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Literature summary for 2.4.1.18 extracted from

  • Nakamura, Y.; Ono, M.; Utsumi, C.; Steup, M.
    Functional interaction between plastidial starch phosphorylase and starch branching enzymes from rice during the synthesis of branched maltodextrins (2012), Plant Cell Physiol., 53, 869-878.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Oryza sativa
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General Information

General Information Comment Organism
physiological function the synthesis of maltodextrins by alpha-glucan phosphorylase Pho1 is markedly accelerated by branching enzyme isozymes, with the greatest effect being exhibited by the presence of branching isozyme BEI rather than by isozyme BEIIa or isozyme BEIIb. The enhancement of the activity of Pho1 by branching enzymes is not merely due to the supply of a non-reducing ends. At the same time, Pho1 greatly enhances the branching enzyme activity, possibly by generating a branched carbohydrate substrate which is used by branching enzyme with a higher affinity. The interaction between Pho1 and branching enzyme is not merely due to chain-elongating and chain-branching reactions, but occurs in a physically and catalytically synergistic manner by each activating the mutual capacity of the other, presumably forming a physical association of Pho1, isoform BEI and branched maltodextrins Oryza sativa