Protein Variants | Comment | Organism |
---|---|---|
F146A | mutation in alpha-subunit. 99% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
F146C | mutation in alpha-subunit. 241% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
F146D | mutation in alpha-subunit. No ampicillin synthesis activity | Escherichia coli |
F146E | mutation in alpha-subunit. 13% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
F146G | mutation in alpha-subunit. 61% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
F146H | mutation in alpha-subunit. 174% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
F146I | mutation in alpha-subunit. 135% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
F146K | mutation in alpha-subunit. 120% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
F146L | mutation in alpha-subunit. 169% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
F146M | mutation in alpha-subunit. 85% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
F146N | mutation in alpha-subunit. 151% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
F146P | mutation in alpha-subunit. 112% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
F146Q | mutation in alpha-subunit. 114% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
F146R | mutation in alpha-subunit. 3% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
F146S | mutation in alpha-subunit. 238% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
F146T | mutation in alpha-subunit. 376% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
F146V | mutation in alpha-subunit. 153% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
F146W | mutation in alpha-subunit. 10% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
F146Y | mutation in alpha-subunit. No ampicillin synthesis activity | Escherichia coli |
R145A | mutation in alpha-subunit. 154% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
R145C | mutation in alpha-subunit. 169% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
R145D | mutation in alpha-subunit. 15% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
R145E | mutation in alpha-subunit. 6% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
R145F | mutation in alpha-subunit. 131% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
R145G | mutation in alpha-subunit. 256% of ampicillin synthesis activity compared to wild-type. Due to increased tendency of the acyl-enzyme intermediate to react with beta-lactam nucleophile instead of water, the mutant demonstrates an enhanced synthetic yield over wild-type penicillin acylase at high substrate concentrations. This is accompanied by an increased conversion of 6-aminopenicillanic acid to ampicillin as well as a decreased undesirable hydrolysis of the acyl donor | Escherichia coli |
R145H | mutation in alpha-subunit. 78% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
R145I | mutation in alpha-subunit. 120% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
R145K | mutation in alpha-subunit. 145% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
R145L | mutation in alpha-subunit. 237% of ampicillin synthesis activity compared to wild-type. Due to increased tendency of the acyl-enzyme intermediate to react with beta-lactam nucleophile instead of water, the mutant demonstrates an enhanced synthetic yield over wild-type penicillin acylase at high substrate concentrations. This is accompanied by an increased conversion of 6-aminopenicillanic acid to ampicillin as well as a decreased undesirable hydrolysis of the acyl donor | Escherichia coli |
R145M | mutation in alpha-subunit. 129% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
R145N | mutation in alpha-subunit. 173% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
R145P | mutation in alpha-subunit. 137% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
R145Q | mutation in alpha-subunit. 158% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
R145S | mutation in alpha-subunit. 192% of ampicillin synthesis activity compared to wild-type. Due to increased tendency of the acyl-enzyme intermediate to react with beta-lactam nucleophile instead of water, the mutant demonstrates an enhanced synthetic yield over wild-type penicillin acylase at high substrate concentrations. This is accompanied by an increased conversion of 6-aminopenicillanic acid to ampicillin as well as a decreased undesirable hydrolysis of the acyl donor | Escherichia coli |
R145T | mutation in alpha-subunit. 127% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
R145V | mutation in alpha-subunit. 127% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
R145W | mutation in alpha-subunit. 103% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
R145Y | mutation in alpha-subunit. 37% of ampicillin synthesis activity compared to wild-type | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.9 | - |
ampicillin | mutant alphaR145L | Escherichia coli | |
2 | 3 | D-phenylglycine amide | mutant alphaR145G | Escherichia coli | |
3.6 | - |
ampicillin | wild-type enzyme | Escherichia coli | |
4.6 | - |
ampicillin | mutant alphaR145S | Escherichia coli | |
5.2 | - |
ampicillin | mutant alphaR145G | Escherichia coli | |
9.1 | - |
D-phenylglycine amide | mutant alphaR145L | Escherichia coli | |
13 | - |
D-phenylglycine amide | mutant alphaR145S | Escherichia coli | |
27 | - |
D-phenylglycine amide | wild-type enzyme | Escherichia coli |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
periplasm | - |
Escherichia coli | - |
- |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-phenylglycine amide + 6-aminopenicillanic acid | - |
Escherichia coli | ampicillin + NH3 | - |
r | |
D-phenylglycine amide + H2O | - |
Escherichia coli | D-phenylglycine + NH3 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
penicillin acylase | - |
Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2.7 | - |
D-phenylglycine amide | mutant alphaR145S | Escherichia coli | |
3 | 6 | D-phenylglycine amide | wild-type enzyme | Escherichia coli | |
3.4 | - |
D-phenylglycine amide | mutant alphaR145G | Escherichia coli | |
6.8 | - |
D-phenylglycine amide | mutant alphaR145L | Escherichia coli | |
14 | - |
ampicillin | mutant alphaR145S | Escherichia coli | |
20 | - |
ampicillin | mutant alphaR145L | Escherichia coli | |
23 | - |
ampicillin | mutant alphaR145G | Escherichia coli | |
37 | - |
ampicillin | wild-type enzyme | Escherichia coli |