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Literature summary extracted from

  • Chand, D.; Varshney, N.; Ramasamy, S.; Panigrahi, P.; Brannigan, J.A.; Wilkinson, A.J.; Suresh, C.G.
    Structure mediation in substrate binding and post-translational processing of penicillin acylases Information from mutant structures of Kluyvera citrophila penicillin G acylase (2015), Protein Sci., 24, 1660-1670 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.11 expression in Escherichia coli strain BL21 pLys (DE3) Kluyvera cryocrescens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.1.11 crystals of both mutants S1C and S1G belong to space group P1 with four molecules in the asymmetric unit. The three-dimensional structures of these mutants are refined at resolutions 2.8 A and 2.5 A, respectively. Comparison of the structures with similar structures of Escherichia coli PGA (EcPGA) reveals various conformational changes that lead to autocatalytic processing and consequent removal of the spacer peptide Kluyvera cryocrescens

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.11 S1C replacement of serine of the beta-subunit with cysteine results in a fully processed but inactive enzyme Kluyvera cryocrescens
3.5.1.11 S1G the second mutant in which the N-terminal serine is replaced by glycine remains in the unprocessed and inactive form Kluyvera cryocrescens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.11 2.7
-
 penicillin G pH 7.5, 50°C Kluyvera cryocrescens

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.11 Kluyvera cryocrescens P07941
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.5.1.11 proteolytic modification the enzyme is expressed as a 93000 Da inactive precursor in the cytoplasm which is directed to the periplasmic space by the 26 amino acid residue signal peptide. Subsequently, the spacer peptide is cleaved off by autocatalytic processing to generate the mature and active enzyme Kluyvera cryocrescens

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.11
-
 Kluyvera cryocrescens

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 62.5
-
 pH 7.5, 50°C Kluyvera cryocrescens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.11 penicillin G + H2O
-
 Kluyvera cryocrescens phenylacetate + 6-aminopenicillanate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.1.11 heterodimer 1 * 23000 (alpha-subunit) + 1 * 63000 (beta-subunit) Kluyvera cryocrescens

Synonyms

EC Number Synonyms Comment Organism
3.5.1.11 penicillin G acylase
-
 Kluyvera cryocrescens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.11 50
-
 assay at Kluyvera cryocrescens

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.1.11 60
-
 30 min, complete loss of activity Kluyvera cryocrescens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.11 7.5
-
-
 Kluyvera cryocrescens

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.5.1.11 7 8 the enzyme is active over the pH range 7.0-8.0 Kluyvera cryocrescens

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.5.1.11 4 10 stable Kluyvera cryocrescens
3.5.1.11 10
-
 23°C, 8 h, the enzyme retains 80% of its activity Kluyvera cryocrescens