Literature summary for 3.2.1.3 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

Application	Comment	Organism
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)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
60000	-	x * 60000, SDS-PAGE	Aspergillus niger

Organism

Organism	UniProt	Comment	Textmining
Aspergillus niger	P69328	G1 isoform	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
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

Subunits	Comment	Organism
?	x * 60000, SDS-PAGE	Aspergillus niger
More	the G1 isoform consists of a catalytic domain and a starch-binding domain connected by a heavily glycosylated linker region	Aspergillus niger

Synonyms

Synonyms	Comment	Organism
glucoamylase	-	Aspergillus niger

General Information

General Information	Comment	Organism
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