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Literature summary for 7.2.2.8 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
Search for more literature for 7.2.2.8

Cloned(Commentary)

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

Protein Variants

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

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Plasmodium berghei

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Plasmodium berghei
-
 gene cutP
-
Plasmodium berghei ANKA
-
 gene cutP
-
Toxoplasma gondii
-
 gene Tgcutp
-

Source Tissue

Source Tissue Comment Organism Textmining
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)

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

Synonyms

Synonyms Comment Organism
copper-transporting ATPase
-
 Plasmodium berghei
copper-transporting ATPase
-
 Toxoplasma gondii
copper-transporting P-type ATPase
-
 Plasmodium berghei
copper-transporting P-type ATPase
-
 Toxoplasma gondii
CuTP
-
 Plasmodium berghei
CuTP
-
 Toxoplasma gondii

General Information

General Information Comment Organism
evolution an evolutionarily highly conserved, copper-transporting P-type ATPase in the murine malaria model parasite Plasmodium berghei Plasmodium berghei
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
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