//S213G Alcaligenes faecalis
190
-
 benzylpenicillin pH 7.5, 25°C, mutant enzyme T206G/S213G/T219G Alcaligenes faecalis

pI Value

Organism Comment pI Value Maximum pI Value
Alcaligenes faecalis wild-type enzyme and pro-peptide mutant T206P, isoelectric focusing
-
 5.3
Alcaligenes faecalis pro-peptide mutant enzymes T206G and T206G/S213G/T219G, isoelectric focusing
-
 5.5
Alcaligenes faecalis pro-peptide mutant enzyme T206G/S213G, isoelectric focusing 5.9 5.6