Cloned (Comment) | Organism |
---|---|
gene XTH2, cloned from young leaves, recombinant expression in Pichia pastoris strain X-33, subcloning in Escherichia coli | Fragaria chiloensis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten kinetics | Fragaria chiloensis | |
0.029 | - |
xyloglucan | recombinant enzyme, pH 5.5, 37°C | Fragaria chiloensis |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cell wall | - |
Fragaria chiloensis | 5618 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Fragaria chiloensis | D5HP43 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | FcXTH2 shows an N-glycosylation site that is located far to the active site and oriented on the edge of the opposite face. In the primary sequence of the protein, the N-glycosylation site is spaced by 17 residues from the catalytic triad | Fragaria chiloensis |
Purification (Comment) | Organism |
---|---|
recombinant enzyme XTH2 12.43fold from Pichia pastoris by anion exchange chromatography, cation exchange chromatography, desalting gel filtration, and affinity chromatography | Fragaria chiloensis |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
fruit | - |
Fragaria chiloensis | - |
leaf | - |
Fragaria chiloensis | - |
additional information | enzyme FcXTH2 shows a high expression level in vegetative tissues and a relatively low but constant expression level in developing fruit | Fragaria chiloensis | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.255 | - |
purified recombinant enzyme, pH 5.5, 37°C | Fragaria chiloensis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | protein-ligand interaction analysis and mode of FcXTH2, overview. Favorable binding energies are obtained between FcXTH2 and the different ligands. Nevertheless, the interaction of FcXTH2 with XXXGXXXG is highly favored, and a weaker binding interaction is found between the protein and cellodextrin 8-mer or XXFGXXFG as ligands. Different octasaccharides are positioned along the open groove of the protein. Only XXXGXXXG hemicellulose octasaccharide locates close to two of the catalytic residues (Glu85, Asp87) being able to interact with them | Fragaria chiloensis | ? | - |
- |
|
xyloglucan + xyloglucan oligosaccharide | the recombinant FcXTH2 protein displays mainly XEH activity and basal XET activity. The Sulova method for XET activity is based in the ability of long xyloglucans (XGs) to bind iodine: the transglycosylation activity causes a reduction in size of XGs that loses the ability to bind the dye. Thus, the XET activity causes the reduction in molecular weight of XGs by transglycosylation of portions of the XG donor to low relative molecular mass (low-Mr) oligosaccharide acceptors whereby no net formation of reducing ends takes place. Thus, the XET activity is assayed by following changes in absorbance at 620 nm | Fragaria chiloensis | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 35900, XTH2 without signal sequence, SDS-PAGE | Fragaria chiloensis |
More | analysis of the FcXTH2 model at secondary structure level shows that the enzyme consists of 1 alpha-helix, 2 310-helices and 15 beta-sheets, all of them connected by 20 loops, structure modeling, overview | Fragaria chiloensis |
Synonyms | Comment | Organism |
---|---|---|
FcXTH2 | - |
Fragaria chiloensis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
recombinant enzyme | Fragaria chiloensis |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | 50 | over 40% of maximal activity within this range, recombinant enzyme, profile overview | Fragaria chiloensis |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
8.21 | - |
xyloglucan | recombinant enzyme, pH 5.5, 37°C | Fragaria chiloensis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.5 | - |
recombinant enzyme | Fragaria chiloensis |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
4 | 7 | over 30% of maximal activity within this range, recombinant enzyme, profile overview | Fragaria chiloensis |
General Information | Comment | Organism |
---|---|---|
additional information | docking studies, molecular dynamics simulation and modeling of a three-dimensional structure of FcXTH2 using the structure of TmNXG1 (PDB ID 2UWA) as template. Analysis of the molecular mechanism of interaction of FcXTH2 with xyloglucans as substrate | Fragaria chiloensis |
physiological function | enzyme FcXTH2 protein displays mainly xyloglucan hydrolase (XEH) activity and basal xyloglucan endotransglycosylase (XET) activity, and FcXTH2 is primarily a XEH. The enzyme is involved in the modification of the xyloglucans, a type of hemicellulose present in the cell wall. Possible role in strawberry development for enzyme FcXTH2 | Fragaria chiloensis |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
283.1 | - |
xyloglucan | recombinant enzyme, pH 5.5, 37°C | Fragaria chiloensis |