Activating Compound | Comment | Organism | Structure |
---|---|---|---|
dithiothreitol | 10-50 mM, 1.2-1.3fold activation | Pyrococcus furiosus | |
Guanidine HCl | 0.1 mM, 1.1fold activation | Pyrococcus furiosus | |
mercaptoethanol | 10 mM, 1.1fold asctivation | Pyrococcus furiosus | |
SDS | 1 mM, 1.7fold activation | Pyrococcus furiosus | |
Triton X-100 | 0.1-5.0%, activity on pullulan doubles after preincubation | Pyrococcus furiosus | |
Urea | 1.0-5.0 mM, 1.1fold activation | Pyrococcus furiosus |
Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli | Pyrococcus furiosus |
General Stability | Organism |
---|---|
the enzyme is highly resistant to chemical denaturing reagents | Pyrococcus furiosus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Guanidine HCl | 2.0 mM, about 55% inhibition | Pyrococcus furiosus | |
SDS | 5-50 mM, 25-85% inhibition | Pyrococcus furiosus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
pullulan | Km-value for pullulan at pH 5.6, 98°C, no metal ion added: 1.6 mg/ml. Km-value for pullulan, at pH 5.6, 98°C, 0.5 mM Ca2+: 0.13 mg/ml | Pyrococcus furiosus | |
additional information | - |
soluble starch | Km-value for soluble starch at pH 5.6, 98°C, no metal ion added: 2.48 mg/ml. Km-value for soluble starch at pH 5.6, 98°C, 0.5 mM Ca2+: 1.17 mg/ml | Pyrococcus furiosus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ba2+ | increases activity | Pyrococcus furiosus | |
Ca2+ | increases activity and substrate affinity | Pyrococcus furiosus | |
Co2+ | increases activity | Pyrococcus furiosus | |
Mg2+ | increases activity | Pyrococcus furiosus | |
Mn2+ | increases activity | Pyrococcus furiosus | |
Sr2+ | increases activity | Pyrococcus furiosus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
50000 | - |
x * 50000, recombinant enzyme after heat treatment in denaturing buffer at 70°C or below, SDS-PAGE | Pyrococcus furiosus |
89000 | - |
- |
Pyrococcus furiosus |
90000 | - |
x * 90000, recombinant enzyme after heat treatment in denaturing buffer at 100°C and 110°C, SDS-PAGE | Pyrococcus furiosus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus furiosus | O30772 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Pyrococcus furiosus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
amylopectin + H2O | - |
Pyrococcus furiosus | ? | - |
? | |
amylose + H2O | - |
Pyrococcus furiosus | ? | - |
? | |
glycogen + H2O | - |
Pyrococcus furiosus | ? | - |
? | |
additional information | the enzyme also hydrolyzes oligosaccharides but much slower. The longer the oligosaccharide chain, the higher the hydrolysis rate | Pyrococcus furiosus | ? | - |
? | |
pullulan + H2O | - |
Pyrococcus furiosus | ? | - |
? | |
soluble starch | - |
Pyrococcus furiosus | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 50000, recombinant enzyme after heat treatment in denaturing buffer at 70°C or below, SDS-PAGE | Pyrococcus furiosus |
? | x * 90000, recombinant enzyme after heat treatment in denaturing buffer at 100°C and 110°C, SDS-PAGE | Pyrococcus furiosus |
Synonyms | Comment | Organism |
---|---|---|
Apu | - |
Pyrococcus furiosus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
105 | - |
with 0.5 mM Ca2+ | Pyrococcus furiosus |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
80 | 115 | 80°C: about 40% of maximal activity, 115°C: about 50% of maximal activity, with or wothout 0.5 mM Ca2+ | Pyrococcus furiosus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
Ca2+ increases thermostability | Pyrococcus furiosus |
70 | - |
the recombinant enzyme remains folded after denaturation at temperatures of below 70°C | Pyrococcus furiosus |
90 | - |
half-life: 11 h for EDTA-treated enzyme, 44 h in presence of 5 mM Ca2+ | Pyrococcus furiosus |
100 | - |
denaturating temperatures of above 100°C are required for complete unfolding. The enzyme remains active even after denaturation at 100 and 110°C,suggesting that unfolding isnot complete | Pyrococcus furiosus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.5 | - |
- |
Pyrococcus furiosus |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
4.3 | 7.2 | pH 4.3: about 80% of maximal activity, pH 7.2: about 75% of maximal activity | Pyrococcus furiosus |