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Literature summary for 1.3.1.13 extracted from

  • Schenck, C.; Westphal, J.; Jayaraman, D.; Garcia, K.; Wen, J.; Mysore, K.; Ane, J.; Sumner, L.; Maeda, H.
    Role of cytosolic, tyrosine-insensitive prephenate dehydrogenase in Medicagoxa0truncatula (2020), Plant Direct, 4, e00218 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.3.1.13

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Medicago truncatula 5829
-

Organism

Organism UniProt Comment Textmining
Medicago truncatula G7J2E9
-
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Medicago truncatula
-
root
-
 Medicago truncatula
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
prephenate + NADP+
-
 Medicago truncatula 4-hydroxyphenylpyruvate + CO2 + NADPH + H+
-
 ?

Synonyms

Synonyms Comment Organism
11415867
-
 Medicago truncatula
MtPDH1
-
 Medicago truncatula
PDH1
-
 Medicago truncatula

General Information

General Information Comment Organism
malfunction pdh1 mutants lack PDH transcript and PDH activity, and display little aberrant morphological phenotypes under standard growth conditions Medicago truncatula
physiological function Pdh1 mutants that lacked PDH transcript and PDH activity display little aberrant morphological phenotypes under standard growth conditions. Nodule number and nitrogenase activity of Pdh1 mutants are not significantly reduced compared with wild-type during symbiosis with nitrogen-fixing bacteria. Tyr levels are not significantly different between wild-type and mutants under standard conditions. When carbon flux is increased by shikimate precursor feeding, mutants accumulate significantly less Tyr than wild-type Medicago truncatula
physiological function the enzyme (MtPDH1) is involved in Tyr biosynthesis when the shikimate pathway is stimulated and possibly linked to unidentified legume-specific specialized metabolism Medicago truncatula