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Literature summary extracted from

  • Kenthirapalan, S.; Waters, A.P.; Matuschewski, K.; Kooij, T.W.
    Copper-transporting ATPase is important for malaria parasite fertility (2014), Mol. Microbiol., 91, 315-325.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.2.2.8 gene cutP Plasmodium berghei
7.2.2.8 gene Tgcutp or TGGT1_020170, recombinant expression of the Myc2-tagged enzyme in Toxoplasma gondii Toxoplasma gondii

Protein Variants

EC Number Protein Variants Comment Organism
7.2.2.8 additional information generation of a Plasmodium berghei loss-of-function mutant line, phenotype, detailed overview Plasmodium berghei

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.2.2.8 intracellular
-
Plasmodium berghei 5622
-
7.2.2.8 intracellular TgCuTP localizes to intraparasitic structures juxtaposed to the acidocalcisomes and/or plant-like vacuole Toxoplasma gondii 5622
-
7.2.2.8 additional information TgCuTP localizes in close proximity of the acidocalcisomes and/or plant-like vacuole in Toxoplasma gondii Toxoplasma gondii
-
-
7.2.2.8 vesicle enzyme CuTP is predominantly located in vesicular bodies of the parasite Plasmodium berghei 31982
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.2.2.8 Mg2+ required Plasmodium berghei

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.2.2.8 ATP + H2O + Cu+[side 1] Plasmodium berghei
-
ADP + phosphate + Cu+[side 2]
-
?
7.2.2.8 ATP + H2O + Cu+[side 1] Plasmodium berghei ANKA
-
ADP + phosphate + Cu+[side 2]
-
?

Organism

EC Number Organism UniProt Comment Textmining
7.2.2.8 Plasmodium berghei
-
gene cutP
-
7.2.2.8 Plasmodium berghei ANKA
-
gene cutP
-
7.2.2.8 Toxoplasma gondii
-
gene Tgcutp
-
7.2.2.9 Plasmodium berghei
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
7.2.2.8 additional information CuTP is expressed in all Plasmodium life cycle stages, including intracellular asexual and sexual blood stages, and extracellular ookinetes and salivary gland sporozoites, and localizes to vesicle-like structures Plasmodium berghei
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.2.2.8 ATP + H2O + Cu+[side 1]
-
Plasmodium berghei ADP + phosphate + Cu+[side 2]
-
?
7.2.2.8 ATP + H2O + Cu+[side 1]
-
Plasmodium berghei ANKA ADP + phosphate + Cu+[side 2]
-
?

Synonyms

EC Number Synonyms Comment Organism
7.2.2.8 copper-transporting ATPase
-
Plasmodium berghei
7.2.2.8 copper-transporting ATPase
-
Toxoplasma gondii
7.2.2.8 copper-transporting P-type ATPase
-
Plasmodium berghei
7.2.2.8 copper-transporting P-type ATPase
-
Toxoplasma gondii
7.2.2.8 CuTP
-
Plasmodium berghei
7.2.2.8 CuTP
-
Toxoplasma gondii
7.2.2.9 CuTP
-
Plasmodium berghei

General Information

EC Number General Information Comment Organism
7.2.2.8 evolution an evolutionarily highly conserved, copper-transporting P-type ATPase in the murine malaria model parasite Plasmodium berghei Plasmodium berghei
7.2.2.8 malfunction a loss-of-function mutant line shows no apparent defect in in vivo blood stage growth. But parasite transmission through the mosquito vector is severely affected, although not entirely abolished. Male and female gametocytes are abundant in cutp? parasites, but activation of male microgametes and exflagellation are strongly impaired. This specific defect can be mimicked by addition of the copper chelator neocuproine to wild-type gametocytes. Female fertility is also severely abrogated. Targeted deletion of CuTP does not affect asexual blood stage growth in mice Plasmodium berghei
7.2.2.8 physiological function the enzyme is involved in homeostasis of the trace element copper, that is essential to all eukaryotic life. Copper serves as a cofactor in metalloenzymes and catalyses electron transfer reactions as well as the generation of potentially toxic reactive oxygen species. A healthy copper homeostasis is critical to malaria parasite fertility of both genders of gametocyte and to transmission to the mosquito vector, Anopheles stephensi Plasmodium berghei
7.2.2.9 physiological function a loss-of-function mutant line shows no apparent defect in in vivo blood stage growth. Parasite transmission through the mosquito vector is severely affected, but not entirely abolished. Male and female gametocytes are abundant in mutant parasites, but activation of male microgametes and exflagellation are strongly impaired. This defect can be mimicked by addition of the copper chelator neocuproine to wild-type gametocytes. Female fertility is also severely abrogated Plasmodium berghei