EC Number | Application | Comment | Organism |
---|---|---|---|
3.5.1.14 | synthesis | because of its thermostability, the enzyme is expected to be useful for the production of L-amino acid derivatives from racemates at temperatures over 90°C | Pyrococcus horikoshii |
EC Number | Cloned (Comment) | Organism |
---|---|---|
3.5.1.14 | - |
Pyrococcus horikoshii |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.5.1.14 | C102A | no hydrolytic activity | Pyrococcus horikoshii |
3.5.1.14 | C102S | Km-values are similar to those of wild-type enzyme | Pyrococcus horikoshii |
3.5.1.14 | E367Q | the kcat-value increases slightly, whereas the Km value does not change for N-acetyl-L-phenylalanine as substrates. Substrate inhibition of aminoacylase activity is also observed. The temperature-dependent activity and pH profile of the activity of E367Q are similar to those of wild-type enzyme | Pyrococcus horikoshii |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.5.1.14 | benzyloxycarbonyl-Gly-Gly-Phe | - |
Pyrococcus horikoshii | |
3.5.1.14 | L-benzylsuccinate | - |
Pyrococcus horikoshii |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.5.1.14 | 4.18 | - |
N-acetyl-L-methionine | pH 7.5, 85°C, wild-type enzyme | Pyrococcus horikoshii | |
3.5.1.14 | 5.2 | - |
N-acetyl-L-phenylalanine | pH 7.5, 85°C, wild-type enzyme | Pyrococcus horikoshii | |
3.5.1.14 | 6.2 | - |
N-acetyl-L-phenylalanine | pH 7.5, 85°C, mutant enzyme C102S | Pyrococcus horikoshii | |
3.5.1.14 | 6.64 | - |
N-acetyl-L-phenylalanine | pH 7.5, 85°C, mutant enzyme E367Q | Pyrococcus horikoshii |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.5.1.14 | Ca2+ | the enzyme contains 1.22 mol of Zn2+ and 0.17 mol of Ca2+ per mol of monomer enzyme protein | Pyrococcus horikoshii | |
3.5.1.14 | Co2+ | when the enzyme is dialyzed against 50 mM EDTA (pH 7.5) for 10 h at 4°C and then against 50 mM sodium phosphate buffer (pH 7.5), the aminoacylase activity is decreased to less than 1.0%. The activity is restored by incubation in 50 mM sodium phosphate buffer (pH 7.5) containing ZnCl2, MnCl2, or CoCl2 at 4°C for 1 h. The restorative effect is dependent on the concentration of the metal ions. 88%, 23%, and 20% of activities are restored by adding 1.0 mM ZnCl2, 1.0 mM MnCl2, and 0.1 mM CoCl2, respectively | Pyrococcus horikoshii | |
3.5.1.14 | Mn2+ | when the enzyme is dialyzed against 50 mM EDTA (pH 7.5) for 10 h at 4°C and then against 50 mM sodium phosphate buffer (pH 7.5), the aminoacylase activity is decreased to less than 1.0%. The activity is restored by incubation in 50 mM sodium phosphate buffer (pH 7.5) containing ZnCl2, MnCl2, or CoCl2 at 4°C for 1 h. The restorative effect is dependent on the concentration of the metal ions. 88%, 23%, and 20% of activities are restored by adding 1.0 mM ZnCl2, 1.0 mM MnCl2, and 0.1 mM CoCl2, respectively | Pyrococcus horikoshii | |
3.5.1.14 | Zn2+ | the enzyme contains 1.22 mol of Zn2+ and 0.17 mol of Ca2+ per mol of monomer enzyme protein. When the enzyme is dialyzed against 50 mM EDTA (pH 7.5) for 10 h at 4°C and then against 50 mM sodium phosphate buffer (pH 7.5), the aminoacylase activity is decreased to less than 1.0%. The activity is restored by incubation in 50 mM sodium phosphate buffer (pH 7.5) containing ZnCl2, MnCl2, or CoCl2 at 4°C for 1 h. The restorative effect is dependent on the concentration of the metal ions. 88%, 23%, and 20% of activities are restored by adding 1.0 mM ZnCl2, 1.0 mM MnCl2, and 0.1 mM CoCl2, respectively | Pyrococcus horikoshii |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.5.1.14 | 43000 | - |
x * 43000, SDS-PAGE | Pyrococcus horikoshii |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.5.1.14 | Pyrococcus horikoshii | O58754 | - |
- |
3.5.1.14 | Pyrococcus horikoshii OT-3 | O58754 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.1.14 | additional information | N-acetyl-D-amino acids are not hydrolyzed | Pyrococcus horikoshii | ? | - |
? | |
3.5.1.14 | additional information | N-acetyl-D-amino acids are not hydrolyzed | Pyrococcus horikoshii OT-3 | ? | - |
? | |
3.5.1.14 | N-acetyl-L-alanine + H2O | - |
Pyrococcus horikoshii | acetate + L-alanine | - |
? | |
3.5.1.14 | N-acetyl-L-methionine + H2O | - |
Pyrococcus horikoshii | acetate + L-methionine | - |
? | |
3.5.1.14 | N-acetyl-L-methionine + H2O | - |
Pyrococcus horikoshii OT-3 | acetate + L-methionine | - |
? | |
3.5.1.14 | N-acetyl-L-phenylalanine + H2O | - |
Pyrococcus horikoshii | acetate + L-phenylalanine | - |
? | |
3.5.1.14 | N-acetyl-L-phenylalanine + H2O | - |
Pyrococcus horikoshii OT-3 | acetate + L-phenylalanine | - |
? | |
3.5.1.14 | N-acetyl-L-tryptophan + H2O | weak activity | Pyrococcus horikoshii | acetate + L-tryptophan | - |
? | |
3.5.1.14 | N-acetyl-L-tryptophan + H2O | weak activity | Pyrococcus horikoshii OT-3 | acetate + L-tryptophan | - |
? | |
3.5.1.14 | N-acetyl-L-tyrosine + H2O | - |
Pyrococcus horikoshii | acetate + L-tyrosine | - |
? | |
3.5.1.14 | N-acetylglycine + H2O | weak activity | Pyrococcus horikoshii | acetate + glycine | - |
? | |
3.5.1.14 | N-acetylglycine + H2O | weak activity | Pyrococcus horikoshii OT-3 | acetate + glycine | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.5.1.14 | ? | x * 43000, SDS-PAGE | Pyrococcus horikoshii |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.5.1.14 | 0.0208 | - |
N-acetyl-L-phenylalanine | pH 7.5, 85°C, mutant enzyme C102S | Pyrococcus horikoshii | |
3.5.1.14 | 34 | - |
N-acetyl-L-phenylalanine | pH 7.5, 85°C, wild-type enzyme | Pyrococcus horikoshii | |
3.5.1.14 | 37.3 | - |
N-acetyl-L-phenylalanine | pH 7.5, 85°C, mutant enzyme E367Q | Pyrococcus horikoshii | |
3.5.1.14 | 45.6 | - |
N-acetyl-L-methionine | pH 7.5, 85°C, wild-type enzyme | Pyrococcus horikoshii |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.5.1.14 | 0.001 | - |
L-benzylsuccinate | pH 7.5, 85°C | Pyrococcus horikoshii | |
3.5.1.14 | 2.93 | - |
benzyloxycarbonyl-Gly-Gly-Phe | pH 7.5, 85°C | Pyrococcus horikoshii |