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Literature summary for 3.2.1.3 extracted from
- Heterologous, expression, and characterization of thermostable glucoamylase derived from Aspergillus flavus NSH9 in Pichia pastoris (2016), BioMed Res. Int., 2016, 5962028 .
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | activates at above 5 mM | Aspergillus flavus |  |
| Cu2+ | activates at 1 mM, inhibits at above 5 mM | Aspergillus flavus | |
| Fe2+ | activates at 1 mM | Aspergillus flavus | |
| Mg2+ | activates at 1 mM | Aspergillus flavus | |
| Pb2+ | activates at 1 mM, inhibits at above 5 mM | Aspergillus flavus | |
| Zn2+ | activates at 1 mM, inhibits at above 5 mM | Aspergillus flavus | |
Application
| Application | Comment | Organism |
|---|---|---|
| food industry | glucoamylase is an important group of enzymes in starch processing in the food industries, as it is used for the production of glucose and fructose syrup from liquefied starch | Aspergillus flavus |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene GAA, DNA and amino acid sequence determination and analysis, phylogenic tree, the N-terminal 17 amino acids are presumed to be a signal peptide, recombinant methanol-induced expression of FLAG-tagged enzyme in Pichia pastoris strain GS115 | Aspergillus flavus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Cu2+ | activates at above 1 mM, inhibits at above 5 mM | Aspergillus flavus | |
| Na+ | at above 5 mM | Aspergillus flavus | |
| Pb2+ | activates at above 1 mM, inhibits at above 5 mM | Aspergillus flavus | |
| Zn2+ | activates at above 1 mM, inhibits at above 5 mM | Aspergillus flavus | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| additional information | the N-terminal 17 amino acids are presumed to be a signal peptide | Aspergillus flavus | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| additional information | metal ions, such as Na+, K+, Ca2+ and Cd2+, have no significant effect on the recombinant glucoamylase activity at concentration of 1 mM | Aspergillus flavus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Aspergillus flavus | glucoamylase is an exo-acting enzyme that yields beta-D-glucose from the nonreducing ends of starch and related oligo- and polysaccharide chains by hydrolyzing alpha-1,4 and alpha-1,6 linkages. The enzyme is able to completely hydrolyze starch if incubated for extended periods of time and hence called the saccharifying enzyme | ? | - |
? | |
| additional information | Aspergillus flavus NSH9 | glucoamylase is an exo-acting enzyme that yields beta-D-glucose from the nonreducing ends of starch and related oligo- and polysaccharide chains by hydrolyzing alpha-1,4 and alpha-1,6 linkages. The enzyme is able to completely hydrolyze starch if incubated for extended periods of time and hence called the saccharifying enzyme | ? | - |
? | |
| starch + H2O | Aspergillus flavus | - |
? | - |
? | |
| starch + H2O | Aspergillus flavus NSH9 | - |
? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus flavus | A0A166HLT6 | - |
- |
| Aspergillus flavus NSH9 | A0A166HLT6 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| amylopectin | - |
Aspergillus flavus | ? | - |
? | |
| amylopectin | - |
Aspergillus flavus NSH9 | ? | - |
? | |
| glycogen + H2O | lower activity | Aspergillus flavus | ? | - |
? | |
| glycogen + H2O | lower activity | Aspergillus flavus NSH9 | ? | - |
? | |
| additional information | glucoamylase is an exo-acting enzyme that yields beta-D-glucose from the nonreducing ends of starch and related oligo- and polysaccharide chains by hydrolyzing alpha-1,4 and alpha-1,6 linkages. The enzyme is able to completely hydrolyze starch if incubated for extended periods of time and hence called the saccharifying enzyme | Aspergillus flavus | ? | - |
? | |
| additional information | glucoamylase is an exo-acting enzyme that yields beta-D-glucose from the nonreducing ends of starch and related oligo- and polysaccharide chains by hydrolyzing alpha-1,4 and alpha-1,6 linkages. The enzyme is able to completely hydrolyze starch if incubated for extended periods of time and hence called the saccharifying enzyme | Aspergillus flavus NSH9 | ? | - |
? | |
| starch + H2O | - |
Aspergillus flavus | ? | - |
? | |
| starch + H2O | best substrate, soluble starch and gelatinized raw sago starch | Aspergillus flavus | ? | - |
? | |
| starch + H2O | - |
Aspergillus flavus NSH9 | ? | - |
? | |
| starch + H2O | best substrate, soluble starch and gelatinized raw sago starch | Aspergillus flavus NSH9 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 78000, recombinant enzyme, SDS-PAGE, x * 55100, about, recombinant enzyme, sequence calculation | Aspergillus flavus |
| More | the enzyme from Aspergillus flavus strain NSH9 contains no starch binding domain (SBD) | Aspergillus flavus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 1,4-alpha-D-glucan glucohydrolase | - |
Aspergillus flavus |
| glucoamylase | - |
Aspergillus flavus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | - |
recombinant enzyme | Aspergillus flavus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 3.5 | 8 | activity range, profile overview | Aspergillus flavus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
purified recombinant enzyme, pH 5.0, stable for 15 min, loss of 20% activity after 30 min, and of 50% after 45 min, 12% activity remains after 90 min, inactivation after 120 min | Aspergillus flavus |
| 80 | - |
purified recombinant enzyme, pH 5.0, loss of 8% activity after 15 min, loss of 20% activity after 30 min, and of 75% after 45 min, 3% activity remains after 75 min, inactivation after 90 min | Aspergillus flavus |
| 90 | - |
purified recombinant enzyme, pH 5.0, loss of 12% activity after 15 min, loss of 75% activity after 30 min, and of 85% after 45 min, inactivation after 75 min | Aspergillus flavus |
| 100 | - |
purified recombinant enzyme, pH 5.0, loss of 43% activity after 15 min, loss of 80% activity after 30 min, and of 88% after 45 min, inactivation after 60 min | Aspergillus flavus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | - |
recombinant enzyme | Aspergillus flavus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 3.5 | 8 | activity range, profile overview | Aspergillus flavus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | the thermostable glucoamylase from Aspergillus flavus strain NSH9 contains no starch binding domain (SBD) | Aspergillus flavus |
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