Application | Comment | Organism |
---|---|---|
degradation | Abf51A shows greater synergistic effect in combination with xylanase (2.92fold) on wheat arabinoxylan degradation than other reported enzymes, the amounts of arabinose, xylose, and xylobiose are all increased in comparison to that by the enzymes acting individually | Alicyclobacillus sp. |
Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Alicyclobacillus sp. |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Alicyclobacillus sp. | A0A0P0ISK8 | cf. EC 3.2.1.55 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the enzyme is an arabinofuranose that may also act as xylanosidase. The enzyme additionally releases xylobiose and xylotriose from wheat arabinoxylan and is active on xylooligosaccharides (xylohexaose 1.2/mM/min, xylopentaose 6.9/mM/min, and xylotetraose 19.7/mM/min), however a lower level of activity | Alicyclobacillus sp. | ? | - |
? | |
wheat arabinoxylan + H2O | - |
Alicyclobacillus sp. | xylobiose + xylotriose + ? | - |
? | |
xylohexaose + H2O | - |
Alicyclobacillus sp. | ? | - |
? | |
xylopentaose + H2O | - |
Alicyclobacillus sp. | ? | - |
? | |
xylotetraose + H2O | - |
Alicyclobacillus sp. | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Abf51A | - |
Alicyclobacillus sp. |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
60 | - |
- |
Alicyclobacillus sp. |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
- |
Alicyclobacillus sp. |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.02 | - |
xylohexaose | pH 6.0, 60°C | Alicyclobacillus sp. | |
0.12 | - |
xylopentaose | pH 6.0, 60°C | Alicyclobacillus sp. | |
0.33 | - |
xylotetraose | pH 6.0, 60°C | Alicyclobacillus sp. |