Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.2.1.151 extracted from

  • Mark, P.; Baumann, M.J.; Ekloef, J.M.; Gullfot, F.; Michel, G.; Kallas, A.M.; Teeri, T.T.; Brumer, H.; Czjzek, M.
    Analysis of nasturtium TmNXG1 complexes by crystallography and molecular dynamics provides detailed insight into substrate recognition by family GH16 xyloglucan endo-transglycosylases and endo-hydrolases (2008), Proteins, 75, 820-836.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
heterologous expression in Pichia pastoris strain GS115 Tropaeolum majus

Crystallization (Commentary)

Crystallization (Comment) Organism
loop mutant TmNXG1-DELTAYNIIG with an oligosaccharide product bound in the negative active-site subsites, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement, molecular dynamics simulations and structure modelling of wild-type and mutant enzyme, detailed overview Tropaeolum majus
TmNXG1-deltaYNIIG with bound substrate xylogluco-oligosaccharide Tropaeolum majus

Protein Variants

Protein Variants Comment Organism
additional information TmNXG1-deltaYNIIG: active site loop deletion mutant, three loops: Asn84-Asp93 (glycosyl donor subsite), Glu117-Gly126, and Trp190-Tyr197 (critical to acceptor substrate binding, inter alia influencing transglycosylation/hydrolysis ratio) Tropaeolum majus
additional information construction of a loop mutant TmNXG1-DELTAYNIIG Tropaeolum majus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information modelling of Michaelis complexes of wild-type and mutant enzyme, overview Tropaeolum majus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Tropaeolum majus nasturtium xyloglucanase 1, predominant endo-hydrolase of Tropaeolum majus that can also perform xyloglucan endo-transglycosylation at elevated substrate concentrations ?
-
?
xyloglucan + H2O Tropaeolum majus
-
xyloglucan oligosaccharides
-
?

Organism

Organism UniProt Comment Textmining
Tropaeolum majus
-
-
-
Tropaeolum majus
-
nasturtium
-

Purification (Commentary)

Purification (Comment) Organism
concentration with Centricon devices, cutoff 10 kDa Tropaeolum majus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information nasturtium xyloglucanase 1, predominant endo-hydrolase of Tropaeolum majus that can also perform xyloglucan endo-transglycosylation at elevated substrate concentrations Tropaeolum majus ?
-
?
octodecasaccharide XLLG-XLLG + H2O xylogluco-nonasaccharide Tropaeolum majus ?
-
?
xyloglucan + H2O
-
Tropaeolum majus xyloglucan oligosaccharides
-
?
xyloglucan + H2O tamarind seed xyloglucan Tropaeolum majus xyloglucan oligosaccharides
-
?

Subunits

Subunits Comment Organism
More importance of various loops lining the active site. Subtle differences leading to a tighter hydrogen bonding pattern on the negative, glycosyl donor, binding subsites, together with loop flexibility on the positive, glycosyl acceptor, binding subsites appear to favor hydrolysis over transglycosylation in GH16 xyloglucan-active enzymes Tropaeolum majus

Synonyms

Synonyms Comment Organism
family GH16 xyloglucan endo-transglycosylase
-
Tropaeolum majus
More the enzyme belongs to the glycoside hydrolase family 16, GH16 Tropaeolum majus
TmNXG1
-
Tropaeolum majus
xyloglucan endotransglycosylase/hydrolase
-
Tropaeolum majus
xyloglucanase 1
-
Tropaeolum majus