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Literature summary for 3.2.1.3 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
Search for more literature for 3.2.1.3

Inhibitors

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Aspergillus niger
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
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

Source Tissue Comment Organism Textmining
commercial preparation
-
 Aspergillus niger
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
More structure-function relationship analysis Aspergillus niger

Synonyms

Synonyms Comment Organism
GA
-
 Aspergillus niger
glucoamylase
-
 Aspergillus niger

Temperature Optimum [°C]

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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
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

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

pI Value

Organism Comment pI Value Maximum pI Value
Aspergillus niger
-
 3.7 3.5