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Literature summary for 3.2.1.8 extracted from
- Computational design-based molecular engineering of the glycosyl hydrolase family 11 B. subtilis XynA endoxylanase improves its acid stability (2009), Protein Eng. Des. Sel., 22, 587-596.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene xynA, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Bacillus subtilis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| G23R | construction of a XynA mutant with increased pH stability, Computational design-based molecular engineering, overview | Bacillus subtilis |
| Q175K | construction of a XynA mutant with increased pH stability, Computational design-based molecular engineering, overview | Bacillus subtilis |
| T10H | construction of a XynA mutant with increased pH stability, Computational design-based molecular engineering, overview | Bacillus subtilis |
| W9H | construction of a XynA mutant with increased pH stability, Computational design-based molecular engineering, overview | Bacillus subtilis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| beta-1,4-xylan + H2O | Bacillus subtilis | - |
? | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | P18429 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Bacillus subtilis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| beta-1,4-xylan + H2O | - |
Bacillus subtilis | ? | - |
? | |
| beta-1,4-xylan + H2O | from birchwood | Bacillus subtilis | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| endo-beta-1,4-xylanase | - |
Bacillus subtilis |
| endoxylanase | - |
Bacillus subtilis |
| More | the enzyme belongs to the glycosyl hydrolase family 11, GH11 | Bacillus subtilis |
| XynA | - |
Bacillus subtilis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
assay at | Bacillus subtilis |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 55 | activity range, inactive at 60°C, temperature profile of recombinant His-tagged wild-type and mutant enzymes, overview | Bacillus subtilis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | - |
recombinant His-tagged wild-type enzyme | Bacillus subtilis |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 11 | activity range, pH dependency of recombinant His-tagged wild-type and mutant enzymes, overview | Bacillus subtilis |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
molecular mechanisms governing the pH-dependent stability of GH11 proteins, overview | Bacillus subtilis |
| 3 | - |
30-70% remaining activity for the enzyme mutants, 23% for the wild-type | Bacillus subtilis |
| 4 | - |
75-95% remaining activity for the enzyme mutants, 57% for the wild-type | Bacillus subtilis |
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