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Literature summary extracted from

  • Varshney, N.K.; Kumar, R.S.; Ignatova, Z.; Prabhune, A.; Pundle, A.; Dodson, E.; Suresh, C.G.
    Crystallization and X-ray structure analysis of a thermostable penicillin G acylase from Alcaligenes faecalis (2012), Acta Crystallogr. Sect. F, 68, 273-277.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
3.5.1.11 synthesis the enzyme is applied for large scale synthesis of 6-aminopenicillanic acid and 7-amino-3-deacetoxycephalosporanic acid Alcaligenes faecalis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.11 recombinant expression in Escherichia coli strain BL21(DE3) Alcaligenes faecalis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.1.11 purified enzyme, hanging drop vapour diffusion method, method optimization, from crystallization solution consisting of 15% w/v PEG 8000, 0.1 M Tris-HCl, pH 7.5, and 0.5% w/v beta-octyl-glucopyranoside solution. The presence of 0.06 ml beta-octyl-glucopyranoside in the well solution leads to orthorhombic crystals, whereas 0.1 ml beta-octyl-glucopyranoside result in tetragonal crystals, X-ray diffraction structure determination and analysis at A resolution at 3.3-3.5 A resolution, molecular replacement method Alcaligenes faecalis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.11 penicillin G + H2O Alcaligenes faecalis
-
 phenylacetate + 6-aminopenicillanate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.11 Alcaligenes faecalis O34142
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.5.1.11 proteolytic modification autocatalytical activation via translocation of the precursor to the periplasmic membrane and processing of the precursor by an autocatalytic intramolecular peptide-bond cleavage. Rate-limiting step in the production of active enzyme is the intramolecular autoproteolytic processing of the precursor molecule, resulting in the removal of a linker peptide Alcaligenes faecalis

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.11 recombinant enzyme from Escherichia coli strain BL21(DE3) by a single-step anion-exchange chromatography Alcaligenes faecalis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.11 penicillin G + H2O
-
 Alcaligenes faecalis phenylacetate + 6-aminopenicillanate
-
 ?
3.5.1.11 penicillin G + H2O penicillin G acylases preferentially hydrolyze penicillin G, i.e. benzylpenicillin Alcaligenes faecalis phenylacetate + 6-aminopenicillanate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.1.11 More three-dimensional structure, overview Alcaligenes faecalis

Synonyms

EC Number Synonyms Comment Organism
3.5.1.11 AfPGA
-
 Alcaligenes faecalis
3.5.1.11 penicillin G acylase
-
 Alcaligenes faecalis

General Information

EC Number General Information Comment Organism
3.5.1.11 evolution the enzyme belongs to the N-terminal nucleophilic hydrolase superfamily. Penicillin acylases are grouped into three classes according to their substrate specificity, penicillin G acylases (PGAs) preferentially hydrolyze penicillin G, i.e. benzylpenicillin Alcaligenes faecalis
3.5.1.11 additional information three-dimensional structure, overview Alcaligenes faecalis