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Literature summary for 3.5.1.11 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

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

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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)

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

Organism

Organism UniProt Comment Textmining
Alcaligenes faecalis O34142
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
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)

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
AfPGA
-
Alcaligenes faecalis
penicillin G acylase
-
Alcaligenes faecalis

General Information

General Information Comment Organism
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
additional information three-dimensional structure, overview Alcaligenes faecalis