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Literature summary for 3.2.1.139 extracted from

  • Shallom, D.; Golan, G.; Shoham, G.; Shoham, Y.
    Effect of dimer dissociation on activity and thermostability of the alpha-glucuronidase from Geobacillus stearothermophilus: dissecting the different oligomeric forms of family 67 glycoside hydrolases (2004), J. Bacteriol., 186, 6928-6937.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.2.1.139

Protein Variants

Protein Variants Comment Organism
W328E/R329T activity of the monomeric mutant enzyme is significantly lower than activity of dimeric wild-type enzyme Geobacillus stearothermophilus
W328E/R329T/R665N activity of the monomeric mutant enzyme is significantly lower than activity of dimeric wild-type enzyme, melting temperature is 0.5°C lower than. OPtimal temperature is around 35°C, compared to 65° for the wild-type enzym Geobacillus stearothermophilus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
78339
-
 1 * 78339, mutant enzymeW328E/R329T, calculated from sequence Geobacillus stearothermophilus
78381
-
 1 * 78381, mutant enzymeW328E/R329T/R665N, calculated from sequence Geobacillus stearothermophilus
78500
-
 1 * 78500, mutant enzymes W328E/R329T/R665N and W328E/R329T, SDS-PAGE Geobacillus stearothermophilus

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus
-
 recombinant enzyme
-
Geobacillus stearothermophilus T-6
-
 recombinant enzyme
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-O-alpha-(4-O-methyl-alpha-D-glucuronosyl)-xylotriose + H2O i.e. aldotetraouronic acid Geobacillus stearothermophilus 4-O-methyl-alpha-D-glucuronic acid + xylotriose
-
 ?
2-O-alpha-(4-O-methyl-alpha-D-glucuronosyl)-xylotriose + H2O i.e. aldotetraouronic acid Geobacillus stearothermophilus T-6 4-O-methyl-alpha-D-glucuronic acid + xylotriose
-
 ?

Subunits

Subunits Comment Organism
dimer wild-type enzyme. The dimerization of AguA is essential for efficient catalysis and the dissociation into monomers results in subtle conformational changes in the structure which indirectly influence the active site region and reduce the activity Geobacillus stearothermophilus
monomer 1 * 78339, mutant enzymeW328E/R329T, calculated from sequence Geobacillus stearothermophilus
monomer 1 * 78381, mutant enzymeW328E/R329T/R665N, calculated from sequence Geobacillus stearothermophilus
monomer 1 * 78500, mutant enzymes W328E/R329T/R665N and W328E/R329T, SDS-PAGE Geobacillus stearothermophilus

Synonyms

Synonyms Comment Organism
AguA
-
 Geobacillus stearothermophilus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
 mutant enzyme W328E/R329T/R665N Geobacillus stearothermophilus
65
-
 wild-type enzyme Geobacillus stearothermophilus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
20 55 20°C: about 50% of maximal activity, 55°C: about 40% of maximal activity, mutant enzyme W328E/R329T/R665N Geobacillus stearothermophilus
60 70 40°C: about 40% of maximal activity, 70°C: about 90% of maximal activity, wild-type enzyme Geobacillus stearothermophilus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70
-
 20 min, wild-type enzyme and mutant enzyme W328E/R329T/R665N, about 10% loss of activity Geobacillus stearothermophilus
73
-
 melting temperature of mutant enzyme W328E/R329T/R665N is 72.9°C, melting temperature of wild-type enzyme is 73.4°C Geobacillus stearothermophilus
75
-
 20 min, wild-type enzyme loses 70% of its activity, mutant enzyme W328E/R329T/R665N copletely loses activity Geobacillus stearothermophilus