Literature summary for 2.4.1.21 extracted from

Valdez, H.A.; Busi, M.V.; Wayllace, N.Z.; Parisi, G.; Ugalde, R.A.; Gomez-Casati, D.F.
Role of the N-terminal starch-binding domains in the kinetic properties of starch synthase III from Arabidopsis thaliana (2008), Biochemistry, 47, 3026-3032.

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Cloned(Commentary)

Cloned (Comment)	Organism
construction of recombinant full length and truncated isoforms of SSIII, lacking one, two, or three starch-binding domains, and recombinant proteins, containing three, two, or one starch-binding domains, to investigate the role of these domains in enzyme activity	Arabidopsis thaliana

Organism

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

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ADP-glucose + (1,4-alpha-D-glucosyl)n	SSIII uses preferentially ADP-glucose, although UDP-glucose can also be used as a sugar donor substrate. the N-terminal starch-binding domains have a regulatory role, showing a starch binding capacity and modulating the catalytic properties of SSIII	Arabidopsis thaliana	ADP + (1,4-alpha-D-glucosyl)n+1	-	?
UDP-glucose + (1,4-alpha-D-glucosyl)n	SSIII uses preferentially ADP-glucose, although UDP-glucose can also be used as a sugar donor substrate	Arabidopsis thaliana	UDP + (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)