EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
3.2.1.8 | additional information | Xyn10A is a modular xylanase comprising nine domains, i.e., three family 22 carbohydrate-binding modules (CBMs), a family 10 catalytic domain of glycosyl hydrolases (xylanase), a family 9 CBM, a glycine-rich region, and three surface layer homology (SLH) domains. The CBMs of Xyn10A play an important role in the hydrolysis of plant cell walls | Paenibacillus curdlanolyticus |
EC Number | Application | Comment | Organism |
---|---|---|---|
3.2.1.8 | industry | purified recombinant Xyn10A is a useful candidate for producing xylooligosaccharides as thickeners, fat substitutes, and antifreeze food additives in the food industry | Paenibacillus curdlanolyticus |
EC Number | Cloned (Comment) | Organism |
---|---|---|
3.2.1.8 | pUC19 plasmid, carrying the 10-kb HindIII fragment containing the xylanase gene expressed in Escherichia coli DH5alpha | Paenibacillus curdlanolyticus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.2.1.8 | additional information | removal of the CBMs from Xyn10A strongly reduces the ability of plant cell wall hydrolysis | Paenibacillus curdlanolyticus |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.2.1.8 | 142700 | - |
sequence analysis | Paenibacillus curdlanolyticus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.8 | Paenibacillus curdlanolyticus | B1A3N2 | - |
- |
3.2.1.8 | Paenibacillus curdlanolyticus B-6 | B1A3N2 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.2.1.8 | by a single step of affinity purification on avicel, 139.4fold with a 38.1% yield | Paenibacillus curdlanolyticus |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.2.1.8 | 0.7 | - |
crude extract | Paenibacillus curdlanolyticus |
3.2.1.8 | 97.6 | - |
139.4fold purifed enzyme | Paenibacillus curdlanolyticus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.8 | alpha-cellulose + H2O | high affinity, affinity is slightly greater for celluloses than for insoluble xylans and chitin | Paenibacillus curdlanolyticus | ? | - |
? | |
3.2.1.8 | alpha-cellulose + H2O | high affinity, affinity is slightly greater for celluloses than for insoluble xylans and chitin | Paenibacillus curdlanolyticus B-6 | ? | - |
? | |
3.2.1.8 | avicel + H2O | high affinity | Paenibacillus curdlanolyticus | ? | - |
? | |
3.2.1.8 | avicel + H2O | high affinity | Paenibacillus curdlanolyticus B-6 | ? | - |
? | |
3.2.1.8 | birchwood xylan + H2O | high affinity, hydrolyzes birchwood xylan (hard wood) more effectively than oat spelt xylan (soft wood) | Paenibacillus curdlanolyticus | ? | - |
? | |
3.2.1.8 | cell wall fragment + H2O | Xyn10A containing three SLH domains at its C-terminus can bind to cell wall fragments significantly (32%) | Paenibacillus curdlanolyticus | ? | - |
? | |
3.2.1.8 | chitin + H2O | high affinity | Paenibacillus curdlanolyticus | ? | - |
? | |
3.2.1.8 | chitin + H2O | high affinity | Paenibacillus curdlanolyticus B-6 | ? | - |
? | |
3.2.1.8 | additional information | can effectively hydrolyze agricultural wastes, e.g., corn cob, corn hull, rice husk (which has a strong structure and is normally not easy to hydrolyze), rice straw, and bagasse | Paenibacillus curdlanolyticus | ? | - |
? | |
3.2.1.8 | additional information | can effectively hydrolyze agricultural wastes, e.g., corn cob, corn hull, rice husk (which has a strong structure and is normally not easy to hydrolyze), rice straw, and bagasse | Paenibacillus curdlanolyticus B-6 | ? | - |
? | |
3.2.1.8 | oat spelt xylan + H2O | high affinity | Paenibacillus curdlanolyticus | ? | - |
? | |
3.2.1.8 | starch + H2O | some affinity for polysaccharides that do not contain beta-1,4 linkages, e.g., starches from potato and wheat | Paenibacillus curdlanolyticus | ? | - |
? | |
3.2.1.8 | starch + H2O | some affinity for polysaccharides that do not contain beta-1,4 linkages, e.g., starches from potato and wheat | Paenibacillus curdlanolyticus B-6 | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.8 | endo-beta-1,4-xylanase | - |
Paenibacillus curdlanolyticus |
3.2.1.8 | xylanase | - |
Paenibacillus curdlanolyticus |
3.2.1.8 | Xyn10A | - |
Paenibacillus curdlanolyticus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.8 | 60 | - |
- |
Paenibacillus curdlanolyticus |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.8 | 50 | - |
- |
Paenibacillus curdlanolyticus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.8 | 7 | - |
- |
Paenibacillus curdlanolyticus |
EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.8 | 5 | 8 | still 80% stability at pH 9.0 | Paenibacillus curdlanolyticus |