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Literature summary for 4.1.1.31 extracted from

  • Hill, A.T.; Ying, S.; Plaxton, W.C.
    Phosphorylation of bacterial-type phosphoenolpyruvate carboxylase by a Ca2+-dependent protein kinase suggests a link between Ca2+ signalling and anaplerotic pathway control in developing castor oil seeds (2014), Biochem. J., 458, 109-118.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ADP + phosphoenolpyruvate + CO2 Ricinus communis
-
ATP + oxaloacetate
-
?

Organism

Organism UniProt Comment Textmining
Ricinus communis
-
cultivar Baker 296
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein phosphorylated at Ser451 Ricinus communis

Source Tissue

Source Tissue Comment Organism Textmining
seed
-
Ricinus communis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + phosphoenolpyruvate + CO2
-
Ricinus communis ATP + oxaloacetate
-
?

Synonyms

Synonyms Comment Organism
bacterial-type phosphoenolpyruvate carboxylase
-
Ricinus communis
BTPC
-
Ricinus communis
PEPC
-
Ricinus communis

Cofactor

Cofactor Comment Organism Structure
ADP
-
Ricinus communis