EC Number | Cloned (Comment) | Organism |
---|---|---|
3.5.1.11 | gene yxeI, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression in Escherichia coli strain BL21(DE3) | Bacillus subtilis |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.5.1.11 | C1A | no activity, catalytic residue | Bacillus subtilis |
3.5.1.11 | C1S | no activity, catalytic residue | Bacillus subtilis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.5.1.11 | cephalosporin C | 65% inhibition; 65% inhibition at 1 mM | Bacillus subtilis | |
3.5.1.11 | cephalosporin G | 79% inhibition; 79% inhibition at 1 mM | Bacillus subtilis | |
3.5.1.11 | deoxycholic acid | slight inhibition | Bacillus subtilis | |
3.5.1.11 | glycodeoxycholic acid | slight inhibition | Bacillus subtilis | |
3.5.1.11 | additional information | poor inhibition by Fe2+, Mn2+, and Co2+ | Bacillus subtilis | |
3.5.1.11 | Ni2+ | slight inhibition | Bacillus subtilis | |
3.5.1.11 | phenoxyacetic acid | slight inhibition | Bacillus subtilis | |
3.5.1.11 | taurodeoxycholic acid | slight inhibition | Bacillus subtilis | |
3.5.1.11 | Zn2+ | slight inhibition | Bacillus subtilis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.5.1.11 | additional information | - |
additional information | MichaelisMenten kinetics | Bacillus subtilis | |
3.5.1.11 | 0.63 | - |
2-nitro-5-(phenoxyacetamido)-benzoic acid | pH 6.6, 40°C | Bacillus subtilis | |
3.5.1.11 | 40 | - |
Penicillin V | pH 6.6, 40°C | Bacillus subtilis |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.5.1.11 | 37008 | - |
4 * 37008, MALDI, gel filtration | Bacillus subtilis |
3.5.1.11 | 37008 | - |
4 * 37008, mass spectrometry | Bacillus subtilis |
3.5.1.11 | 148000 | - |
gel filtration | Bacillus subtilis |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.5.1.11 | Bacillus subtilis | Q2HPP6 | - |
- |
3.5.1.11 | Bacillus subtilis | Q2HPP6 | gene yxeI | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.5.1.11 | hydrophobic interaction chromatography | Bacillus subtilis |
3.5.1.11 | recombinant enzyme from Escherichia coli strain BL21(DE3) by hydrophobic interaction chrmatography and ultrafiltration | Bacillus subtilis |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.5.1.11 | 4.8 | - |
substrate penicillin V, pH 6.6, 40°C | Bacillus subtilis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.1.11 | 2-nitro-5-(phenoxyacetamido)-benzoic acid + H2O | - |
Bacillus subtilis | ? | - |
? | |
3.5.1.11 | 2-nitro-5-(phenoxyacetamido)-benzoic acid + H2O | - |
Bacillus subtilis | 5-amino-2-nitrobenzoic acid + phenoxyacetate | - |
? | |
3.5.1.11 | additional information | substrate specificity, overview. No activity with ampicillin, amoxicillin, or cephalosporin. Penicillin G is a poor substrate | Bacillus subtilis | ? | - |
? | |
3.5.1.11 | penicillin V + H2O | penicillin G: negligible activity, ampicillin or amoxicillin: no activity | Bacillus subtilis | 6-aminopenicillanic acid + phenoxyacetic acid | - |
? | |
3.5.1.11 | penicillin V + H2O | - |
Bacillus subtilis | phenoxyacetate + 6-aminopenicillinate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.5.1.11 | homotetramer | 4 * 37008, MALDI, gel filtration | Bacillus subtilis |
3.5.1.11 | homotetramer | 4 * 37008, mass spectrometry | Bacillus subtilis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.5.1.11 | penicillin acylase | - |
Bacillus subtilis |
3.5.1.11 | penicillin V acylase | - |
Bacillus subtilis |
3.5.1.11 | YxeI | - |
Bacillus subtilis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.5.1.11 | 40 | - |
assay at | Bacillus subtilis |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.5.1.11 | 30 | 70 | - |
Bacillus subtilis |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.5.1.11 | 40 | - |
after 4 h at 40°C 80% residual activity, after 4 h at 50°C 40% residual activity, after 4 h at 55°C 20% residual activity, at 60°C rapidly inactivated | Bacillus subtilis |
3.5.1.11 | 50 | - |
purified recombinant enzyme, pH 6.6, 15 min, completely stable up to | Bacillus subtilis |
3.5.1.11 | 55 | - |
purified recombinant enzyme, pH 6.6, 15 min, 80% activity remaining | Bacillus subtilis |
3.5.1.11 | 60 | - |
purified recombinant enzyme, pH 6.6, 15 min, inactivation | Bacillus subtilis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.5.1.11 | 6.6 | - |
assay at | Bacillus subtilis |
3.5.1.11 | 6.6 | 7.4 | - |
Bacillus subtilis |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
3.5.1.11 | 4 | 10 | activity range | Bacillus subtilis |
3.5.1.11 | 5.5 | 9 | - |
Bacillus subtilis |
EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|---|
3.5.1.11 | 5 | - |
purified recombinant enzyme, 4 h at room temperature, over 50% activity remaning | Bacillus subtilis |
3.5.1.11 | 5 | 12 | 10 min at 40°C, more than 50% of the activity is retained | Bacillus subtilis |
3.5.1.11 | 6 | 8 | purified recombinant enzyme, 4 h at room temperature, completely stable at | Bacillus subtilis |
3.5.1.11 | 10 | - |
purified recombinant enzyme, 4 h at room temperature, over 50% activity remaning | Bacillus subtilis |
EC Number | Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|---|
3.5.1.11 | Bacillus subtilis | isoelectric focusing | - |
5.3 |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.5.1.11 | evolution | the enzyme belongs to the N-terminal nucleophile (Ntn) hydrolase superfamily of proteins, which is characterized by a distinct alphabetabetaalpha fold (Ntn fold). Based on their substrate specificity, they are classified into penicillin V acylases (PVA), penicillin G acylases (PGA) and ampicillin acylases, which preferentially cleave penicillin V (PenV), penicillin G (PenG) and ampicillin, respectively | Bacillus subtilis |