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Literature summary for 4.1.1.2 extracted from

  • Chakraborty, N.; Ghosh, R.; Ghosh, S.; Narula, K.; Tayal, R.; Datta, A.; Chakraborty, S.
    Reduction of oxalate levels in tomato fruit and consequent metabolic remodeling following overexpression of a fungal oxalate decarboxylase (2013), Plant Physiol., 162, 364-378.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene FvOXDC, recombinant expression in Solanum lycopersicum fruits under the control of a fruit-specific promoter E8.2 being active upon ethylene induction only in ripening fruits, via Agrobacterium tumefaciens-mediated transformation, OXDC is targeted to the cell vacuole in the transgenic fruits. The transgenic fruits show up to a 90% reduction in oxalate content, which correlates with concomitant increases in calcium, iron, and citrate, compared to wild-type fruits. Expression of OXDC affects neither CO2 assimilation rates nor results in any detectable morphological differences in the transgenic plants. OXDC-responsive proteins involved in metabolism and stress responses represent the most substantially up- and down-regulated categories, respectively, in the transgenic fruit, compared with those of wild-type plants, proteome analysis, overview Flammulina velutipes

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
oxalate + H+ Flammulina velutipes
-
formate + CO2
-
?

Organism

Organism UniProt Comment Textmining
Flammulina velutipes
-
-
-
no activity in Solanum lycopersicum
-
in fruits
-

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
oxalate + H+
-
Flammulina velutipes formate + CO2
-
?

Synonyms

Synonyms Comment Organism
FvOXDC
-
Flammulina velutipes
OXDC
-
Flammulina velutipes

General Information

General Information Comment Organism
evolution oxalate decarboxylase belongs to the low-pH-inducible cupin superfamily of enzymes Flammulina velutipes