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Article

A single residue mutation abolishes attachment of the CBM26 starch-binding domain from Lactobacillus amylovorus alpha-amylase.

Journal of industrial microbiology & biotechnology - 1 Mar 2009

Rodríguez-Sanoja Romina, Oviedo N, Escalante L, Ruiz B, Sánchez S

Abstract excerpt

Starch is degraded by amylases that frequently have a modular structure composed of a catalytic domain and at least one non-catalytic domain that is involved in polysaccharide binding. The C-terminal domain from the Lactobacillus amylovorus alpha-amylase has an unusual architecture composed of five tandem starch-binding domains (SBDs). These domains belong to family 26 in the carbohydrate-binding modules (CBM)...

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Source

Identifiers

PMID: 19052787
DOI: 10.1007/s10295-008-0502-y

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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