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

BRENDA support

Literature summary extracted from

  • McMillan, P.J.; Stimmler, L.M.; Foth, B.J.; McFadden, G.I.; Mueller, S.
    The human malaria parasite Plasmodium falciparum possesses two distinct dihydrolipoamide dehydrogenases (2005), Mol. Microbiol., 55, 27-38.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.4.2 enzyme E1o is located on chromosome 8 Plasmodium falciparum
1.8.1.4 DNA and amino acid sequence determination and analysis of both lipdh genes using RT-PCR, expression of the mitochondrial isozyme as GFP-fusion protein giving green fluorescence and of the apicoplast isozyme fused to acyl-carrier-protein resulting in red fluorescence, expression of truncated mitochondrial and apicoplastic isozymes lacking the putative target sequences as His-tagged proteins in Escherichia coli strain BL21-RIL(DE3), the apicoplast isozyme is expressed at very low levels Plasmodium falciparum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.1.4 additional information
-
additional information ping pong kinetics Plasmodium falciparum
1.8.1.4 0.021
-
NADH pH 8.0, 25°C, mitochondrial isozyme Plasmodium falciparum
1.8.1.4 0.045
-
NAD+ pH 8.0, 25°C, mitochondrial isozyme Plasmodium falciparum
1.8.1.4 0.146
-
dihydrolipoamide pH 8.0, 25°C, mitochondrial isozyme Plasmodium falciparum
1.8.1.4 0.87
-
Lipoamide pH 8.0, 25°C, mitochondrial isozyme Plasmodium falciparum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.2.4.2 mitochondrion enzyme E1o contains mitochondrial targeting sequence Plasmodium falciparum 5739
-
1.2.4.2 additional information enzyme complex is expressed during erythrocytic stage of the parasite Plasmodium falciparum
-
-
1.8.1.4 apicoplast isozyme aLipDH Plasmodium falciparum 20011
-
1.8.1.4 mitochondrion isozyme mLipDH is a component of the branched-chain 2-ketoacid dehydrogenase and the 2-ketoglutarate dehydrogenase multienzyme complexes Plasmodium falciparum 5739
-
1.8.1.4 additional information subcellular localization study using recombinant expression of the isozymes fused to fluorescent protein tags Plasmodium falciparum
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.8.1.4 57200
-
2 * 57200, mitochondrial enzyme, SDS-PAGE and gel filtration, 2 * 75600, apicoplast enzyme, SDS-PAGE and gel filtration Plasmodium falciparum
1.8.1.4 75600
-
2 * 57200, mitochondrial enzyme, SDS-PAGE and gel filtration, 2 * 75600, apicoplast enzyme, SDS-PAGE and gel filtration Plasmodium falciparum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.4.2 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine Plasmodium falciparum
-
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
ir
1.8.1.4 dihydrolipoamide + NAD+ Plasmodium falciparum the forward reaction is the physiological one lipoamide + NADH
-
r

Organism

EC Number Organism UniProt Comment Textmining
1.2.4.2 Plasmodium falciparum
-
enzyme E1o is a component of the alpha-ketoglutarate dehydrogenase multienzyme complex KGDH
-
1.8.1.4 Plasmodium falciparum
-
3D7, 2 lipdh genes encoding 2 isozymes in mitochondrion and apicoplast, both indispensable components of the 2-ketoacid dehydrogenase multienzyme complexes
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.8.1.4 additional information the apicoplast isozyme contains a potential transit peptide, the mitochondrial isozyme contains targeting sequence Plasmodium falciparum

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.1.4 recombinant His-tagged truncated isozymes from Escherichia coli by nickel affinity chromatography to 98% homogeneity Plasmodium falciparum

Reaction

EC Number Reaction Comment Organism Reaction ID
1.8.1.4 protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+ the mitochondrial isozyme shows ping pong kinetic mechanism Plasmodium falciparum

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.8.1.4 additional information both genes are transcribed during erythrocytic development of the parasite Plasmodium falciparum
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.4.2 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
-
Plasmodium falciparum [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
ir
1.8.1.4 dihydrolipoamide + NAD+
-
Plasmodium falciparum lipoamide + NADH
-
r
1.8.1.4 dihydrolipoamide + NAD+ the forward reaction is the physiological one Plasmodium falciparum lipoamide + NADH
-
r

Subunits

EC Number Subunits Comment Organism
1.8.1.4 dimer 2 * 57200, mitochondrial enzyme, SDS-PAGE and gel filtration, 2 * 75600, apicoplast enzyme, SDS-PAGE and gel filtration Plasmodium falciparum
1.8.1.4 More 2 distinct dihydrolipoamide dehydrogenases, both indispensable components of the 2-ketoacid dehydrogenase multienzyme complexes Plasmodium falciparum

Synonyms

EC Number Synonyms Comment Organism
1.2.4.2 E1o component of the alpha-ketoglutarate dehydrogenase multienzyme complex KGDH consisting of components E1o, EC 1.2.4.2, E2, EC 2.1.3.6, and E3, EC 1.8.1.4 Plasmodium falciparum
1.8.1.4 dihydrolipoamide dehydrogenase
-
Plasmodium falciparum
1.8.1.4 LipDH
-
Plasmodium falciparum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.8.1.4 135.5 337 NAD+ pH 8.0, 25°C, mitochondrial isozyme, forward reaction, varying conditions Plasmodium falciparum
1.8.1.4 135.5 337 Lipoamide pH 8.0, 25°C, mitochondrial isozyme, forward reaction, varying conditions Plasmodium falciparum
1.8.1.4 448
-
NADH pH 8.0, 25°C, mitochondrial isozyme, reverse reaction, varying conditions Plasmodium falciparum
1.8.1.4 448
-
dihydrolipoamide pH 8.0, 25°C, mitochondrial isozyme, reverse reaction, varying conditions Plasmodium falciparum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.1.4 7
-
reverse reaction, isozyme mLipDH Plasmodium falciparum
1.8.1.4 9
-
forward reaction, isozyme LipDH Plasmodium falciparum

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.4.2 NAD+
-
Plasmodium falciparum
1.2.4.2 thiamine diphosphate
-
Plasmodium falciparum
1.8.1.4 FAD protein-bound Plasmodium falciparum
1.8.1.4 NAD+
-
Plasmodium falciparum
1.8.1.4 NADH
-
Plasmodium falciparum