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Phylogenetic analysis reveals key residues in substrate hydrolysis in the isomaltase domain of sucrase-isomaltase and its role in starch digestion.

Marcia M Chaudet | Mahdi Amiri | Nathalie Marth | Hassan Y Naim | David R Rose
Biochimica et biophysica acta. General subjects | 2019

Starch constitutes one of the main sources of nutrition in the human diet and is broken down through a number of stages of digestion. Small intestinal breakdown of starch-derived substrates occurs through the mechanisms of small intestinal brush border enzymes, maltase-glucoamylase and sucrase-isomaltase. These enzymes each contain two functional enzymatic domains, and though they share sequence and structural similarities due to their evolutionary conservation, they demonstrate distinct substrate preferences and catalytic efficiency. The N-terminal isomaltase domain of sucrase-isomaltase has a unique ability to actively hydrolyze isomaltose substrates in contrast to the sucrase, maltase and glucoamylase enzymes.

Pubmed ID: 31254546

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COS-1 (tool)

RRID:CVCL_0223

Cell line COS-1 is a Transformed cell line with a species of origin Chlorocebus aethiops (Green monkey)

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