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Structure of the catalytic domain of glucoamylase from Aspergillus niger.


ABSTRACT: Glucoamylase from Aspergillus niger is an industrially important biocatalyst that is utilized in the mass production of glucose from raw starch or soluble oligosaccharides. The G1 isoform consists of a catalytic domain and a starch-binding domain connected by a heavily glycosylated linker region. The amino-terminal catalytic domain of the G1 isoform generated by subtilisin cleavage has been crystallized at pH 8.5, which is a significantly higher pH condition than used for previously characterized glucoamylase crystals. The refined structure at 1.9 Å resolution reveals the active site of the enzyme in complex with both Tris and glycerol molecules. The ligands display both unique and analogous interactions with the substrate-binding site when compared with previous structures of homologous enzymes bound to inhibitors.

SUBMITTER: Lee J 

PROVIDER: S-EPMC3034606 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature

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Structure of the catalytic domain of glucoamylase from Aspergillus niger.

Lee Jaeyong J   Paetzel Mark M  

Acta crystallographica. Section F, Structural biology and crystallization communications 20110121 Pt 2


Glucoamylase from Aspergillus niger is an industrially important biocatalyst that is utilized in the mass production of glucose from raw starch or soluble oligosaccharides. The G1 isoform consists of a catalytic domain and a starch-binding domain connected by a heavily glycosylated linker region. The amino-terminal catalytic domain of the G1 isoform generated by subtilisin cleavage has been crystallized at pH 8.5, which is a significantly higher pH condition than used for previously characterize  ...[more]

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