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Literature summary for 3.2.1.3 extracted from
- Small angle X-ray studies reveal that Aspergillus niger glucoamylase has a defined extended conformation and can form dimers in solution (2008), J. Biol. Chem., 283, 14772-14780.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Aspergillus niger |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | engineered low-glycosylated variant of glucoamylase 1 with a short linker, low-glycosylated GA1 (dgGA). Low-glycosylated linker variant of GA1; GA1:L0 and dgGA:L0 | Aspergillus niger |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | binding of a short heterobidentate inhibitor simultaneously directed toward the catalytic and starch binding domains causes dimerization of glucoamylase and not, an intramolecular conformational rearrangement mediated by linker flexibility | Aspergillus niger |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 62000 | - |
experimental molecular weight for low-glycosylated linker variant dgGA | Aspergillus niger |
| 68000 | - |
experimental molecular weight for glucoamylase 2, excellent agreement with the theoretical value | Aspergillus niger |
| 70000 | - |
calculated molecular weight for low-glycosylated linker variant dgGA | Aspergillus niger |
| 73000 | - |
calculated molecular weight for dgGA:L0 | Aspergillus niger |
| 73000 | - |
experimental molecular weight for glucoamylase1 | Aspergillus niger |
| 82000 | - |
calculated molecular weight for glucoamylase1 | Aspergillus niger |
| 85000 | - |
calculated molecular weight for GA1:L0 | Aspergillus niger |
| 90000 | - |
experimental molecular weight for dgGA:L0 | Aspergillus niger |
| 94000 | - |
experimental molecular weight for GA1:L0 | Aspergillus niger |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Aspergillus niger | glucoamylase functions via transient dimer formation during hydrolysis of insoluble substrates and address the question of the cooperative effect of starch binding and hydrolysis | ? | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus niger | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | - |
Aspergillus niger |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Aspergillus niger |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | glucoamylase functions via transient dimer formation during hydrolysis of insoluble substrates and address the question of the cooperative effect of starch binding and hydrolysis | Aspergillus niger | ? | - |
? | |
| starch + H2O | - |
Aspergillus niger | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | complex formation with a heterobidentate ligand induces dimerization | Aspergillus niger |
| monomer | a starch binding and a catalytic domain interspersed by a highly glycosylated polypeptide linker | Aspergillus niger |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GA1 | - |
Aspergillus niger |
| GA2 | - |
Aspergillus niger |
| glucoamylase | - |
Aspergillus niger |
| glucoamylase 1 | - |
Aspergillus niger |
| glucoamylase 2 | lacks a starch binding domain | Aspergillus niger |
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Release 2023.1 (January 2023)
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