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Literature summary extracted from
- Purification and biochemical characterization of a novel mesophilic glucoamylase from Aspergillus tritici WZ99 (2018), Int. J. Biol. Macromol., 107, 1122-1130 .
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.3 | additional information | EDTA and Na2EDTA do not affect the enzyme activity | Aspergillus tritici |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.2.1.3 | DNA and amino acid sequence determination and analysis, sequence comparisons | Aspergillus tritici |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.3 | Fe2+ | activates at 1-5 mM, inhibits at 10 mM | Aspergillus tritici |  |
| 3.2.1.3 | Fe3+ | activates at 1-5 mM, inhibits at 10 mM | Aspergillus tritici | |
| 3.2.1.3 | additional information | EDTA and Na2EDTA do not affect the enzyme activity | Aspergillus tritici |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.2.1.3 | additional information | - |
additional information | Michaelis-Menten kinetics, Km and Vmax of the glucoamylase are calculated as 15.02 g/l and 81.13 U/mg, pH 5.0, 45°C | Aspergillus tritici |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.2.1.3 | extracellular | - |
Aspergillus tritici | - |
- |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.3 | Co2+ | activates at 1-10 mM | Aspergillus tritici | |
| 3.2.1.3 | Fe2+ | activates at 1-5 mM, inhibits at 10 mM | Aspergillus tritici | |
| 3.2.1.3 | Fe3+ | activates at 1-5 mM, inhibits at 10 mM | Aspergillus tritici | |
| 3.2.1.3 | Mn2+ | activates at 1-10 mM | Aspergillus tritici | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.3 | starch + H2O | Aspergillus tritici | - |
? | - |
? | |
| 3.2.1.3 | starch + H2O | Aspergillus tritici CGMCC 3.15694.3.2 | - |
? | - |
? | |
| 3.2.1.3 | starch + H2O | Aspergillus tritici WZ99 | - |
? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.3 | Aspergillus tritici | A0A1S6XZP1 | isolated from environmental samples collected in the suburbs of Wuzhou City (Guangxi Zhuang Autonomous Region,China) from decaying foods, rotten agriculture crops and nonfood plant tissues, and soils | - |
| 3.2.1.3 | Aspergillus tritici CGMCC 3.15694.3.2 | A0A1S6XZP1 | isolated from environmental samples collected in the suburbs of Wuzhou City (Guangxi Zhuang Autonomous Region,China) from decaying foods, rotten agriculture crops and nonfood plant tissues, and soils | - |
| 3.2.1.3 | Aspergillus tritici WZ99 | A0A1S6XZP1 | isolated from environmental samples collected in the suburbs of Wuzhou City (Guangxi Zhuang Autonomous Region,China) from decaying foods, rotten agriculture crops and nonfood plant tissues, and soils | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.2.1.3 | native extracellular enzyme 53.64fold by ammonium sulfate fractionation, hydrophobic interaction chromatography, ion exchange chromatography, and native PAGE | Aspergillus tritici |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 3.2.1.3 | (alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose | the enzyme from Aspergillus tritici strain WZ99 degrades alpha-1,4 glucoside linkages faster than alpha-1,6 glucoside linkages | Aspergillus tritici |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.3 | 18.73 | - |
substrate pullalan, pH 5.0, 45°C | Aspergillus tritici |
| 3.2.1.3 | 30.14 | - |
substrate soluble potato starch, pH 5.0, 45°C | Aspergillus tritici |
| 3.2.1.3 | 34.3 | - |
substrate amylose, pH 5.0, 45°C | Aspergillus tritici |
| 3.2.1.3 | 36.73 | - |
substrate amylopectin, pH 5.0, 45°C | Aspergillus tritici |
| 3.2.1.3 | 39.64 | - |
substrate soluble wheat starch, pH 5.0, 45°C | Aspergillus tritici |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.3 | amylopectin + H2O | - |
Aspergillus tritici | ? | - |
? | |
| 3.2.1.3 | amylose + H2O | - |
Aspergillus tritici | ? | - |
? | |
| 3.2.1.3 | amylose + H2O | - |
Aspergillus tritici CGMCC 3.15694.3.2 | ? | - |
