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Literature summary for 3.2.1.26 extracted from

  • Tamoi, M.; Tabuchi, T.; Demuratani, M.; Otori, K.; Tanabe, N.; Maruta, T.; Shigeoka, S.
    Point mutation of a plastidic invertase inhibits development of the photosynthetic apparatus and enhances nitrate assimilation in sugar-treated Arabidopsis seedlings (2010), J. Biol. Chem., 285, 15399-15407.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
C294Y i.e. mutant sicy-192. Mutation leads to inhibition of cotyledon greening by treatments with sugars such as sucrose, glucose, and fructose. The greening of cotyledons in the knock-out INV-E lines is not inhibited by treatment with the sugars. A recombinant INV-E:C294Y protein has the same enzymatic activity as a recombinant INV-E protein, suggesting that the Cys-294 residue of INV-E is important for its functions in the chloroplasts. On treatment with sucrose, the expression of photosynthesis-related genes is weaker in seedlings of mutant plants than wild-type seedlings, whereas the activity of nitrate reductase is stronger in the mutant plants than wild-type plants Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
cotyledon
-
Arabidopsis thaliana
-

Synonyms

Synonyms Comment Organism
INV-E
-
Arabidopsis thaliana

General Information

General Information Comment Organism
physiological function INV-E is associated with the development of the photosynthetic apparatus and the assimilation of nitrogen in Arabidopsis seedlings to control the ratio of sucrose content to hexose content Arabidopsis thaliana