Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.1.100 extracted from

  • Wickramasinghe, S.R.; Inglis, K.A.; Urch, J.E.; Mueller, S.; van Aalten, D.M.; Fairlamb, A.H.
    Kinetic, inhibition and structural studies on 3-oxoacyl-ACP reductase from Plasmodium falciparum, a key enzyme in fatty acid biosynthesis (2006), Biochem. J., 393, 447-457.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene fabG, DNA and amino acid sequence determination and analysis, expression of His10-tagged enzyme in Escherichia coli Plasmodium falciparum

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant enzyme, vapour diffusion method, 10 mg/ml protein in 20 mM HEPES, pH 6.8, 0.5 M NaCl, 1 mM DTT, and 0.5 mM EDTA, is mixed with an equal volume of reservoir solution containing 0.1 M MES, pH 6.0, 35% v/v 2-methyl-2,4-pentanediol, and 0.2 M LiSO4, equilibration against 1 ml of mother liquor, room temperature, 6 weeks, X-ray diffraction structure determination and analysis at 1.9 A resolution Plasmodium falciparum

General Stability

General Stability Organism
the purified recombinant enzyme is stable at room temperature at concentrations above 0.2 mg/ml, but unstable at 0.01 mg/ml Plasmodium falciparum

Inhibitors

Inhibitors Comment Organism Structure
3-hydroxybutyryl-CoA competitive product inhibition Plasmodium falciparum
bithionol over 75% inhibition at 0.02 mM, IC50: 0.010 mM Plasmodium falciparum
bromochlorophen an anthelmintic agent, over 75% inhibition at 0.02 mM, IC50: 0.0154 mM Plasmodium falciparum
di-resorcinol sulfide over 75% inhibition at 0.02 mM, IC50: 0.0038 mM Plasmodium falciparum
Hexachlorophene an anthelmintic and antimicrobial agent, over 75% inhibition at 0.02 mM, IC50: 0.002 mM Plasmodium falciparum
additional information no inhibition by triclosan Plasmodium falciparum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic analysis of the recombinant enzyme, kinetic mechanism Plasmodium falciparum
0.0475
-
NADPH pH 6.8, 25┬░C, recombinant enzyme Plasmodium falciparum
0.51
-
acetoacetyl-CoA pH 6.8, 25┬░C, recombinant enzyme Plasmodium falciparum

Metals/Ions

Metals/Ions Comment Organism Structure
additional information the enzyme activity is maximal at a ionic strength of 325 mM Plasmodium falciparum

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum Q86RB1 gene fabG
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information the enzyme contains a signal peptide Plasmodium falciparum

Purification (Commentary)

Purification (Comment) Organism
recombinant His10-tagged enzyme from Escherichia coli by nickel affinity chromatography and gel filtration Plasmodium falciparum

Reaction

Reaction Comment Organism Reaction ID
a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ = a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+ ordered bi bi kinetic mechanism, [acyl-carrier protein] recognition mechanism Plasmodium falciparum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetoacetyl-CoA + NADPH
-
Plasmodium falciparum 3-hydroxybutyryl-CoA + NADP+
-
?

Subunits

Subunits Comment Organism
tetramer crystal structure and ultrafiltration, quarternary structure analysis, monomer interactions, conformations in absence and presence of cofactor NADP+ Plasmodium falciparum

Synonyms

Synonyms Comment Organism
3-oxoacyl-ACP reductase
-
Plasmodium falciparum
FabG
-
Plasmodium falciparum
OAR
-
Plasmodium falciparum

Temperature Optimum [┬░C]

Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
25
-
assay at Plasmodium falciparum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
265
-
NADPH pH 6.8, 25┬░C, recombinant enzyme Plasmodium falciparum
265
-
acetoacetyl-CoA pH 6.8, 25┬░C, recombinant enzyme Plasmodium falciparum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8
-
-
Plasmodium falciparum

Cofactor

Cofactor Comment Organism Structure
NADPH cofactor binding structure and mechanism Plasmodium falciparum

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0102
-
3-hydroxybutyryl-CoA pH 6.8, 25┬░C, recombinant enzyme Plasmodium falciparum

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.002
-
an anthelmintic and antimicrobial agent, over 75% inhibition at 0.02 mM, IC50: 0.002 mM Plasmodium falciparum Hexachlorophene
0.0038
-
over 75% inhibition at 0.02 mM, IC50: 0.0038 mM Plasmodium falciparum di-resorcinol sulfide
0.01
-
over 75% inhibition at 0.02 mM, IC50: 0.010 mM Plasmodium falciparum bithionol
0.0154
-
an anthelmintic agent, over 75% inhibition at 0.02 mM, IC50: 0.0154 mM Plasmodium falciparum bromochlorophen