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 (Comment) | Organism |
---|---|
recombinant expression in Escherichia coli strain BL21(DE3) | Alcaligenes faecalis |
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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
penicillin G + H2O | Alcaligenes faecalis | - |
phenylacetate + 6-aminopenicillanate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Alcaligenes faecalis | O34142 | - |
- |
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 (Comment) | Organism |
---|---|
recombinant enzyme from Escherichia coli strain BL21(DE3) by a single-step anion-exchange chromatography | Alcaligenes faecalis |
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 | Comment | Organism |
---|---|---|
More | three-dimensional structure, overview | Alcaligenes faecalis |
Synonyms | Comment | Organism |
---|---|---|
AfPGA | - |
Alcaligenes faecalis |
penicillin G acylase | - |
Alcaligenes faecalis |
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 |