? | |
| 3.2.1.3 | amylose + H2O | - |
Aspergillus tritici WZ99 | ? | - |
? | |
| 3.2.1.3 | additional information | the strain WZ99 glucoamylase shows a substrate bias of soluble starch > pullulan > cycledextrin. The enzyme degrades alpha-1,4 glucoside linkages faster than alpha-1,6 glucoside linkages | Aspergillus tritici | ? | - |
? | |
| 3.2.1.3 | additional information | the strain WZ99 glucoamylase shows a substrate bias of soluble starch > pullulan > cycledextrin. The enzyme degrades alpha-1,4 glucoside linkages faster than alpha-1,6 glucoside linkages | Aspergillus tritici CGMCC 3.15694.3.2 | ? | - |
? | |
| 3.2.1.3 | additional information | the strain WZ99 glucoamylase shows a substrate bias of soluble starch > pullulan > cycledextrin. The enzyme degrades alpha-1,4 glucoside linkages faster than alpha-1,6 glucoside linkages | Aspergillus tritici WZ99 | ? | - |
? | |
| 3.2.1.3 | pullulan + H2O | low activity | Aspergillus tritici | ? | - |
? | |
| 3.2.1.3 | pullulan + H2O | low activity | Aspergillus tritici CGMCC 3.15694.3.2 | ? | - |
? | |
| 3.2.1.3 | pullulan + H2O | low activity | Aspergillus tritici WZ99 | ? | - |
? | |
| 3.2.1.3 | starch + H2O | - |
Aspergillus tritici | ? | - |
? | |
| 3.2.1.3 | starch + H2O | standard assay substrate is soluble corn starch. Highest specific activity toward soluble wheat starch and lowest specific activity toward soluble potato starch | Aspergillus tritici | ? | - |
? | |
| 3.2.1.3 | starch + H2O | - |
Aspergillus tritici CGMCC 3.15694.3.2 | ? | - |
? | |
| 3.2.1.3 | starch + H2O | standard assay substrate is soluble corn starch. Highest specific activity toward soluble wheat starch and lowest specific activity toward soluble potato starch | Aspergillus tritici CGMCC 3.15694.3.2 | ? | - |
? | |
| 3.2.1.3 | starch + H2O | - |
Aspergillus tritici WZ99 | ? | - |
? | |
| 3.2.1.3 | starch + H2O | standard assay substrate is soluble corn starch. Highest specific activity toward soluble wheat starch and lowest specific activity toward soluble potato starch | Aspergillus tritici WZ99 | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.2.1.3 | ? | x * 51000, extracellular enzyme, SDS-PAGE | Aspergillus tritici |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.2.1.3 | AtriGA15A | - |
Aspergillus tritici |
| 3.2.1.3 | glucoamylase | - |
Aspergillus tritici |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.3 | 45 | - |
- |
Aspergillus tritici |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.3 | 30 | 55 | over 50% of maximal activity at 30-55°C | Aspergillus tritici |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.3 | 40 | - |
purified extracellular enzyme, pH 5.0, 1 h, stable up to | Aspergillus tritici |
| 3.2.1.3 | 50 | - |
purified extracellular enzyme, pH 5.0, 1 h, loss of 50% activity | Aspergillus tritici |
| 3.2.1.3 | 60 | - |
purified extracellular enzyme, pH 5.0, 1 h, inactivation | Aspergillus tritici |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.2.1.3 | 67.15 | - |
starch | pH 5.0, 45°C | Aspergillus tritici | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.3 | 4.5 | 5 | - |
Aspergillus tritici |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.3 | 3.5 | 10.5 | 85% of maximal activity at pH 4.0-10.0, and 70% of maximal activity at pH 3.5 and 75% at pH 10.5, respectively | Aspergillus tritici |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.3 | 4.5 | 10 | purified extracellular enzyme, 4°C, stable at | Aspergillus tritici |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.2.1.3 | evolution | the glucoamylase contains a catalytic domain belonging to glycosyl hydrolase family 15, GH15 | Aspergillus tritici |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.2.1.3 | additional information | - |
additional information | Kcat/Km value is calculated as 4.47 l/g/s | Aspergillus tritici |
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