Literature summary for 2.4.1.18 extracted from

Liu, F.; Romanova, N.; Lee, E.A.; Ahmed, R.; Evans, M.; Gilbert, E.P.; Morell, M.K.; Emes, M.J.; Tetlow, I.J.
Glucan affinity of starch synthase IIa determines binding of starch synthase I and starch branching enzyme IIb to starch granules (2012), Biochem. J., 448, 373-387.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Zea mays

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
amyloplast	-	Zea mays	9501	-

Organism

Organism	UniProt	Comment	Textmining
Zea mays	-	-	-

Subunits

Subunits	Comment	Organism
More	isoform IIb assembles to trimer with starch synthase I and starch synthase IIa. Starch synthase IIa is at the core of the complex, interacting with starch synthase I and starch branching enzyme IIb, which do not interact directly with each other	Zea mays

General Information

General Information	Comment	Organism
metabolism	granule-bound proteins involved in amylopectin synthesis are partitioned into the starch granule as a result of their association within protein complexes, and strach synthase IIa plays a crucial role in trafficking starch synthase I and starch branching enzyme IIb into the granule matrix. A mutant starch synthase IIa that has lost catalytic activity and is inable to bind to starch additionally leads to greatly reduced activities of starch synthase I and starch branching enzyme IIb	Zea mays

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Release 2023.1 (January 2023)