Application | Comment | Organism |
---|---|---|
degradation | the enzyme has potential for promoting hemicellulose degradation and other industrial applications | Thermobifida halotolerans |
Cloned (Comment) | Organism |
---|---|
overexpression in Escherichia coli | Thermobifida halotolerans |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.42 | - |
p-nitrophenyl alpha-L-arabinoside | 55°C, pH 7.0 | Thermobifida halotolerans | |
0.78 | - |
4-nitrophenyl beta-D-xyloside | 55°C, pH 7.0 | Thermobifida halotolerans |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
additional information | activity is not affected by K+, Mg2+, Fe2+, Fe3+, Ca2+, Co2+, Ba2+ | Thermobifida halotolerans | |
NaCl | the enzyme displays high catalytic activity (60%) in presence of 5-35% NaCl (w/v) | Thermobifida halotolerans |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
61500 | - |
- |
Thermobifida halotolerans |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermobifida halotolerans | A0A399G7U0 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Thermobifida halotolerans |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-nitrophenyl beta-D-xyloside + H2O | the enzyme displays high catalytic activity (60%) in presence of 5-35% NaCl (w/v) or 1-20% ionic liquid (w/v) or 1-50 mM xylose | Thermobifida halotolerans | 4-nitrophenol + beta-D-xylose | - |
? | |
additional information | no activity is found for beechwood xylan and cellobiose | Thermobifida halotolerans | ? | - |
? | |
p-nitrophenyl alpha-L-arabinoside + H2O | about 6% of the activity with 4-nitrophenyl beta-D-xylopyranoside | Thermobifida halotolerans | 4-nitrophenol + alpha-L-arabinose | - |
? | |
xylobiose + H2O | 25% of the activity with 4-nitrophenyl beta-D-xylopyranoside | Thermobifida halotolerans | 2 beta-D-xylose | - |
? | |
xylotetraose + H2O | 21% of the activity with 4-nitrophenyl beta-D-xylopyranoside | Thermobifida halotolerans | xylotriose + beta-D-xylose | - |
? | |
xylotriose + 2 H2O | about 12.1% of the activity with 4-nitrophenyl beta-D-xylopyranoside | Thermobifida halotolerans | 3 D-xylose | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | 1 * 61500 | Thermobifida halotolerans |
Synonyms | Comment | Organism |
---|---|---|
Thxyl43A | - |
Thermobifida halotolerans |
xyl43A | - |
Thermobifida halotolerans |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
55 | - |
- |
Thermobifida halotolerans |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
15 | 60 | 15°C: 27 % of maximal activity, 25°C: 40% of maximal activity, 60°C: 60% of maximal activity | Thermobifida halotolerans |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | - |
the enzyme retains more than 80% activity after incubation for 66 h | Thermobifida halotolerans |
50 | - |
the enzyme retains more than 80% activity after incubation for 66 h | Thermobifida halotolerans |
55 | - |
t1/2: 29.7 h. The enzyme retains 47% of its activity after 30 h incubation at 55°C, the enzyme retains 90% of its activity after 24 h incubation at 55°C | Thermobifida halotolerans |
60 | - |
t1/2: 4.8 h | Thermobifida halotolerans |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
3.8 | - |
p-nitrophenyl alpha-L-arabinoside | 55°C, pH 7.0 | Thermobifida halotolerans | |
50 | - |
4-nitrophenyl beta-D-xyloside | 55°C, pH 7.0 | Thermobifida halotolerans |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
- |
Thermobifida halotolerans |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
4 | 10.6 | the enzyme is notably active at pH 4-6 and pH 9-10. At pH 8.0 about 65% and 90% relative activity is detected in citrate buffer and borate buffer respectively. At pH 8.6 and 9.0 less than 65% relative activity is observed in borate buffer, while more than 85% is found in Gly-NaOH buffer. More than 60% relative activity is noted at pH 10.6 | Thermobifida halotolerans |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
4 | 12 | the enzyme retains more than 80% residual activity after incubation at pH range of 4.0 to 12.0 for 24 h | Thermobifida halotolerans |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
9 | - |
p-nitrophenyl alpha-L-arabinoside | 55°C, pH 7.0 | Thermobifida halotolerans | |
64.1 | - |
4-nitrophenyl beta-D-xyloside | 55°C, pH 7.0 | Thermobifida halotolerans |