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Literature summary for 2.4.1.18 extracted from

  • Boyer, L.; Roussel, X.; Courseaux, A.; Ndjindji, O.; Lancelon-Pin, C.; Putaux, J.; Tetlow, I.; Emes, M.; Pontoire, B.; D Hulst, C.; Wattebled, F.
    Expression of Escherichia coli glycogen branching enzyme in an Arabidopsis mutant devoid of endogenous starch branching enzymes induces the synthesis of starch-like polyglucans (2016), Plant Cell Environ., 39, 1432-1447.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene glgB, functional recombinant expression of the bacterial enzyme in Arabidopsis thaliana be2 be3 double mutant leaves, ecotype WS, which is devoid of BE activity and consequently free of starch. The synthesis of a water-insoluble, partly crystalline, amylose-containing starch-like polyglucan is restored in GlgB-expressing transgenic plants, morphology of purified insoluble and soluble polyglucans, phenotype, overview Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P07762 gene glgB
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Synonyms

Synonyms Comment Organism
GlgB
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Escherichia coli
glycogen branching enzyme
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Escherichia coli

General Information

General Information Comment Organism
metabolism the balance between branching and debranching is crucial for the synthesis of starch, as an excess of branching activity results in the formation of highly branched, water-soluble, poorly crystalline polyglucan Escherichia coli
additional information the branching enzyme's origin has only a limited impact on establishing essential characteristics of starch Escherichia coli
physiological function starch synthesis requires several enzymatic activities including branching enzymes (BEs) responsible for the formation of alpha(1->6) linkages. Distribution and number of these linkages are further controlled by debranching enzymes that cleave some of them, rendering the polyglucan water-insoluble and semi-crystalline. The activity of BEs and debranching enzymes is mandatory to sustain normal starch synthesis Escherichia coli