Literature summary extracted from
Lee, J.; Paetzel, M.
Structure of the catalytic domain of glucoamylase from Aspergillus niger (2011), Acta Crystallogr. Sect. F, 67, 188-192.
Application
EC Number |
Application |
Comment |
Organism |
---|
3.2.1.3 |
industry |
glucoamylase from Aspergillus niger is an industrially important biocatalyst that is utilized in the mass production of glucose from raw starch or soluble oligosaccharides |
Aspergillus niger |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
3.2.1.3 |
purified isolated N-terminal catalytic domain of the G1 isoform, generated by subtilisin cleavage, sitting-drop vapour-diffusion method, 20 mg/ml protein at pH 8.5, 22°C room temperatur, the reservoir solution contains 50 mM Tris acetate, pH 8.5, 22.5% PEG 6000, 0.4 M sodium acetate and 10% glycerol, mixing of 0.001 ml protein and reservoir solution and equilibration against 1 ml reservoir solution, 2 weeks, X-ray diffraction structure determination and analysis at 1.9 A resolution, the active site of the enzyme is in complex with both Tris and glycerol molecules, structure modelling |
Aspergillus niger |
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
3.2.1.3 |
60000 |
- |
x * 60000, SDS-PAGE |
Aspergillus niger |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.2.1.3 |
Aspergillus niger |
P69328 |
G1 isoform |
- |
Posttranslational Modification
EC Number |
Posttranslational Modification |
Comment |
Organism |
---|
3.2.1.3 |
glycoprotein |
the linker region between starch-binding and catalytic domains is heavily glycosylated. The O-glycosylated residues are Ser467(443), Ser468(444), Thr476(452), Ser477(453), Ser483(459), Ser484(460) and Thr486(462) |
Aspergillus niger |
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
3.2.1.3 |
? |
x * 60000, SDS-PAGE |
Aspergillus niger |
3.2.1.3 |
More |
the G1 isoform consists of a catalytic domain and a starch-binding domain connected by a heavily glycosylated linker region |
Aspergillus niger |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
3.2.1.3 |
glucoamylase |
- |
Aspergillus niger |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
3.2.1.3 |
physiological function |
glucoamylase is an exoglucohydrolase that primarily catalyzes the hydrolysis of alpha-1,4 glycosidic linkages in raw starch and soluble oligosaccharides to generate beta-D-glucose |
Aspergillus niger |