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Literature summary extracted from
- Alteration of substrate specificities of thermophilic alpha/beta hydrolases through domain swapping and domain interface optimization (2012), Acta Biochim. Biophys. Sin., 44, 965-973.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.1.1.1 | expression in Escherichia coli of chimeras of a carboxylesterase (EC 3.1.1.1) from Archaeoglobus fulgidus and an acylpeptide hydrolase (EC 3.4.19.1) from Aeropyrum pernix K1 | Archaeoglobus fulgidus |
| 3.4.19.1 | expression in Escherichia coli of of chimeras of a carboxylesterase (EC 3.1.1.1) from Archaeoglobus fulgidus and an acylpeptide hydrolase (EC 3.4.19.1) from Aeropyrum pernix K1 | Aeropyrum pernix |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.1.1.1 | additional information | construction of chimeras of a carboxylesterase (EC 3.1.1.1) from Archaeoglobus fulgidus and an acylpeptide hydrolase (EC 3.4.19.1) from Aeropyrum pernix K1. Their activities to hydrolyze 4-nitrophenyl esters (pNP) with different acyl chain lengths is explored. The chimeras inherit the thermophilic property of both parents. The substrate-binding domain is the dominant factor on enzyme substrate specificity, and the optimization of the newly formed domain interface is an important guarantee for successful domain swapping of proteins with low-sequence homology | Archaeoglobus fulgidus |
| 3.4.19.1 | additional information | construction of chimeras of a carboxylesterase (EC 3.1.1.1) from Archaeoglobus fulgidus and an acylpeptide hydrolase (EC 3.4.19.1) from Aeropyrum pernix K1. Their activities to hydrolyze 4-nitrophenyl esters (pNP) with different acyl chain lengths is explored. The chimeras inherit the thermophilic property of both parents. The substrate-binding domain is the dominant factor on enzyme substrate specificity, and the optimization of the newly formed domain interface is an important guarantee for successful domain swapping of proteins with low-sequence homology | Aeropyrum pernix |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.1.1 | 0.0327 | - |
4-nitrophenyl butanoate | 80°C, pH 8.0, wild-type enzyme | Archaeoglobus fulgidus |  |
| 3.1.1.1 | 0.0768 | - |
4-nitrophenyl acetate | 80°C, pH 8.0, wild-type enzyme | Archaeoglobus fulgidus | |
| 3.1.1.1 | 0.289 | - |
4-nitrophenyl octanoate | 80°C, pH 8.0, wild-type enzyme | Archaeoglobus fulgidus | |
| 3.1.1.1 | 0.507 | - |
4-nitrophenyl hexadecanoate | 80°C, pH 8.0, wild-type enzyme | Archaeoglobus fulgidus | |
| 3.1.1.1 | 0.651 | - |
4-nitrophenyl decanoate | 80°C, pH 8.0, wild-type enzyme | Archaeoglobus fulgidus | |
| 3.1.1.1 | 0.654 | - |
4-nitrophenyl dodecanoate | 80°C, pH 8.0, wild-type enzyme | Archaeoglobus fulgidus | |
| 3.1.1.1 | 1.054 | - |
4-nitrophenyl tetradecanoate | 80°C, pH 8.0, wild-type enzyme | Archaeoglobus fulgidus | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.1.1 | Archaeoglobus fulgidus | - |
- |
- |
| 3.4.19.1 | Aeropyrum pernix | Q9YBQ2 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.1.1.1 | purification of chimeras of a carboxylesterase (EC 3.1.1.1) from Archaeoglobus fulgidus and an acylpeptide hydrolase (EC 3.4.19.1) from Aeropyrum pernix K1 | Archaeoglobus fulgidus |
| 3.4.19.1 | - |
Aeropyrum pernix |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.1.1 | 4-nitrophenyl acetate + H2O | - |
