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Literature summary for 3.1.3.4 extracted from

  • Eastmond, P.J.; Quettier, A.L.; Kroon, J.T.; Craddock, C.; Adams, N.; Slabas, A.R.
    A phosphatidate phosphatase double mutant provides a new insight into plant membrane lipid homeostasis (2011), Plant Signal. Behav., 6, 526-527.
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ dependent on Arabidopsis thaliana

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Arabidopsis thaliana
-
root
-
Arabidopsis thaliana
-

Synonyms

Synonyms Comment Organism
pah1 isoform Arabidopsis thaliana
PAH2 isoform Arabidopsis thaliana
PAP
-
Arabidopsis thaliana
phosphatidic acid phosphatase
-
Arabidopsis thaliana

General Information

General Information Comment Organism
malfunction partitioning of substrate between the prokaryotic and eukaryotic pathways is perturbed in the pah1 pah2-1 double mutant. Both the total lipid content and the phospholipid content of pah1 pah2-1 mutant leaves and roots is greater than wild type on a per unit fresh weight basis Arabidopsis thaliana
physiological function phosphatidic acid phosphatase enzymes, PAH1 and PAH2, are capable of repressing phospholipid biosynthesis at the endoplasmic reticulum in Arabidopsis thaliana. PAH1/2 play a role in the provision of eukaryotic substrate for galactolipid synthesis in leaves Arabidopsis thaliana