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Literature summary for 2.4.1.207 extracted from

  • Morales-Quintana, L.; Carrasco-Orellana, C.; Beltran, D.; Moya-Leon, M.A.; Herrera, R.
    Molecular insights of a xyloglucan endo-transglycosylase/hydrolase of radiata pine (PrXTH1) expressed in response to inclination kinetics and computational study (2019), Plant Physiol. Biochem., 136, 155-161 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene XTH1, recombinant expression of His-tagged enzyme in Pichia pastoris Pinus radiata

KM Value [mM]

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

Organism UniProt Comment Textmining
Pinus radiata A0A059SVJ4
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-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged XTH1 from Pichia pastoris by anion exchange chromatography and nickel affinity chromatography Pinus radiata

Substrates and Products (Substrate)

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

Synonyms Comment Organism
PrXTH1
-
Pinus radiata
XET
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Pinus radiata
XTH1
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Pinus radiata
xyloglucan endo-transglycosylase/hydrolase
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Pinus radiata

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
Pinus radiata

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
inactivation within 10 min at 100°C Pinus radiata

Turnover Number [1/s]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
-
Pinus radiata

General Information

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 [mM/s]

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