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Literature summary extracted from

  • Karmodiya, K.; Surolia, N.
    Analyses of co-operative transitions in Plasmodium falciparum beta-ketoacyl acyl carrier protein reductase upon co-factor and acyl carrier protein binding (2006), FEBS J., 273, 4093-4103.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.1.1.100 drug development the enzyme has no isoforms and thus is a good target for inhibitor design Plasmodium falciparum

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.100 gene fabG, DNA and amino acid sequence determination and analysis, expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3) Plasmodium falciparum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.100 additional information
-
 additional information cooperativity kinetics, binding constants of substrates and cofactors Plasmodium falciparum
1.1.1.100 0.043
-
 NADPH pH 6.8, 22°C, recombinant enzyme Plasmodium falciparum
1.1.1.100 0.43
-
 acetoacetyl-CoA pH 6.8, 22°C, recombinant enzyme Plasmodium falciparum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.100 3-oxoacyl-[acyl-carrier protein] + NADPH Plasmodium falciparum
-
 3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.100 Plasmodium falciparum
-
 gene fabG, no isozymes
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.100 recombinant C-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Plasmodium falciparum

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.100 a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ = a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+ cofactor and substrate binding kinetics, allosteric regulation mechanism, overview Plasmodium falciparum
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.100 59.8
-
 purified recombinant enzyme Plasmodium falciparum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.100 3-oxoacyl-[acyl-carrier protein] + NADPH
-
 Plasmodium falciparum 3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
 r
1.1.1.100 3-oxoacyl-[acyl-carrier protein] + NADPH cooperative transitions in the enzyme due to cofactor and [acyl-carrier-protein] binding Plasmodium falciparum 3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
 r
1.1.1.100 acetoacetyl-CoA + NADPH
-
 Plasmodium falciparum 3-hydroxybutyryl-CoA + NADP+
-
 r

Synonyms

EC Number Synonyms Comment Organism
1.1.1.100 beta-ketoacyl acyl carrier protein reductase
-
 Plasmodium falciparum
1.1.1.100 FabG
-
 Plasmodium falciparum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.100 22
-
 assay at room temperature Plasmodium falciparum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.100 259
-
 NADPH pH 6.8, 22°C, recombinant enzyme Plasmodium falciparum
1.1.1.100 259
-
 acetoacetyl-CoA pH 6.8, 22°C, recombinant enzyme Plasmodium falciparum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.100 6.8
-
 assay at Plasmodium falciparum

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.100 NADP+ cooperative transitions in the enzyme due to cofactor and [acyl-carrier-protein] binding, cooperative cofactor binding Plasmodium falciparum
1.1.1.100 NADPH cooperative transitions in the enzyme due to cofactor and [acyl-carrier-protein] binding, cooperative allosteric cofactor binding in presence of [acyl-carrier-protein] Plasmodium falciparum