Any feedback?
Literature summary for 3.2.1.8 extracted from
- A novel trifunctional, family GH10 enzyme from Acidothermus cellulolyticus 11B, exhibiting endo-xylanase, arabinofuranosidase and acetyl xylan esterase activities (2018), Extremophiles, 22, 109-119 .
Application
| Application | Comment | Organism |
|---|---|---|
| food industry | the enzyme is important for industrial applications such as pretreatment of poultry cereals, bio-bleaching of wood pulp and degradation of plant biomass | Acidothermus cellulolyticus |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli BL21 Codon Plus (DE3) RIPL cells | Acidothermus cellulolyticus |
| gene xyn10B, sequence comparisons, recombinant expression in Escherichia coli strain BL21 CodonPlus (RIPL) | Acidothermus cellulolyticus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | about 90% residual activity at 1 mM | Acidothermus cellulolyticus |  |
| EDTA | about 78% residual activity at 50 mM | Acidothermus cellulolyticus | |
| Mn2+ | 40% inhibition at 1 mM; about 55% residual activity at 1 mM | Acidothermus cellulolyticus | |
| additional information | no inhibition by 1-10 mM EDTA | Acidothermus cellulolyticus | |
| Ni2+ | about 95% residual activity at 1 mM | Acidothermus cellulolyticus | |
| SDS | 20% inhibition at 0.5%; about 78% residual activity at 0.5% (w/v) | Acidothermus cellulolyticus | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Km value for Xyn10B with 0.5% beechwood xylan is 2.5 mg/ml | Acidothermus cellulolyticus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | slight increase of activity at 1 mM | Acidothermus cellulolyticus | |
| additional information | not influenced by Cu2+ | Acidothermus cellulolyticus | |
| additional information | poor effects by 1 mM of Ni2+, Ca2+, Mg2+, Fe3+, and Cu2+ | Acidothermus cellulolyticus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Acidothermus cellulolyticus | A0LR95 | - |
- |
| Acidothermus cellulolyticus 11B | A0LR95 | - |
- |
| Acidothermus cellulolyticus ATCC 43068 | A0LR95 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme Xyn10B 10fold from Escherichia coli strain BL21 CodonPlus (RIPL) to homogeneity by adsorption chromatography on amorphous cellulose resin, dialysis, and ultrafiltration | Acidothermus cellulolyticus |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 1833 | - |
purified recombinant enzyme, pH 6.0, 70°C, substrate beechwood xylan | Acidothermus cellulolyticus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-nitrophenyl acetate + H2O | - |
Acidothermus cellulolyticus | 4-nitrophenol + acetate | - |
? | |
| 4-nitrophenyl acetate + H2O | - |
Acidothermus cellulolyticus 11B | 4-nitrophenol + acetate | - |
? | |
| 4-nitrophenyl acetate + H2O | - |
Acidothermus cellulolyticus ATCC 43068 | 4-nitrophenol + acetate | - |
? | |
| 4-nitrophenyl alpha-L-arabinofuranoside + H2O | - |
Acidothermus cellulolyticus | 4-nitrophenol + alpha-L-arabinofuranose | - |
? | |
| beechwood xylan + H2O | best substrate | Acidothermus cellulolyticus | xylobiose + xylotriose | - |
? | |
| beechwood xylan + H2O | best substrate | Acidothermus cellulolyticus | xylobiose + xylose + ? | - |
? | |
| birchwood xylan + H2O | - |
Acidothermus cellulolyticus | xylobiose + ? | - |
? | |
| birchwood xylan + H2O | - |
Acidothermus cellulolyticus | xylobiose + xylotriose + ? | - |
? | |
| insoluble xylan + H2O | - |
Acidothermus cellulolyticus | ? | - |
? | |
| additional information | no activity with 4-nitrophenyl galactopyranoside, 4-nitrophenyl glucopyranoside, Avicel and carboxymethyl cellulose | Acidothermus cellulolyticus | ? | - |
? | |
| additional information | the purified recombinant enzyme Xyn10B is highly active producing xylobiose and xylose as the major end products, as well as debranching the substrates by removing arabinose and acetyl side chains. Xyn10B is a trifunctional enzyme having endo-xylanase, arabinofuranosidase and acetyl xylan esterase activities, the latter two with p-nitrophenyl arabinofuranoside and p-nitrophenyl acetate as substrates, respectively. No activity with Avicel, carboxymethyl cellulose, p-nitrophenyl galactopyranoside, and p-nitrophenyl glucopyranoside | Acidothermus cellulolyticus | ? | - |
? | |
| additional information | no activity with 4-nitrophenyl galactopyranoside, 4-nitrophenyl glucopyranoside, Avicel and carboxymethyl cellulose | Acidothermus cellulolyticus 11B | ? | - |
