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Literature summary for 3.2.1.177 extracted from
- Structural elements to convert Escherichia coli alpha-xylosidase (YicI) into alpha-glucosidase (2006), FEBS Lett., 580, 2707-2711.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C307I | isoprimeverose-hydrolyzing activity of the mutant enzyme is reduced 400fold compared to wild-type enzyme. alpha-Glucosidase activity is not detected | Escherichia coli |
| C307I/F308D | alpha-xylosidase activity of wild-type enzyme is converted into alpha-glucosidase activity. Mutant shows 140fold higher hydrolytic activity against p-nitrophenyl alpha-glucopyranoside than wild-type YicI. The mutant is able to hydrolyze nigerose [alpha-D-Glcp-(1->3)-D-Glcp] and kojibiose [alpha-D-Glcp-(1->2)-D-Glcp], which are not hydrolyzed by the wild-type enzyme. Isoprimeverose-hydrolyzing activity of the L1Chi mutant is decreased by about 3700fold, and that of C307I/F308D is diminished to below the limits of detection. alpha-Glucosidase activity with 4-nitrophenyl alpha-D-glucoside is increased 132fold compared to wild-type activity | Escherichia coli |
| F277Y | isoprimeverose-hydrolyzing activity of the mutant enzyme is reduced 20fold compared to wild-type enzyme. alpha-Glucosidase activity is not detected (alpha-glucosidase activity of the wild-type enzyme is 96244fold lower than specific activity with isoprimeverose) | Escherichia coli |
| K414W | isoprimeverose-hydrolyzing activity of the mutant enzyme is reduced 12000fold compared to wild-type enzyme. alpha-Glucosidase activity is not detected | Escherichia coli |
| W345I | isoprimeverose-hydrolyzing activity of the mutant enzyme is reduced 16000fold compared to wild-type enzyme. alpha-Glucosidase activity is not detected | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P31434 | - |
- |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.00126 | - |
isoprimeverose, pH 7.0, 37°C, mutant enzyme C307I | Escherichia coli |
| 0.00545 | - |
isoprimeverose, pH 7.0, 37°C, mutant enzyme K414W | Escherichia coli |
| 0.0187 | - |
4-nitrophenyl-alpha-D-xyloside, pH 7.0, 37°C, wild-type enzyme | Escherichia coli |
| 0.0192 | - |
isoprimeverose, pH 7.0, 37°C, mutant enzyme W345I | Escherichia coli |
| 0.0495 | - |
isoprimeverose, pH 7.0, 37°C, mutant enzyme F277Y | Escherichia coli |
| 20.5 | - |
isoprimeverose, pH 7.0, 37°C, wild-type enzyme | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-nitrophenyl-alpha-D-xyloside + H2O | - |
Escherichia coli | 4-nitrophenol + alpha-D-xylose | - |
? |  |
| isoprimeverose + H2O | - |
Escherichia coli | alpha-D-xylose + beta-D-glucose | - |
? | |
| additional information | specific activity of wild-type enzyme with 4-nitrophenyl-alpha-D-glucoside is 96244fold lower compared to specific activity with isoprimeverose | Escherichia coli | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| YicI | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Escherichia coli |
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