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Literature summary extracted from

  • Busi, M.V.; Palopoli, N.; Valdez, H.A.; Fornasari, M.S.; Wayllace, N.Z.; Gomez-Casati, D.F.; Parisi, G.; Ugalde, R.A.
    Functional and structural characterization of the catalytic domain of the starch synthase III from Arabidopsis thaliana (2008), Proteins, 70, 31-40.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.21 the catalytic C-terminal domain (SSIII-CD) of is cloned and expressed in Escherichia coli. SSIII-CD fully complements the production of glycogen by an Agrobacterium tumefaciens glycogen synthase null mutant, suggesting that this truncated isoform restores in vivo de novo synthesis of bacterial glycogen Arabidopsis thaliana

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.21 Arabidopsis thaliana F4IAG2 var. Columbia Col-0
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Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.21 recombinantly expressed catalytic C-terminal domain (SSIII-CD) Arabidopsis thaliana

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.21 ADP-glucose + (1,4-alpha-D-glucosyl)n recombinant SSIII-CD uses with more efficiency rabbit muscle glycogen than amylopectin as primer and displays a high apparent affinity for ADP-Glc Arabidopsis thaliana ADP + (1,4-alpha-D-glucosyl)n+1
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Synonyms

EC Number Synonyms Comment Organism
2.4.1.21 SSIII
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Arabidopsis thaliana
2.4.1.21 starch synthase III
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Arabidopsis thaliana