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Article

Stability and function of interdomain linker variants of glucoamylase 1 from Aspergillus niger.

Biochemistry - 7 Aug 2001

Sauer J, Christensen T, Frandsen T P, Mirgorodskaya E, McGuire K A, Driguez H, Roepstorff P, Sigurskjold B W, Svensson B

Abstract excerpt

Several variants of glucoamylase 1 (GA1) from Aspergillus niger were created in which the highly O-glycosylated peptide (aa 468--508) connecting the (alpha/alpha)(6)-barrel catalytic domain and the starch binding domain was substituted at the gene level by equivalent segments of glucoamylases from Hormoconis resinae, Humicola grisea, and Rhizopus oryzae encoding 5, 19, and 36 amino acid residues. Variants were...

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PMID: 11478902
DOI: 10.1021/bi010515i

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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