Literature summary for 2.4.1.21 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.

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Cloned(Commentary)

Cloned (Comment)	Organism
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

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	F4IAG2	var. Columbia Col-0	-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	-	?

Synonyms

Synonyms	Comment	Organism
SSIII	-	Arabidopsis thaliana
starch synthase III	-	Arabidopsis thaliana

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Release 2023.1 (January 2023)