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Literature summary extracted from

  • Jorgensen, A.D.; Nohr, J.; Kastrup, J.S.; Gajhede, M.; Sigurskjold, B.W.; Sauer, J.; Svergun, D.I.; Svensson, B.; Vestergaard, B.
    Small angle X-ray studies reveal that Aspergillus niger glucoamylase has a defined extended conformation and can form dimers in solution (2008), J. Biol. Chem., 283, 14772-14780.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.3
-
 Aspergillus niger

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.3 additional information engineered low-glycosylated variant of glucoamylase 1 with a short linker, low-glycosylated GA1 (dgGA). Low-glycosylated linker variant of GA1; GA1:L0 and dgGA:L0 Aspergillus niger

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.3 additional information binding of a short heterobidentate inhibitor simultaneously directed toward the catalytic and starch binding domains causes dimerization of glucoamylase and not, an intramolecular conformational rearrangement mediated by linker flexibility Aspergillus niger

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.3 62000
-
 experimental molecular weight for low-glycosylated linker variant dgGA Aspergillus niger
3.2.1.3 68000
-
 experimental molecular weight for glucoamylase 2, excellent agreement with the theoretical value Aspergillus niger
3.2.1.3 70000
-
 calculated molecular weight for low-glycosylated linker variant dgGA Aspergillus niger
3.2.1.3 73000
-
 calculated molecular weight for dgGA:L0 Aspergillus niger
3.2.1.3 73000
-
 experimental molecular weight for glucoamylase1 Aspergillus niger
3.2.1.3 82000
-
 calculated molecular weight for glucoamylase1 Aspergillus niger
3.2.1.3 85000
-
 calculated molecular weight for GA1:L0 Aspergillus niger
3.2.1.3 90000
-
 experimental molecular weight for dgGA:L0 Aspergillus niger
3.2.1.3 94000
-
 experimental molecular weight for GA1:L0 Aspergillus niger

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.3 additional information Aspergillus niger glucoamylase functions via transient dimer formation during hydrolysis of insoluble substrates and address the question of the cooperative effect of starch binding and hydrolysis ?
-
 ?

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
-
 Aspergillus niger

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.3
-
 Aspergillus niger

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.3 additional information glucoamylase functions via transient dimer formation during hydrolysis of insoluble substrates and address the question of the cooperative effect of starch binding and hydrolysis Aspergillus niger ?
-
 ?
3.2.1.3 starch + H2O
-
 Aspergillus niger ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.3 dimer complex formation with a heterobidentate ligand induces dimerization Aspergillus niger
3.2.1.3 monomer a starch binding and a catalytic domain interspersed by a highly glycosylated polypeptide linker Aspergillus niger

Synonyms

EC Number Synonyms Comment Organism
3.2.1.3 GA1
-
 Aspergillus niger
3.2.1.3 GA2
-
 Aspergillus niger
3.2.1.3 glucoamylase
-
 Aspergillus niger
3.2.1.3 glucoamylase 1
-
 Aspergillus niger
3.2.1.3 glucoamylase 2 lacks a starch binding domain Aspergillus niger