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Literature summary extracted from

  • Jafari-Aghdam, J.; Khajeh, K.; Ranjbar, B.; Nemat-Gorgani, M.
    Deglycosylation of glucoamylase from Aspergillus niger: effects on structure, activity and stability (2005), Biochim. Biophys. Acta, 1750, 61-68.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.3 additional information the deglycosylated enzyme is more sensitive to proteolytic degradation by subtilisin than the native enzyme Aspergillus niger

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.3 1.1
-
 starch pH 4.8, 37°C, deglycosylated enzyme Aspergillus niger
3.2.1.3 1.2
-
 starch pH 4.8, 37°C, native enzyme Aspergillus niger

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.3 Aspergillus niger
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.3 glycoprotein effects of deglycosylation on enzyme structure, activity and stability, overview, deglycosylation by alpha-mannosidase does not affect the pH optimum or the active site and catalytic reaction mechanism including conformational changes of the enzyme, the secondary enzyme structure remains unaltered, deglycosylation increases the enzyme aggregation and reduces the thermal stability, the deglycosylated enzyme is more sensitive to proteolytic degradation by subtilisin than the native enzyme Aspergillus niger

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.3 commercial preparation
-
 Aspergillus niger
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.3 starch + H2O
-
 Aspergillus niger starch + beta-D-glucose
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.3 More structure-function relationship analysis Aspergillus niger

Synonyms

EC Number Synonyms Comment Organism
3.2.1.3 GA
-
 Aspergillus niger
3.2.1.3 glucoamylase
-
 Aspergillus niger

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.3 22
-
 assay at room temperature Aspergillus niger

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.3 additional information
-
 the deglycosylated enzyme shows a higher aggregation rate compared to the native enzyme dependent on pH and presence of divalent cations, e.g. Mg2+ or Ca2+ Aspergillus niger
3.2.1.3 60 80 the thermal stability at 70°C and other temperatures of the deglycosylated enzyme is reduced compared to the native enzyme Aspergillus niger

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.3 4.8
-
 native and deglycosylated enzyme Aspergillus niger

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.2.1.3 Aspergillus niger
-
 3.7 3.5