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Literature summary 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.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.18 expression in Escherichia coli Zea mays
2.4.1.21 expression in Escherichia coli Zea mays

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.4.1.18 amyloplast
-
Zea mays 9501
-
2.4.1.21 amyloplast
-
Zea mays 9501
-

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.18 Zea mays
-
-
-
2.4.1.21 Zea mays
-
-
-

Subunits

EC Number Subunits Comment Organism
2.4.1.18 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
2.4.1.21 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

EC Number General Information Comment Organism
2.4.1.18 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
2.4.1.21 metabolism granule-bound proteins involved in amylopectin synthesis are partitioned into the starch granule as a result of their association within protein complexes, and starch 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 unable to bind to starch additionally leads to greatly reduced activities of starch synthase I and starch branching enzyme IIb Zea mays