Literature summary for 1.1.1.100 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.

Search for more literature for 1.1.1.100

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Plasmodium falciparum

KM Value [mM]

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

Localization

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

Molecular Weight [Da]

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

Organism

Organism	UniProt	Comment	Textmining
Plasmodium falciparum	Q965D6	-	-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms	Comment	Organism
FabG	-	Plasmodium falciparum

Turnover Number [1/s]

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

Cofactor

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

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Release 2023.1 (January 2023)