Protein Variants | Comment | Organism |
---|---|---|
F488G/R526V/T560W | 1.55fold increase in activity with 4-nitrophenyl laurate compared to activity of mutant R526V/T560W | Aeropyrum pernix |
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 |
R526V | mutant enzyme with high esterase activity, extreme thermal stability, and high tolerance to organic solvents | Aeropyrum pernix |
R526V/T560W | 1.5fold increase in activity with 4-nitrophenyl dodecanoate compared to activity of mutant R526V | Aeropyrum pernix |
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 |
W474V/R526V/T560W | 3.11fold increase in activity with 4-nitrophenyl laurate compared to activity of mutant R526V/T560W | Aeropyrum pernix |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aeropyrum pernix | Q9YBQ2 | - |
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Aeropyrum pernix DSM 11879 | Q9YBQ2 | - |
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Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | - |
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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 | - |
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