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Literature summary for 3.2.1.151 extracted from
- Substrate recognition and hydrolysis by a fungal xyloglucan-specific family 12 hydrolase (2009), Carbohydr. Res., 344, 1175-1179.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.54 | - |
xyloglucan | pH 5.0, 50°C, substrate from pea seed | Aspergillus niger |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| xyloglucan + H2O | Aspergillus niger | - |
xyloglucan oligosaccharides | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus niger | - |
- |
- |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 113 | - |
substrate pea seed xyloglucan | Aspergillus niger |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | modelling of substrate binding, overview. Substrate fucosylation does not affect the specific activity of this enzyme. AnXEG12A prefers xylogluco-oligosaccharides containing more than six glucose units, and with xylose substitution at the -3 and +1 subsites, branching structures do not significantly affect the hydrolytic efficiency of the enzyme, overview | Aspergillus niger | ? | - |
? | |
| xyloglucan + H2O | - |
Aspergillus niger | xyloglucan oligosaccharides | - |
? | |
| xyloglucan + H2O | pea seed xyloglucan | Aspergillus niger | xyloglucan oligosaccharides | - |
? | |
| xyloglucan oligosaccharide + H2O | diverse substrates, substrate specificity, overview | Aspergillus niger | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | AnXEG12A structure homology modelling, overview. Catalytic residues are D100, E115, and E201, predicted substrate binding residues are W22, and W119, and residues that are predicted to influence substrate specificity in GH12 are xyloglucanases W7, V94, and G127. The SST insertion sequence is loacted at residues 130-132 | Aspergillus niger |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GH12 xyloglucanase | - |
Aspergillus niger |
| XEG12A | - |
Aspergillus niger |
| xyloglucan-specific family 12 hydrolase | - |
Aspergillus niger |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
assay at | Aspergillus niger |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 49 | - |
xyloglucan | pH 5.0, 50°C, substrate from pea seed | Aspergillus niger | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | - |
assay at | Aspergillus niger |
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Release 2023.1 (January 2023)
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