? | |
| additional information | the purified recombinant enzyme Xyn10B is highly active producing xylobiose and xylose as the major end products, as well as debranching the substrates by removing arabinose and acetyl side chains. Xyn10B is a trifunctional enzyme having endo-xylanase, arabinofuranosidase and acetyl xylan esterase activities, the latter two with p-nitrophenyl arabinofuranoside and p-nitrophenyl acetate as substrates, respectively. No activity with Avicel, carboxymethyl cellulose, p-nitrophenyl galactopyranoside, and p-nitrophenyl glucopyranoside | Acidothermus cellulolyticus 11B | ? | - |
? | |
| additional information | no activity with 4-nitrophenyl galactopyranoside, 4-nitrophenyl glucopyranoside, Avicel and carboxymethyl cellulose | Acidothermus cellulolyticus ATCC 43068 | ? | - |
? | |
| additional information | the purified recombinant enzyme Xyn10B is highly active producing xylobiose and xylose as the major end products, as well as debranching the substrates by removing arabinose and acetyl side chains. Xyn10B is a trifunctional enzyme having endo-xylanase, arabinofuranosidase and acetyl xylan esterase activities, the latter two with p-nitrophenyl arabinofuranoside and p-nitrophenyl acetate as substrates, respectively. No activity with Avicel, carboxymethyl cellulose, p-nitrophenyl galactopyranoside, and p-nitrophenyl glucopyranoside | Acidothermus cellulolyticus ATCC 43068 | ? | - |
? | |
| oat spelt xylan + H2O | - |
Acidothermus cellulolyticus | xylobiose + xylotriose + ? | - |
? | |
| oat spelt xylan + H2O | - |
Acidothermus cellulolyticus | xylobiose + ? | - |
? | |
| xylotetraose + H2O | - |
Acidothermus cellulolyticus | 2 xylobiose | - |
? | |
| xylotriose + H2O | - |
Acidothermus cellulolyticus | xylobiose + xylose | - |
? | |
| xylotriose + H2O | - |
Acidothermus cellulolyticus 11B | xylobiose + xylose | - |
? | |
| xylotriose + H2O | - |
Acidothermus cellulolyticus ATCC 43068 | xylobiose + xylose | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 69000, SDS-PAGE | Acidothermus cellulolyticus |
| More | secondary structure comparisons, overview | Acidothermus cellulolyticus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Acel_0180 | - |
Acidothermus cellulolyticus |
| endo-xylanase | - |
Acidothermus cellulolyticus |
| xylanase 10B | - |
Acidothermus cellulolyticus |
| Xyn10B | - |
Acidothermus cellulolyticus |
| Xyn10B | the trifunctional enzyme exhibits endo-xylanase, arabinofuranosidase and acetyl xylan esterase activities | Acidothermus cellulolyticus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | - |
- |
Acidothermus cellulolyticus |
| 70 | - |
recombinant enzyme | Acidothermus cellulolyticus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | 85 | activity range, inactive below and above, recombinant enzyme, profile overview | Acidothermus cellulolyticus |
| 50 | 80 | about 60% activity at 50°C, about 750% activity at 60°C, 100% activity at 70°C, about 90% activity at 80°C, no activity at 90°C | Acidothermus cellulolyticus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | 70 | purified recombinant enzyme, 30 min, completely stable at 20-50°C, 90% activity is retained at 60°C, and 70% at 70°C, inactivation at 80°C | Acidothermus cellulolyticus |
| 20 | 80 | the enzyme remains completely stable from 20 to 50°C, while about 90 and 70% of the activity is retained at 60 and 70°C after 30 min. The melting temperature is 80°C | Acidothermus cellulolyticus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | - |
- |
Acidothermus cellulolyticus |
| 6 | - |
recombinant enzyme | Acidothermus cellulolyticus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 3.5 | 8.5 | activity range, recombinant enzyme, profile overview | Acidothermus cellulolyticus |
| 5 | 8 | more than 60% activity between pH 5.0 and 8.0 | Acidothermus cellulolyticus |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 8 | purified recombinant enzyme, stable at | Acidothermus cellulolyticus |
| 5 | 8 | the enzyme remains completely stable after 30 min incubation between pH 5.0 and 8.0 | Acidothermus cellulolyticus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | enzyme Xyn10B belongs to the glycoside hydrolase family 10, GH10 | Acidothermus cellulolyticus |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
