EC Number   |
General Information |
Reference |
|---|
    3.2.1.3 | evolution |
the enzyme belongs to the glycosyl hydrolase family 15, GH15 |
-, 750105, 750142 |
| 3.2.1.3 | evolution |
the enzyme belongs to the superfamily of CBM 20, phylogenetic tree |
-, 750762 |
| 3.2.1.3 | evolution |
the enzyme is a member of the glycoside hydrolase family 15 (GH15) |
-, 749503 |
| 3.2.1.3 | evolution |
the glucoamylase contains a catalytic domain belonging to glycosyl hydrolase family 15, GH15 |
-, 750771 |
| 3.2.1.3 | malfunction |
the starch-binding domain (SBD) deletion analysis reveals that SBD plays a very important role in raw starch hydrolysis by the enzyme PoGA15A |
-, 750142 |
| 3.2.1.3 | metabolism |
dynamic metabolic response of Aspergillus niger to glucose perturbation, regulatory mechanism for reduced glucoamylase production. Reduction of the total adenine nucleotides and major precursor amino acids indicate the upregulated RNA synthesis is required to produce stress proteins, and partially explains the drop of glucoamylase production when Aspergillus niger experiences a fluctuated glucose concentration environment, adenine nucleotides dynamic concentration profiles, overview |
751164 |
| 3.2.1.3 | more |
enzyme structure modelling and comparison of the structural model of Tetracladium sp. glucoamylase with the solved structure of the Hypocrea jecorina glucoamylase |
751479 |
| 3.2.1.3 | more |
the relative orientation between the carbohydrate-binding domain (CBM) and the catalytic domain is flexible, as the domains can adopt different orientations independently of ligand binding, suggesting a role as an anchor to increase the contact time and the relative concentration of substrate near the active site. The C-terminal CBM adopts the well known beta-sandwich motif, which is a hallmark of carbohydrate-binding modules |
-, 749503 |
| 3.2.1.3 | more |
the relative orientation between the carbohydrate-binding domain (CBM) and the catalytic domain is flexible, as the domains can adopt different orientations independently of ligand binding, suggesting a role as an anchor to increase the contact time and the relative concentration of substrate near the active site. The model of enzyme HrGA with two molecules in the asymmetric unit includes residues 29-616 and up to seven N-glycosylation sites and has acarbose bound in the active site. The C-terminal CBM adopts the well known beta-sandwich motif, which is a hallmark of carbohydrate-binding modules |
749503 |
| 3.2.1.3 | more |
the replacement of native beta-glucosidase Bgl1 signal peptide by that of Sta1, SPS-Bgl1, increases the production of the enzyme by about threefold without affecting the ratio between the values of activity associated to cells and free in the medium |
-, 717130 |