Archaeoglobus fulgidus | 4-nitrophenol + acetate | - |
? | |
| 3.1.1.1 | 4-nitrophenyl butanoate + H2O | - |
Archaeoglobus fulgidus | 4-nitrophenol + butanoate | - |
? | |
| 3.1.1.1 | 4-nitrophenyl decanoate + H2O | - |
Archaeoglobus fulgidus | 4-nitrophenol + decanoate | - |
? | |
| 3.1.1.1 | 4-nitrophenyl dodecanoate + H2O | - |
Archaeoglobus fulgidus | 4-nitrophenol + dodecanoate | - |
? | |
| 3.1.1.1 | 4-nitrophenyl hexadecanoate + H2O | - |
Archaeoglobus fulgidus | 4-nitrophenol + hexadecanoate | - |
? | |
| 3.1.1.1 | 4-nitrophenyl octanoate + H2O | - |
Archaeoglobus fulgidus | 4-nitrophenol + octanoate | - |
? | |
| 3.1.1.1 | 4-nitrophenyl tetradecanoate + H2O | - |
Archaeoglobus fulgidus | 4-nitrophenol + tetradecanoate | - |
? | |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.1 | 80 | - |
wild-type enzyme | Archaeoglobus fulgidus |
| 3.4.19.1 | 80 | - |
wild-type enzyme | Aeropyrum pernix |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.1 | 60 | 90 | 60°C: about 55% of maximal activity, 90°C: about 85% of maximal activity, wild-type enzyme | Archaeoglobus fulgidus |
| 3.4.19.1 | 60 | 80 | 60°C: about 40% of maximal activity, 80°C: optimum | Aeropyrum pernix |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.1.1 | 5.3 | - |
4-nitrophenyl hexadecanoate | 80°C, pH 8.0, wild-type enzyme | Archaeoglobus fulgidus | |
| 3.1.1.1 | 42.3 | - |
4-nitrophenyl tetradecanoate | 80°C, pH 8.0, wild-type enzyme | Archaeoglobus fulgidus | |
| 3.1.1.1 | 120 | - |
4-nitrophenyl acetate | 80°C, pH 8.0, wild-type enzyme | Archaeoglobus fulgidus | |
| 3.1.1.1 | 128 | - |
4-nitrophenyl dodecanoate | 80°C, pH 8.0, wild-type enzyme | Archaeoglobus fulgidus | |
| 3.1.1.1 | 277 | - |
4-nitrophenyl butanoate | 80°C, pH 8.0, wild-type enzyme | Archaeoglobus fulgidus | |
| 3.1.1.1 | 477 | - |
4-nitrophenyl decanoate | 80°C, pH 8.0, wild-type enzyme | Archaeoglobus fulgidus | |
| 3.1.1.1 | 831 | - |
4-nitrophenyl octanoate | 80°C, pH 8.0, wild-type enzyme | Archaeoglobus fulgidus | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.1 | 7 | 7.5 | wild-type enzyme | Archaeoglobus fulgidus |
| 3.4.19.1 | 8.8 | - |
wild-type enzyme | Aeropyrum pernix |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.1 | 6 | 10.5 | pH 6.0: about 50% of maximal activity, pH 10.5: about 50% of maximal activity, wild-type enzyme | Archaeoglobus fulgidus |
| 3.4.19.1 | 7.5 | 9.5 | pH 7.5: about 50% of maximal activity, pH 9.5: about 65% of maximal activity, wild-type enzyme | 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 | 10 | - |
4-nitrophenyl hexadecanoate | 80°C, pH 8.0, wild-type enzyme | Archaeoglobus fulgidus | |
| 3.1.1.1 | 40 | - |
4-nitrophenyl tetradecanoate | 80°C, pH 8.0, wild-type enzyme | Archaeoglobus fulgidus | |
| 3.1.1.1 | 200 | - |
4-nitrophenyl dodecanoate | 80°C, pH 8.0, wild-type enzyme | Archaeoglobus fulgidus | |
| 3.1.1.1 | 700 | - |
4-nitrophenyl decanoate | 80°C, pH 8.0, wild-type enzyme | Archaeoglobus fulgidus | |
| 3.1.1.1 | 1600 | - |
4-nitrophenyl acetate | 80°C, pH 8.0, wild-type enzyme | Archaeoglobus fulgidus | |
| 3.1.1.1 | 2900 | - |
4-nitrophenyl octanoate | 80°C, pH 8.0, wild-type enzyme | Archaeoglobus fulgidus | |
| 3.1.1.1 | 8500 | - |
4-nitrophenyl butanoate | 80°C, pH 8.0, wild-type enzyme | Archaeoglobus fulgidus | |
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