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Literature summary extracted from
- Switch of substrate specificity of hyperthermophilic acylaminoacyl peptidase by combination of protein and solvent engineering (2011), Protein Cell, 2, 497-506.
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.1.1.1 | F488G/R526V/T560W | 1.55fold increase in activity with 4-nitrophenyl dodecanoate compared to activity of mutant R526V/T560W | Aeropyrum pernix |
| 3.1.1.1 | additional information | the esterase activity of the mutant R526V (this mutation transforms a promiscuous acylaminoacyl peptidase into a specific carboxylesterase) towards substrates with long acyl chains is enhanced by protein engineering and solvent optimization. The substrate preference of the enzyme can be further changed from 4-nitrophenyl octanoate to 4-nitrophenyl dodecanoate by protein and solvent engineering | Aeropyrum pernix |
| 3.1.1.1 | R526V | mutant enzyme with high esterase activity, extreme thermal stability, and high tolerance to organic solvents | Aeropyrum pernix |
| 3.1.1.1 | R526V/T560W | 1.5fold increase in activity with 4-nitrophenyl dodecanoate compared to activity of mutant R526V | Aeropyrum pernix |
| 3.1.1.1 | W474V/F488G/R526V/T560W | the mutant enzyme has 7fold higher catalytic efficiency (kcat/Km) for 4-nitrophenyl dodecanoate than the mutant enzyme R526V | Aeropyrum pernix |
| 3.1.1.1 | W474V/R526V/T560W | 3.11fold increase in activity with 4-nitrophenyl dodecanoate compared to activity of mutant R526V/T560W | Aeropyrum pernix |
| 3.4.19.1 | F488G/R526V/T560W | 1.55fold increase in activity with 4-nitrophenyl laurate compared to activity of mutant R526V/T560W | Aeropyrum pernix |
| 3.4.19.1 | additional information | the esterase activity of the mutant R526V (this mutation transforms a promiscuous acylaminoacyl peptidase into a specific carboxylesterase) towards substrates with long acyl chains is enhanced by protein engineering and solvent optimization. The substrate preference of the enzyme can be further changed from 4-nitrophenyl octanoate to 4-nitrophenyl dodecanoate by protein and solvent engineering | Aeropyrum pernix |
| 3.4.19.1 | R526V | mutant enzyme with high esterase activity, extreme thermal stability, and high tolerance to organic solvents | Aeropyrum pernix |
| 3.4.19.1 | R526V/T560W | 1.5fold increase in activity with 4-nitrophenyl dodecanoate compared to activity of mutant R526V | Aeropyrum pernix |
| 3.4.19.1 | W474V/F488G/R526V/T560W | the mutant enzyme has 7fold higher catalytic efficiency (kcat/Km) for 4-nitrophenyl dodecanoate than the mutant enzyme R526V | Aeropyrum pernix |
| 3.4.19.1 | W474V/R526V/T560W | 3.11fold increase in activity with 4-nitrophenyl laurate compared to activity of mutant R526V/T560W | Aeropyrum pernix |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.1.1 | 0.00075 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme W474Q/R526V/T560W | Aeropyrum pernix |  |
| 3.1.1.1 | 0.00076 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme F488Y/R526V/T560W | Aeropyrum pernix | |
| 3.1.1.1 | 0.00101 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme F488W/R526V/T560W | Aeropyrum pernix | |
| 3.1.1.1 | 0.00122 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme R526V/T560W | Aeropyrum pernix | |
| 3.1.1.1 | 0.00183 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme W474A/R526V/T560W | Aeropyrum pernix | |
| 3.1.1.1 | 0.00234 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme W474V/F488G/R526V/T560W | Aeropyrum pernix | |
| 3.1.1.1 | 0.00243 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme W474V/R526V/T560W | Aeropyrum pernix | |
| 3.1.1.1 | 0.00388 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme F488P/R526V/T560W | Aeropyrum pernix | |
| 3.1.1.1 | 0.00579 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme F488S/R526V/T560W | Aeropyrum pernix | |
| 3.1.1.1 | 0.00737 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme F488A/R526V/T560W | Aeropyrum pernix | |
| 3.1.1.1 | 0.00834 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme F488G/R526V/T560W | Aeropyrum pernix | |
| 3.1.1.1 | 0.00862 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, wild-type enzyme | Aeropyrum pernix | |
| 3.1.1.1 | 0.0118 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme R526V | Aeropyrum pernix | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.1.1 | Aeropyrum pernix | Q9YBQ2 | - |
- |
