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Literature summary for 3.2.1.151 extracted from

  • Matsuzawa, T.; Saito, Y.; Yaoi, K.
    Key amino acid residues for the endo-processive activity of GH74 xyloglucanase (2014), FEBS Lett., 588, 1731-1738.
    View publication on PubMed
Search for more literature for 3.2.1.151

Cloned(Commentary)

Cloned (Comment) Organism
expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21-CodonPlus (DE3) RP Paenibacillus sp.

Protein Variants

Protein Variants Comment Organism
additional information selective replacement of the positive subsite residues with alanine mutations reduces the degree of processive activity and resulted in the more endo-dissociative-activity Paenibacillus sp.
W318A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Paenibacillus sp.
W319A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Paenibacillus sp.
W61A site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme Paenibacillus sp.
W64A site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme Paenibacillus sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics with one unit defined as the amount of enzyme that released 0.001 mmol of glucose equivalents as reducing sugars from xyloglucan per minute Paenibacillus sp.

Organism

Organism UniProt Comment Textmining
Paenibacillus sp. Q3MUH7
-
-
Paenibacillus sp. KM21 Q3MUH7
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21-CodonPlus (DE3) RP by nickel affinity chromatography and gel filtration Paenibacillus sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information analysis of xyloglucan digestion products by gel-filtration chromatography. Modelling of endo-dissociative- and endo-processive-type xyloglucanase structures, overview Paenibacillus sp. ?
-
 ?
additional information analysis of xyloglucan digestion products by gel-filtration chromatography. Modelling of endo-dissociative- and endo-processive-type xyloglucanase structures, overview Paenibacillus sp. KM21 ?
-
 ?
tamarind seed xyloglucan + H2O
-
 Paenibacillus sp. alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc + alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc + alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc + alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc
-
 ?
tamarind seed xyloglucan + H2O
-
 Paenibacillus sp. KM21 alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc + alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc + alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc + alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc
-
 ?

Synonyms

Synonyms Comment Organism
XEG74
-
 Paenibacillus sp.
xyloglucanase
-
 Paenibacillus sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
 assay at Paenibacillus sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 purified enzyme, stable up to Paenibacillus sp.

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
49.2
-
 tamarind seed xyloglucan pH 6.0, 45°C, recombinant wild-type enzyme catalytic domain Paenibacillus sp.
54.3
-
 tamarind seed xyloglucan pH 6.0, 45°C, recombinant mutant W61A enzyme catalytic domain Paenibacillus sp.
64.3
-
 tamarind seed xyloglucan pH 6.0, 45°C, recombinant mutant W64A enzyme catalytic domain Paenibacillus sp.
65.8
-
 tamarind seed xyloglucan pH 6.0, 45°C, recombinant mutant W319A enzyme catalytic domain Paenibacillus sp.
72
-
 tamarind seed xyloglucan pH 6.0, 45°C, recombinant mutant w318A enzyme catalytic domain Paenibacillus sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 assay at Paenibacillus sp.

pH Stability

pH Stability pH Stability Maximum Comment Organism
4 9 purified enzyme, stable at Paenibacillus sp.

General Information

General Information Comment Organism
additional information key amino acid residues for the endo-processive activity of GH74 xyloglucanase, an endo-processive xyloglucanase, are W318 and W319, found in the positive subsites. They are essential for processive degradation and are responsible for maintaining binding interactions with xyloglucan polysaccharide through a stacking effect, three-dimensional homology modelling, overview. The enzyme has four characteristic tryptophan residues (W61, W64, W318, and W319) around the active site cleft. Although W61 and W64 are dispensable for endo-processive xyloglucanase activity, these residues contribute slightly to endo-processive activity and/or substrate recognition Paenibacillus sp.