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Literature summary for 2.7.1.33 extracted from

  • Lehane, A.M.; Marchetti, R.V.; Spry, C.; van Schalkwyk, D.A.; Teng, R.; Kirk, K.; Saliba, K.J.
    Feedback inhibition of pantothenate kinase regulates pantothenol uptake by the malaria parasite (2007), J. Biol. Chem., 282, 25395-25405.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
acetyl-CoA effective inhibitor Plasmodium falciparum
CoA IC50: 0.2 mM Plasmodium falciparum
coenzyme A feedback inhibition regulates pantothenol uptake. Furosemide reduces this inherent feedback inhibition by competing with coenzyme A for binding to pantothenate kinase, thereby increasing pantothenol uptake Plasmodium falciparum
malonyl-CoA effective inhibitor Plasmodium falciparum

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
-
-
-
Plasmodium falciparum
-
strains 3D7 and FAF6
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + (R)-pantothenate
-
Plasmodium falciparum ADP + (R)-4'-phosphopantothenate
-
?

Synonyms

Synonyms Comment Organism
PanK
-
Plasmodium falciparum

Cofactor

Cofactor Comment Organism Structure
ATP
-
Plasmodium falciparum

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.2
-
IC50: 0.2 mM Plasmodium falciparum CoA