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Literature summary for 3.1.1.117 extracted from
- Investigation of a thermostable multi-domain xylanase-glucuronoyl esterase enzyme from Caldicellulosiruptor kristjanssonii incorporating multiple carbohydrate-binding modules (2020), Biotechnol. Biofuels, 13, 68 .
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | due to its thermostability, enzyme CkXyn10C-GE15A is a promising candidate for industrial processes, with both catalytic domains exhibiting melting temperatures over 70°C. Of particular interest is the glucuronoyl esterase domain, as it represents the first studied thermostable enzyme displaying this activity | Caldicellulosiruptor acetigenus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 8.6 | - |
benzyl-D-glucuronate | pH 7.5, 40°C | Caldicellulosiruptor acetigenus |  |
| 18.5 | - |
benzyl-D-glucuronate | pH 7.5, 22°C | Caldicellulosiruptor acetigenus | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cell wall | the enzyme is anchored to the cell wall by its C-terminal surface layer homology (SLH)-domains, overview | Caldicellulosiruptor acetigenus | 5618 | - |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Caldicellulosiruptor acetigenus | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| allyl-D-glucuronate + H2O | - |
Caldicellulosiruptor acetigenus | prop-2-en-1-ol + glucuronic acid | - |
? | |
| benzyl-D-glucuronate + H2O | - |
Caldicellulosiruptor acetigenus | benzyl alcohol + D-glucuronic acid | - |
? | |
| methyl-D-glucuronate + H2O | low activity | Caldicellulosiruptor acetigenus | methanol + glucuronic acid | - |
? | |
| additional information | no activity is detected with methyl-D-galacturonate, indicating that CkGE15A has a strict preference for GlcA-derived esters | Caldicellulosiruptor acetigenus | ? | - |
- |
|
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | domain architecture of CkXyn10C-GE15A with ten domains: enzyme CkXyn10C-GE15A contains two distinct putative catalytic modules: a GH10 xylanase and a GE from CE15. In addition, two N-terminal CBM22 domains as well as three CBM9 domains sandwiched between the catalytic domains are predicted, as well as a cadherin-like domain and two surface layer homology (SLH) domains following the GE domain at the C-terminus | Caldicellulosiruptor acetigenus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CkXyn10C-GE15A | - |
Caldicellulosiruptor acetigenus |
| dual-function xylanase-glucuronoyl esterase enzyme | - |
Caldicellulosiruptor acetigenus |
| More | cf. EC 3.2.1.8 | Caldicellulosiruptor acetigenus |
| multi-domain xylanase-glucuronoyl esterase | - |
Caldicellulosiruptor acetigenus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 22 | 40 | assay at | Caldicellulosiruptor acetigenus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 22 | 40 | assay at, the activity at 40°C is about 6fold higher compared to 22°C | Caldicellulosiruptor acetigenus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 72 | - |
enzyme melting temperature | Caldicellulosiruptor acetigenus |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0197 | - |
benzyl-D-glucuronate | pH 7.5, 22°C | Caldicellulosiruptor acetigenus | |
| 0.0565 | - |
benzyl-D-glucuronate | pH 7.5, 40°C | Caldicellulosiruptor acetigenus | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
with benzyl-D-glucuronate | Caldicellulosiruptor acetigenus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | as there are no bacterial CBM1 modules, it is possible that the CBM9 modules present in CkXyn10C-GE15A are performing a similar function as the CBM1 modules would in fungal enzymes | Caldicellulosiruptor acetigenus |
| physiological function | the thermostable, dual-function enzyme CkXyn10C-GE15A from the hyperthermophilic bacterium Caldicellulosiruptor kristjanssonii shows xylanase as well as glucuronoyl esterase activities. Although the enzyme domains are naturally linked together, when added separately to biomass, the expected boosting of the xylanase action is not seen. This lack of intramolecular synergy might suggest, that increased xylose release is not the main beneficial trait given by glucuronoyl esterases | Caldicellulosiruptor acetigenus |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0011 | - |
benzyl-D-glucuronate | pH 7.5, 22°C | Caldicellulosiruptor acetigenus | |
| 0.0066 | - |
benzyl-D-glucuronate | pH 7.5, 40°C | Caldicellulosiruptor acetigenus | |
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