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 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 | UniProt | Comment | Textmining |
---|---|---|---|
Geobacillus stearothermophilus | - |
recombinant enzyme | - |
Geobacillus stearothermophilus T-6 | - |
recombinant enzyme | - |
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 | 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 | Comment | Organism |
---|---|---|
AguA | - |
Geobacillus stearothermophilus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
35 | - |
mutant enzyme W328E/R329T/R665N | Geobacillus stearothermophilus |
65 | - |
wild-type enzyme | Geobacillus stearothermophilus |
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 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 |