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Literature summary for 1.1.1.100 extracted from

  • Karmodiya, K.; Modak, R.; Sahoo, N.; Sajad, S.; Surolia, N.
    Deciphering the key residues in Plasmodium falciparum beta-ketoacyl acyl carrier protein reductase responsible for interactions with Plasmodium falciparum acyl carrier protein (2008), FEBS J., 275, 4756-4766.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
wild-type and mutants cloned into the pET-28a(+) vector and expressed in Escherichia coli BL21 (DE3) codon plus Plasmodium falciparum

Protein Variants

Protein Variants Comment Organism
R187A kinetic constants (Km and acyl-carrier protein-independent specific activities) remain largely unchanged with respect to wild-type. Exhibits very poor activity in the acyl-carrier protein-dependent spectroscopic assay. No inhibition by increasing concentrations of acyl-carrier protein. 3fold decreased affinity binding to acyl-carrier protein with respect to wild-type Plasmodium falciparum
R187A/R230A kinetic constants (Km and acyl-carrier protein-independent specific activities) remain largely unchanged with respect to wild-type. Exhibits very poor activity in the acyl-carrier protein-dependent spectroscopic assay. 5fold decreased affinity binding to acyl-carrier protein with respect to wild-type Plasmodium falciparum
R187E kinetic constants (Km and acyl-carrier protein-independent specific activities) remain largely unchanged with respect to wild-type. Exhibits very poor activity in the acyl-carrier protein-dependent spectroscopic assay. No inhibition by increasing concentrations of acyl-carrier protein. 4fold decreased affinity binding to acyl-carrier protein with respect to wild-type Plasmodium falciparum
R187E/R230E kinetic constants (Km and acyl-carrier protein-independent specific activities) remain largely unchanged with respect to wild-type. Exhibits very poor activity in the acyl-carrier protein-dependent spectroscopic assay. 80fold decreased affinity binding to acyl-carrier protein with respect to wild-type Plasmodium falciparum
R187K no decreased affinity binding to acyl-carrier protein with respect to wild-type Plasmodium falciparum
R230A kinetic constants (Km and acyl-carrier protein-independent specific activities) remain largely unchanged with respect to wild-type. Exhibits very poor activity in the acyl-carrier protein-dependent spectroscopic assay. No inhibition by increasing concentrations of acyl-carrier protein. 5fold decreased affinity binding to acyl-carrier protein with respect to wild-type Plasmodium falciparum
R230E kinetic constants (Km and acyl-carrier protein-independent specific activities) remain largely unchanged with respect to wild-type. Exhibits very poor activity in the acyl-carrier protein-dependent spectroscopic assay. No inhibition by increasing concentrations of acyl-carrier protein. 41fold decreased affinity binding to acyl-carrier protein with respect to wild-type Plasmodium falciparum

Inhibitors

Inhibitors Comment Organism Structure
acyl-carrier protein inhibition of wild-type with increasing concentrations Plasmodium falciparum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.43
-
acetoacetyl-CoA wild-type Plasmodium falciparum
0.44
-
acetoacetyl-CoA mutant R230A Plasmodium falciparum
0.45
-
acetoacetyl-CoA mutant R187A Plasmodium falciparum
0.47
-
acetoacetyl-CoA mutant R187A/R230A Plasmodium falciparum
0.47
-
acetoacetyl-CoA mutant R187E Plasmodium falciparum
0.49
-
acetoacetyl-CoA mutant R230E Plasmodium falciparum
0.58
-
acetoacetyl-CoA mutant R187E/R230E Plasmodium falciparum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
31000
-
4 * 31000, SDS-PAGE, wild-type and mutants Plasmodium falciparum
110000
-
gel filtration, wild-type and mutants Plasmodium falciparum

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
wild-type and mutants purified to homogeneity using an Ni2+-nitrilotriacetic acid affinity column Plasmodium falciparum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2
-
mutant R187E/R230E, acyl-carrier protein-dependent spectroscopic assay Plasmodium falciparum
3
-
mutant R187A/R230A, acyl-carrier protein-dependent spectroscopic assay Plasmodium falciparum
4
-
mutant R230E, acyl-carrier protein-dependent spectroscopic assay Plasmodium falciparum
6.1
-
mutant R230A, acyl-carrier protein-dependent spectroscopic assay Plasmodium falciparum
6.3
-
mutant R187E, acyl-carrier protein-dependent spectroscopic assay Plasmodium falciparum
6.9
-
mutant R187A, acyl-carrier protein-dependent spectroscopic assay Plasmodium falciparum
42.6
-
mutant R187E/R230E, acyl-carrier protein-independent spectroscopic assay Plasmodium falciparum
45.6
-
mutant R187A/R230A, acyl-carrier protein-independent spectroscopic assay Plasmodium falciparum
54.2
-
mutant R230E, acyl-carrier protein-independent spectroscopic assay Plasmodium falciparum
54.5
-
mutant R187E, acyl-carrier protein-independent spectroscopic assay Plasmodium falciparum
55.3
-
mutant R230A, acyl-carrier protein-independent spectroscopic assay Plasmodium falciparum
57.9
-
mutant R187A, acyl-carrier protein-independent spectroscopic assay Plasmodium falciparum
59.8
-
wild-type, acyl-carrier protein-independent spectroscopic assay Plasmodium falciparum
70.6
-
wild-type, acyl-carrier protein-dependent spectroscopic assay Plasmodium falciparum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetoacetyl-CoA + NADPH wild-type shows less activity with acetoacetyl-CoA than with acetoacetyl-[acyl-carrier protein] Plasmodium falciparum ? + NADP+
-
?
acetoacetyl-[acyl-carrier protein] + NADPH Arg187 and Arg230 are critical residues for the FabG-acyl-carrier protein interactions, significance of the positively charged/hydrophobic patch located adjacent to the active site cavities of FabG for interactions with acyl carrier protein Plasmodium falciparum D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
-
?

Subunits

Subunits Comment Organism
homotetramer 4 * 31000, SDS-PAGE, wild-type and mutants Plasmodium falciparum

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
NADPH 3fold enhancement in acyl-carrier protein binding to wild-type in the presence of NADPH Plasmodium falciparum