EC Number | Cloned (Comment) | Organism |
---|---|---|
3.2.1.3 | expression in Saccharomyces cerevisiae using the yeast phosphoglycerate kinase gene promoter with the original vector signal sequence eliminated, co-expression with a barley alpha-amylase 1 mutant with constitutive secretion in active forms | Lentinula edodes |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.2.1.3 | additional information | co-expressed recombinant barley alpha-amylase 1 mutant and recombinant GLA synergistically enhanced the rate of hydrolysis by about 3fold for corn and wheat starch granules, compared to the sum of the individual activities, exo-endo synergism, reaction ratios, overview | Lentinula edodes |
EC Number | General Stability | Organism |
---|---|---|
3.2.1.3 | the recombinant enzyme stability is enhanced by 27% by Ca2+ at 0.1 mM | Lentinula edodes |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.2.1.3 | Cu2+ | 53% inhibition at 10 mM | Lentinula edodes | |
3.2.1.3 | EDTA | slight inhibition | Lentinula edodes | |
3.2.1.3 | Fe2+ | 29% inhibition at 10 mM | Lentinula edodes | |
3.2.1.3 | Mg2+ | slight inhibition | Lentinula edodes |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.2.1.3 | Ca2+ | bound Ca2+ in the enzyme molecule is essential at 50°C | Lentinula edodes |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.3 | starch + H2O | Lentinula edodes | - |
D-glucose + ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.3 | Lentinula edodes | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.3 | starch + H2O | - |
Lentinula edodes | D-glucose + ? | - |
? | |
3.2.1.3 | starch + H2O | soluble corn and wheat starch granules | Lentinula edodes | D-glucose + ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.3 | GLA | - |
Lentinula edodes |
3.2.1.3 | glucoamylase | - |
Lentinula edodes |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.3 | 50 | - |
- |
Lentinula edodes |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.3 | 25 | 50 | - |
Lentinula edodes |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.3 | 50 | - |
recombinant enzyme, stable up to, stability is enhanced by Ca2+ | Lentinula edodes |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.3 | 4.6 | - |
- |
Lentinula edodes |