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Literature summary for 3.1.1.72 extracted from
- Biochemical characterization of recombinant acetyl xylan esterase from Aspergillus awamori expressed in Pichia pastoris: mutational analysis of catalytic residues (2005), Biochim. Biophys. Acta, 1749, 7-13.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Pichia pastoris by fusing to the Saccharomyces cerevisiae alpha-factor secretion signal peptide | Aspergillus awamori |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D168A | kcat/Km for alpha-naphthylacetate is 1.7fold lower than the wild-type value | Aspergillus awamori |
| D202A | inactive mutant enzyme | Aspergillus awamori |
| D202A | mutant shows greater synthetic activity of ethyl n-hexanoate as compared with the wild-type. kcat/Km for alpha-naphthylacetate is 1.5fold higher than the wild-type value | Aspergillus awamori |
| S119A | inactive mutant enzyme | Aspergillus awamori |
| S146A | mutant enzyme shows lower specific activity towards the C2 substrate and higher thermal stability than wild-type enzyme. the lower activity is due to a combination of increased Km and decreased kcat. The catalytic efficiency of the mutant is 41% lower than that of wild-type enzyme | Aspergillus awamori |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.43 | - |
(25R)-3beta-hydroxycholest-5-en-27-oate | substrate: alpha-naphthylacetate, wild-type enzyme | Aspergillus awamori |  |
| 1.5 | 2 | (25R)-3beta-hydroxycholest-5-en-27-oate | substrate: alpha-naphthylacetate, mutant enzyme D168A | Aspergillus awamori | |
| 1.8 | - |
(25R)-3beta-hydroxycholest-5-en-27-oate | substrate: alpha-naphthylacetate, mutant enzyme S146A | Aspergillus awamori | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus awamori | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| culture medium | recombinant enzyme expressed by Pichia pastoris | Aspergillus awamori | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 3.9 | - |
substrate: alpha-naphthylpropionate, mutant enzyme S146A | Aspergillus awamori |
| 5 | - |
substrate: alpha-naphthylpropionate, wild-type D168A | Aspergillus awamori |
| 6.6 | - |
substrate: alpha-naphthylpropionate, wild-type enzyme | Aspergillus awamori |
| 14.7 | - |
substrate: alpha-naphthylacetate, mutant enzyme S146A | Aspergillus awamori |
| 19 | - |
substrate: alpha-naphthylacetate, mutant enzyme D168A | Aspergillus awamori |
| 19.7 | - |
substrate: alpha-naphthylacetate, wild-type enzyme | Aspergillus awamori |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (25R)-3beta-hydroxycholest-5-en-27-oate + H2O | - |
Aspergillus awamori | ? | - |
? | |
| 1-naphthyl acetate + H2O | - |
Aspergillus awamori | 1-naphthol + acetate | - |
? | |
| alpha-naphthyl propionate + H2O | - |
Aspergillus awamori | 1-naphthol + propionate | - |
? | |
| additional information | no activity towards acyl-chain substrates containing four or more carbon atoms, methyl esters of ferulic, caffeic or sinapic acids | Aspergillus awamori | ? | - |
? | |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.53 | - |
1-naphthyl acetate | substrate: alpha-naphthylacetate, wild-type enzyme | Aspergillus awamori | |
| 60.5 | - |
1-naphthyl acetate | substrate: alpha-naphthylacetate, mutant enzyme S146A | Aspergillus awamori | |
| 81.9 | - |
1-naphthyl acetate | substrate: alpha-naphthylacetate, wild-type enzyme | Aspergillus awamori | |
| 131.3 | - |
1-naphthyl acetate | substrate: alpha-naphthylacetate, mutant enzyme D168A | Aspergillus awamori | |
| 411 | - |
1-naphthyl acetate | substrate: alpha-naphthylacetate, mutant enzyme D168A | Aspergillus awamori | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 7 | alpha-naphthylacetate, wild-type enzyme and mutant enzymes S146A and D168A | Aspergillus awamori |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 8 | pH 5: wild-type enzyme shows about 55% of maximal activity, mutant enzymes S146A and D168A show about 35% of maximal activity, pH 8.0: wild-type enzyme shows about 40% of maximal activity, mutant enzymes S146A and D168A show about 75% of maximal activity | Aspergillus awamori |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 5 | - |
37°C, 1 h, wild-type enzyme loses about 30% of initial activity, mutant enzyme S146A loses about 25% of initial activity, mutant enzyme D168A loses about 35% of initial activity | Aspergillus awamori |
| 7 | 9 | 37°C, 1 h, wild-type enzyme and mutant enzymes S146A and D168A are stable | Aspergillus awamori |
| 10 | - |
37°C, 1 h, wild-type enzyme loses about 20% of initial activity, mutant enzyme S146A loses about 65% of initial activity, mutant enzyme D168A loses about 40% of initial activity | Aspergillus awamori |
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