EC Number | Cloned (Comment) | Organism |
---|---|---|
3.2.1.3 | - |
Aspergillus niger |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.2.1.3 | 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 |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.2.1.3 | 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 |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.2.1.3 | 62000 | - |
experimental molecular weight for low-glycosylated linker variant dgGA | Aspergillus niger |
3.2.1.3 | 68000 | - |
experimental molecular weight for glucoamylase 2, excellent agreement with the theoretical value | Aspergillus niger |
3.2.1.3 | 70000 | - |
calculated molecular weight for low-glycosylated linker variant dgGA | Aspergillus niger |
3.2.1.3 | 73000 | - |
calculated molecular weight for dgGA:L0 | Aspergillus niger |
3.2.1.3 | 73000 | - |
experimental molecular weight for glucoamylase1 | Aspergillus niger |
3.2.1.3 | 82000 | - |
calculated molecular weight for glucoamylase1 | Aspergillus niger |
3.2.1.3 | 85000 | - |
calculated molecular weight for GA1:L0 | Aspergillus niger |
3.2.1.3 | 90000 | - |
experimental molecular weight for dgGA:L0 | Aspergillus niger |
3.2.1.3 | 94000 | - |
experimental molecular weight for GA1:L0 | Aspergillus niger |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.3 | 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 | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.3 | Aspergillus niger | - |
- |
- |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
3.2.1.3 | glycoprotein | - |
Aspergillus niger |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.2.1.3 | - |
Aspergillus niger |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.3 | 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 | ? | - |
? | |
3.2.1.3 | starch + H2O | - |
Aspergillus niger | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.2.1.3 | dimer | complex formation with a heterobidentate ligand induces dimerization | Aspergillus niger |
3.2.1.3 | monomer | a starch binding and a catalytic domain interspersed by a highly glycosylated polypeptide linker | Aspergillus niger |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.3 | GA1 | - |
Aspergillus niger |
3.2.1.3 | GA2 | - |
Aspergillus niger |
3.2.1.3 | glucoamylase | - |
Aspergillus niger |
3.2.1.3 | glucoamylase 1 | - |
Aspergillus niger |
3.2.1.3 | glucoamylase 2 | lacks a starch binding domain | Aspergillus niger |