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Literature summary for 2.4.1.21 extracted from
- Functional interactions between starch synthase III and isoamylase-type starch-debranching enzyme in maize endosperm (2012), Plant Physiol., 158, 679-692.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Zea mays | F2YI17 | isoform SSIII | - |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| endosperm | - |
Zea mays | - |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| dull1 | - |
Zea mays |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | double mutant endosperms which are affected in both isoform SSIII and ISA2, encoding a noncatalytic subunit of heteromeric isoamylase-type starch-debranching enzyme, are starch deficient and accumulate phytoglycogen. Despite lack of functional isa2, ISA1 homomeric enzyme complexes assemble in both double mutants and are enzymatically active in vitro. Thus, SSIII is required for normal starch crystallization and the prevention of phytoglycogen accumulation when the only isoamylase-type debranching activity present is ISA1 homomer, but not in the wild-type condition, when both ISA1 homomer and ISA1/ISA2 heteromer are present | Zea mays |
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Release 2023.1 (January 2023)
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