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Literature summary for 2.4.1.221 extracted from

  • Lopaticki, S.; Yang, A.S.P.; John, A.; Scott, N.E.; Lingford, J.P.; ONeill, M.T.; Erickson, S.M.; McKenzie, N.C.; Jennison, C.; Whitehead, L.W.; Douglas, D.N.; Kneteman, N.M.; Goddard-Borger, E.D.; Boddey, J.A.
    Protein O-fucosylation in Plasmodium falciparum ensures efficient infection of mosquito and vertebrate hosts (2017), Nat. Commun., 8, 561 .
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
Plasmodium falciparum 5783
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
59000
-
calculated from sequence Plasmodium falciparum

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum Q8I360 isolate 3D7
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GDP-L-fucose + protein
-
Plasmodium falciparum GDP + fucosylated protein
-
?

Synonyms

Synonyms Comment Organism
GDP-fucose protein O-fucosyltransferase 2
-
Plasmodium falciparum
POFUT2
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Plasmodium falciparum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Plasmodium falciparum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Plasmodium falciparum

General Information

General Information Comment Organism
malfunction genetic disruption of POFUT2 in Plasmodium falciparum results in ookinetes that are attenuated for colonizing the mosquito midgut, an essential step in malaria transmission. Some POFUT2-deficient parasites mature into salivary gland sporozoites although they are impaired for gliding motility, cell traversal, hepatocyte invasion, and production of exoerythrocytic forms in humanized chimeric liver mice Plasmodium falciparum
physiological function the enzyme is responsible for O-glycosylating of the sporozoite surface proteins CSP and TRAP. The enzyme (POFUT2) ensures the trafficking of Plasmodium thrombospondin repeat proteins as part of a non-canonical glycosylation-dependent endoplasmic reticulum protein quality control mechanism Plasmodium falciparum