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Literature summary for 2.4.1.207 extracted from

  • Stratilova, B.; Firakova, Z.; Klaudiny, J.; Sestak, S.; Kozmon, S.; Strouhalova, D.; Garajova, S.; Ait-Mohand, F.; Horvathova, A.; Farkas, V.; Stratilova, E.; Hrmova, M.
    Engineering the acceptor substrate specificity in the xyloglucan endotransglycosylase TmXET6.3 from nasturtium seeds (Tropaeolum majus L.) (2019), Plant Mol. Biol., 100, 181-197 .
    View publication on PubMed
Search for more literature for 2.4.1.207

Cloned(Commentary)

Cloned (Comment) Organism
gene xet6.3, sequence comparisons and analysis, recombinant expression of His-/FLAG-tagged wild-type and mutant enzymes in Escherichia coli strain XL10-Gold, recombinant expression of His-/FLAG-tagged wild-type and mutant enzymes in Pichia pastoris strain GS115, from the latter the enzymes are secreted Tropaeolum majus

Protein Variants

Protein Variants Comment Organism
H94Q site-directed mutagenesis, the mutant enzymes exhibits increased activity with cello-oligosacchrides, relative to those with the natural xyloglucan octasaccharide acceptor substrate Tropaeolum majus
H94Q/A104D/Q108R site-directed mutagenesis, the mutant enzymes exhibits increased activity with cello-oligosacchrides, relative to those with the natural xyloglucan octasaccharide acceptor substrate Tropaeolum majus
K234T/K237T site-directed mutagenesis, the mutant enzymes exhibits increased activity with cello-oligosacchrides, relative to those with the natural xyloglucan octasaccharide acceptor substrate Tropaeolum majus
K237T site-directed mutagenesis, the mutant enzymes exhibits increased activity with cello-oligosacchrides, relative to those with the natural xyloglucan octasaccharide acceptor substrate Tropaeolum majus
Q108R site-directed mutagenesis, the mutant enzymes exhibits increased activity with cello-oligosacchrides, relative to those with the natural xyloglucan octasaccharide acceptor substrate Tropaeolum majus

Localization

Localization Comment Organism GeneOntology No. Textmining
cell wall
-
 Tropaeolum majus 5618
-
additional information the putative signal peptide is predicted to be 30 residues long with a cleavage site between Ala30 and Gly31 Tropaeolum majus
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-

Organism

Organism UniProt Comment Textmining
Tropaeolum majus V5ZEF7
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-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein enzyme are deglycosylated with commercial N-glycosidase F. Unglycosylated TmXET6.3 due to N-deglycosylation loses its enzyme activity, it is likely that N-glycosylation affects protein folding and/or catalytic activity Tropaeolum majus

Purification (Commentary)

Purification (Comment) Organism
recombinant extracellular His-/FLAG-tagged wild-type and mutant enzymes expressed from Pichia pastoris strain GS115 by nickel affinity chromatography and desalting gel filtration Tropaeolum majus

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Tropaeolum majus
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root
-
 Tropaeolum majus
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seed germinated Tropaeolum majus
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seedling
-
 Tropaeolum majus
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stem
-
 Tropaeolum majus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information SR-labelled xyloglucan-oligosaccharides, laminari-oligosaccharides, mixed-linkage (1,3/1,4)-beta-D-glucosaccharides, (1,4)-beta-D-glucurono-xylooligosaccharides, cello-oligosaccharides, manno-oligosaccharides and penta-galacturonic acid oligosaccharide, are used as acceptors. Preferred substrate are xyloglucan-oligosaccharides and cello-oligosaccharides, no activity is detected in tissues other than germinating seeds with laminari-oligosaccharides, mixed-linkage (1,3/1,4)-beta-D-glucosaccharides, (1,4)-beta-D-glucurono-xylooligosaccharides, manno-oligosaccharides and penta-galacturonic acid oligosaccharide. Heterotransglycosylation activities and acceptor substrate specificity of TmXET6.3, overview Tropaeolum majus ?
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Subunits

Subunits Comment Organism
? x * 30000, recombinant unglycosylated His-FLAG-tagged TmXET6.3 lacking the 30-residue signal peptide, SDS-PAGE, x * 31300, recombinant glycosylated His-FLAG-tagged TmXET6.3 lacking the 30-residue signal peptide, SDS-PAGE Tropaeolum majus

Synonyms

Synonyms Comment Organism
XET
-
 Tropaeolum majus
XET6.3
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 Tropaeolum majus
xyloglucan xyloglucosyl transferase
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 Tropaeolum majus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
 assay at room temperature Tropaeolum majus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
 assay at Tropaeolum majus

General Information

General Information Comment Organism
evolution isozyme TmXET6.3 is a membrer of the GH16 family Tropaeolum majus
malfunction compared to the wild-type enzyme, the single Q108R and K237T, and double-K234T/K237T and triple-H94Q/A104D/Q108R variants exhibit enhanced heterotransglycosylation activities with xyloglucan and (1,4)-beta-D-glucooligosaccharides, while those with (1,3/1,4)- and (1,6)-beta D-glucooligosaccharides are suppressed, the incorporation of xyloglucan to (1,4)-beta-D-glucooligosaccharides by the H94Q variant is influenced most extensively. Physiological effects, overview Tropaeolum majus
metabolism typically, several XET isoforms operate during plant development or in response to environmental stimuli, consequently the expression of XTH genes needs to be regulated Tropaeolum majus
additional information homology modeling of TmXET6.3 constructed based on the coordinates of the crystal structure of hybrid aspen PttXET16A as the template (PDB ID 1UN1). H94, A104, Q108, K234 and K237 are the key residues that underpinned the acceptor substrate specificity of TmXET6.3, evaluations of TmXET6.3 transglycosylation activities Tropaeolum majus