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Article

Multi-site substrate binding and interplay in barley alpha-amylase 1.

FEBS letters - 23 Jul 2008

Nielsen Morten Munch, Seo Eun-Seong, Bozonnet Sophie, Aghajari Nushin, Robert Xavier, Haser Richard, Svensson Birte

Abstract excerpt

Certain starch hydrolases possess secondary carbohydrate binding sites outside of the active site, suggesting that multi-site substrate interactions are functionally significant. In barley alpha-amylase both Tyr380, situated on a remote non-catalytic domain, and Tyr105 in subsite -6 of the active site cleft are principal carbohydrate binding residues. The dual active site/secondary site mutants Y105A/Y380A and...

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PMID: 18588886
DOI: 10.1016/j.febslet.2008.06.027

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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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