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Literature summary extracted from

  • Pillai, S.; Rajagopal, C.; Kapoor, M.; Kumar, G.; Gupta, A.; Surolia, N.
    Functional characterization of beta-ketoacyl-ACP reductase (FabG) from Plasmodium falciparum (2003), Biochem. Biophys. Res. Commun., 303, 387-392.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.100 expression in Escherichia coli Plasmodium falciparum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.100 0.075
-
 acetoacetyl-CoA pH 7.5 Plasmodium falciparum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.1.100 soluble recombinant enzyme from Escherichia coli Plasmodium falciparum
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.100 28000
-
 x * 28000, SDS-PAGE Plasmodium falciparum

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.100 Plasmodium falciparum Q965D6
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.100 acetoacetyl-CoA + NADPH + H+
-
 Plasmodium falciparum D-beta-hydroxybutyryl-CoA + NADP+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.100 ? x * 28000, SDS-PAGE Plasmodium falciparum

Synonyms

EC Number Synonyms Comment Organism
1.1.1.100 FabG
-
 Plasmodium falciparum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.100 0.014
-
 acetoacetyl-CoA pH 7.5 Plasmodium falciparum

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.100 NADPH exhibits negative cooperativity for its interaction with the enzyme Plasmodium falciparum