| 3.1.1.1 | Aeropyrum pernix DSM 11879 | Q9YBQ2 | - |
- |
| 3.4.19.1 | Aeropyrum pernix | Q9YBQ2 | - |
- |
| 3.4.19.1 | Aeropyrum pernix DSM 11879 | Q9YBQ2 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.1.1 | 4-nitrophenyl dodecanoate + H2O | switch of substrate specificity of hyperthermophilic promiscuous acylaminoacyl peptidase by combination of protein and solvent engineering into a specific carboxylesterase | Aeropyrum pernix | 4-nitrophenol + dodecanoate | - |
? | |
| 3.1.1.1 | 4-nitrophenyl dodecanoate + H2O | switch of substrate specificity of hyperthermophilic promiscuous acylaminoacyl peptidase by combination of protein and solvent engineering into a specific carboxylesterase | Aeropyrum pernix DSM 11879 | 4-nitrophenol + dodecanoate | - |
? | |
| 3.4.19.1 | N-acetyl-Leu-4-nitroanilide + H2O | switch of substrate specificity of hyperthermophilic promiscuous acylaminoacyl peptidase by combination of protein and solvent engineering into a specific carboxylesterase | Aeropyrum pernix | N-acetyl-L-Leu + 4-nitroaniline | - |
? | |
| 3.4.19.1 | N-acetyl-Leu-4-nitroanilide + H2O | switch of substrate specificity of hyperthermophilic promiscuous acylaminoacyl peptidase by combination of protein and solvent engineering into a specific carboxylesterase | Aeropyrum pernix DSM 11879 | N-acetyl-L-Leu + 4-nitroaniline | - |
? | |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.1.1 | 1.35 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, wild-type enzyme | Aeropyrum pernix | |
| 3.1.1.1 | 1.73 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme F488W/R526V/T560W | Aeropyrum pernix | |
| 3.1.1.1 | 2.05 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme F488Y/R526V/T560W | Aeropyrum pernix | |
| 3.1.1.1 | 5.29 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme W474Q/R526V/T560W | Aeropyrum pernix | |
| 3.1.1.1 | 5.47 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme R526V | Aeropyrum pernix | |
| 3.1.1.1 | 7.96 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme R526V/T560W | Aeropyrum pernix | |
| 3.1.1.1 | 8.17 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme F488P/R526V/T560W | Aeropyrum pernix | |
| 3.1.1.1 | 10.45 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme F488S/R526V/T560W | Aeropyrum pernix | |
| 3.1.1.1 | 12.08 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme F488A/R526V/T560W | Aeropyrum pernix | |
| 3.1.1.1 | 12.61 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme W474A/R526V/T560W | Aeropyrum pernix | |
| 3.1.1.1 | 17.17 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme F488G/R526V/T560W | Aeropyrum pernix | |
| 3.1.1.1 | 23.5 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme W474V/R526V/T560W | Aeropyrum pernix | |
| 3.1.1.1 | 26.25 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme W474V/F488G/R526V/T560W | Aeropyrum pernix | |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.1.1 | 157.2 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, wild-type enzyme | Aeropyrum pernix | |
| 3.1.1.1 | 462.5 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme R526V | Aeropyrum pernix | |
| 3.1.1.1 | 1638 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme F488A/R526V/T560W | Aeropyrum pernix | |
| 3.1.1.1 | 1712 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme F488W/R526V/T560W | Aeropyrum pernix | |
| 3.1.1.1 | 1804 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme F488S/R526V/T560W | Aeropyrum pernix | |
| 3.1.1.1 | 2059 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme F488G/R526V/T560W | Aeropyrum pernix | |
| 3.1.1.1 | 2107 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme F488P/R526V/T560W | Aeropyrum pernix | |
| 3.1.1.1 | 2703 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme F488Y/R526V/T560W | Aeropyrum pernix | |
| 3.1.1.1 | 6528 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme R526V/T560W | Aeropyrum pernix | |
| 3.1.1.1 | 6876 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme W474A/R526V/T560W | Aeropyrum pernix | |
| 3.1.1.1 | 7018 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme W474Q/R526V/T560W | Aeropyrum pernix | |
| 3.1.1.1 | 9662 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme W474V/R526V/T560W | Aeropyrum pernix | |
| 3.1.1.1 | 11220 | - |
4-nitrophenyl dodecanoate | pH 8.0, 60°C, mutant enzyme W474V/F488G/R526V/T560W | Aeropyrum pernix | |
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