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Literature summary 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)

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.207 additional information
-
 additional information Michaelis-Menten kinetics Pinus radiata
2.4.1.207 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

EC Number Organism UniProt Comment Textmining
2.4.1.207 Pinus radiata A0A059SVJ4
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.207 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 ?
-
-
2.4.1.207 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

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.207 37
-
-
 Pinus radiata

Temperature Stability [°C]

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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.4.1.207 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

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.207 5
-
-
 Pinus radiata

General Information

EC Number General Information Comment Organism
2.4.1.207 evolution xyloglucan endotransglycosylase/hydrolase (XTH) enzymes hold transglycosylase (XET), hydrolase (XEH), or both activities Pinus radiata
2.4.1.207 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]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.4.1.207 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