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Literature summary 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

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.5.1.11 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

EC Number Protein Variants Comment Organism
3.5.1.11 T206G specific activity of the mutant enzyme is 60% higher compared to the wild-type enzyme, pI is 5.5 Alcaligenes faecalis
3.5.1.11 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
3.5.1.11 T206G/S213G/T219G mutant enzyme with 2.3fold increased specific activity compared to completely processed wild-type enzyme Alcaligenes faecalis
3.5.1.11 T206P mutant undergoes normal proteolytic processing leading to a completely processed enzyme with pI 5.3 Alcaligenes faecalis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.11 0.0065
-
 benzylpenicillin pH 7.5, 25°C, mutant enzyme T206G/S213G/T219G Alcaligenes faecalis
3.5.1.11 0.007
-
 benzylpenicillin pH 7.5, 25°C, mutant enzyme T206G//S213G Alcaligenes faecalis
3.5.1.11 0.008
-
 benzylpenicillin pH 7.5, 25°C, mutant enzyme T206G and wild-type enzyme Alcaligenes faecalis

Metals/Ions

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

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.11 Alcaligenes faecalis
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.5.1.11 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)

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

Substrates and Products (Substrate)

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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.1.11 80
-
 benzylpenicillin pH 7.5, 25°C, wild-type enzyme Alcaligenes faecalis
3.5.1.11 120
-
 benzylpenicillin pH 7.5, 25°C, mutant enzyme T206G Alcaligenes faecalis
3.5.1.11 140
-
 benzylpenicillin pH 7.5, 25°C, mutant enzyme T206G//S213G Alcaligenes faecalis
3.5.1.11 190
-
 benzylpenicillin pH 7.5, 25°C, mutant enzyme T206G/S213G/T219G Alcaligenes faecalis

pI Value

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