Cloned (Comment) | Organism |
---|---|
gene XTH1, recombinant expression of His-tagged enzyme in Pichia pastoris | Pinus radiata |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten kinetics | Pinus radiata | |
0.0209 | - |
alpha-D-Xyl-(1->6)-[alpha-D-Xyl-(1->6)-[alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)]-beta-D-Glc-(1->4)]-beta-D-Glc-(1->4)-D-Glc | pH 5.0, 37°C, recombinant enzyme | Pinus radiata |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pinus radiata | A0A059SVJ4 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged XTH1 from Pichia pastoris by anion exchange chromatography and nickel affinity chromatography | Pinus radiata |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | prediction of union type and energy stability of the complexes formed between PrXTH1 and different substrates (XXXGXXXG, XXFGXXFG, XLFGXLFG and cellulose), structures overview. Molecular docking, molecular dynamics, MM-GBSA and electrostatic potential calculations are employed to predict the binding modes, free energies of interaction, and the distribution of electrostatic charge. The results suggest that the enzyme forms more stable complexes with hemicellulose substrates than cellulose, and the best ligand is the xyloglucan XLFGXLFG. PrXTH1 is able to interact with different xyloglycans structures but no activity is observed for cellulose as substrate | Pinus radiata | ? | - |
- |
|
tamarind xyloglucan + alpha-D-Xyl-(1->6)-[alpha-D-Xyl-(1->6)-[alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)]-beta-D-Glc-(1->4)]-beta-D-Glc-(1->4)-D-Glc | i.e. XGO, the enzyme activity is assayed by the colorimetric method, overview | Pinus radiata | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
PrXTH1 | - |
Pinus radiata |
XET | - |
Pinus radiata |
XTH1 | - |
Pinus radiata |
xyloglucan endo-transglycosylase/hydrolase | - |
Pinus radiata |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
- |
Pinus radiata |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
inactivation within 10 min at 100°C | Pinus radiata |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.02 | - |
alpha-D-Xyl-(1->6)-[alpha-D-Xyl-(1->6)-[alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)]-beta-D-Glc-(1->4)]-beta-D-Glc-(1->4)-D-Glc | pH 5.0, 37°C, recombinant enzyme | Pinus radiata |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5 | - |
- |
Pinus radiata |
General Information | Comment | Organism |
---|---|---|
evolution | xyloglucan endotransglycosylase/hydrolase (XTH) enzymes hold transglycosylase (XET), hydrolase (XEH), or both activities | Pinus radiata |
additional information | the model structure of the PrXTH1 is reported, displaying a beta-sandwich structure characteristic of the XTH protein family, with the catalytic residues in the middle of the protein structure, composed of residues Glu79, Asp81, and Glu83 | Pinus radiata |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
48.8 | - |
alpha-D-Xyl-(1->6)-[alpha-D-Xyl-(1->6)-[alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)]-beta-D-Glc-(1->4)]-beta-D-Glc-(1->4)-D-Glc | pH 5.0, 37°C, recombinant enzyme | Pinus radiata |