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Literature summary extracted from

  • Hollin, T.; De Witte, C.; Lenne, A.; Pierrot, C.; Khalife, J.
    Analysis of the interactome of the Ser/Thr protein phosphatase type 1 in Plasmodium falciparum (2016), BMC Genomics, 17, 246 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.16 gene PF3D7_1414400 Plasmodium falciparum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.3.16 [a protein]-serine/threonine phosphate + H2O Plasmodium falciparum
-
 [a protein]-serine/threonine + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.16 Plasmodium falciparum Q8ILV1
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.16 [a protein]-serine/threonine phosphate + H2O
-
 Plasmodium falciparum [a protein]-serine/threonine + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.3.16 PF3D7_1414400
-
 Plasmodium falciparum
3.1.3.16 PfPP1
-
 Plasmodium falciparum
3.1.3.16 PP1
-
 Plasmodium falciparum
3.1.3.16 protein phosphatase 1
-
 Plasmodium falciparum
3.1.3.16 Ser/Thr protein phosphatase type 1
-
 Plasmodium falciparum

General Information

EC Number General Information Comment Organism
3.1.3.16 additional information detection of the PfPP1 interactome and PP1 interacting proteins (Pips) by mass spectrometry, yeast two-hybrid screening, and in silico analysis of the Plasmodium falciparum predicted proteome. The Pips include a large range of proteins, overview Plasmodium falciparum
3.1.3.16 physiological function protein phosphatase 1 (PP1) is an enzyme essential to cell viability in the malaria parasite Plasmodium falciparum. The activity of PP1 is regulated by the binding of regulatory subunits, of which there are 3 reported for the parasite to date Plasmodium falciparum