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Literature summary for 2.4.1.207 extracted from

  • Morales-Quintana, L.; Beltran, D.; Mendez-Yanez, A.; Valenzuela-Riffo, F.; Herrera, R.; Moya-Leon, M.A.
    Characterization of FcXTH2, a novel xyloglucan endotransglycosylase/hydrolase enzyme of chilean strawberry with hydrolase activity (2020), Int. J. Mol. Sci., 21, 3380 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

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 [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

Localization Comment Organism GeneOntology No. Textmining
cell wall
-
Fragaria chiloensis 5618
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Organism

Organism UniProt Comment Textmining
Fragaria chiloensis D5HP43
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-

Posttranslational Modification

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 (Commentary)

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

Source Tissue Comment Organism Textmining
fruit
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Fragaria chiloensis
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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 [micromol/min/mg]

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 and Products (Substrate)

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

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

Synonyms Comment Organism
FcXTH2
-
Fragaria chiloensis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
recombinant enzyme Fragaria chiloensis

Temperature Range [°C]

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 [1/s]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
recombinant enzyme Fragaria chiloensis

pH Range

pH Minimum pH Maximum Comment Organism
4 7 over 30% of maximal activity within this range, recombinant enzyme, profile overview Fragaria chiloensis

General Information

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 [mM/s]

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