Literature summary for 2.4.1.207 extracted from

Mark, P.; Zhang, Q.; Czjzek, M.; Brumer, H.; Ågren, H.
Molecular dynamics simulations of a branched tetradecasaccharide substrate in the active site of a xyloglucan endo-transglycosylase (2011), Mol. Simul., 37, 1001-1013.

No PubMed abstract available

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Organism

Organism	UniProt	Comment	Textmining
Populus tremula x Populus tremuloides	-	gene PtxtXET16-34	-

Synonyms

Synonyms	Comment	Organism
xyloglucan endo-transglycosylase	-	Populus tremula x Populus tremuloides

General Information

General Information	Comment	Organism
evolution	the enzyme belongs to the GH16 XTH family, extension clan GH-B enzymes	Populus tremula x Populus tremuloides
additional information	catalytic nucleophile is Glu85, general acid/base residue is Glu89, Asp87 is the so-called helper residue, molecular dynamics simulations of a branched tetradecasaccharide substrate XXXGXXXG in the active site of xyloglucan endo-transglycosylase. When Asp87 is deprotonated, electrostatic repulsion forces the nucleophilic away from C1 of the sugar ring in subsite 21 and the proton-donating ability of Glu89 iss also weakened due to the formation of a hydrogen bond with Asp87, whereas protonation of Asp87 results in the formation of a hydrogen bond with the catalytic nucleophile and correct positioning of the catalytic machinery	Populus tremula x Populus tremuloides

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Release 2023.1 (January 2023)