Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.4.1.242 extracted from

  • Seung, D.; Soyk, S.; Coiro, M.; Maier, B.A.; Eicke, S.; Zeeman, S.C.
    PROTEIN TARGETING TO STARCH is required for localising GRANULE-BOUND STARCH SYNTHASE to starch granules and for normal amylose synthesis in Arabidopsis (2015), PLoS Biol., 13, e1002080.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.4.1.242

Activating Compound

Activating Compound Comment Organism Structure
protein targeting to starch PTST protein targeting to starch, PTST, is required for localising granule-bound starch synthase to starch granules and for normal amylose synthesis. PTST is a plastidial protein possessing an N-terminal coiled coil domain and a C-terminal carbohydrate binding module. Enzyme GBSS physically interacts with protein PTST via a coiled coil. The CBM48 domain of PTST, which mediates its interaction with starch granules, is also required for correct GBSS localisation Arabidopsis thaliana

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of C-terminally HA and cyan fluorescent protein (CFP) tandem tagged wild-type nd mutant enzymes in Arabidopsis thaliana leaves via Agrobactrium tumefaciens transformation and in Nicotiana tabacum epidermal cells. Wild-type GBSS enzyme is only detected in the immunoprecipitate when TAP-tagged PTST is coexpressed, confirming the protein-protein interaction Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
additional information protein targeting to starch, PTST, is required for localising granule-bound starch synthase to starch granules and for normal amylose synthesis. PTST is a plastidial protein possessing an N-terminal coiled coil domain and a C-terminal carbohydrate binding module, the CBM domain of PTST, which mediates its interaction with starch granules, is required for correct enzyme GBSS localisation. PTST remains in the stroma impliing that it interacts only transiently with starch during the GBSS localisation Arabidopsis thaliana
-
-
plastid mutation of the carbohydrate binding module of plastidial protein PTST causes GBSS to remain in the plastid stroma Arabidopsis thaliana 9536
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ADP-glucose + (1,4-alpha-D-glucosyl)n Arabidopsis thaliana
-
 ADP + (1,4-alpha-D-glucosyl)n+1
-
 ?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-
Arabidopsis thaliana Q9MAQ0
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP-glucose + (1,4-alpha-D-glucosyl)n
-
 Arabidopsis thaliana ADP + (1,4-alpha-D-glucosyl)n+1
-
 ?

Synonyms

Synonyms Comment Organism
GBSS
-
 Arabidopsis thaliana
granule-bound starch synthase
-
 Arabidopsis thaliana

General Information

General Information Comment Organism
malfunction Arabidopsis thaliana ptst mutants synthesise amylose-free starch and are phenotypically similar to mutants lacking GBSS. Mutation of the CBM domain of PTST causes GBSS to remain in the plastid stroma Arabidopsis thaliana
physiological function Arabidopsis thaliana mutants lacking plastidial protein PTST synthesise amylose-free starch and are phenotypically similar to mutants lacking granule-bound starch synthase GBSS. PTST mutant starch granules show a dramatic reduction of GBSS protein. GBSS physically interacts with PTST via a coiled coil. The carbohydrate binding module of PTST, which mediates its interaction with starch granules, is also required for correct GBSS localisation. Arabidopsis GBSS requires the presence of Arabidopsis PTST to localise to starch granules. Mutation of the carbohydrate binding module of PTST causes GBSS to remain in the plastid stroma Arabidopsis thaliana