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Literature summary extracted from

  • Guerra, A.; Afanador, G.; Prigge, S.
    Crystal structure of lipoate-bound lipoate ligase 1, LipL1, from Plasmodium falciparum (2017), Proteins, 85, 1777-1783 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.1.20 recombinant expression of truncated enzyme mutants from plasmid pMALcHT, encoding a maltose-binding protein (MBP) followed by a linker region composed of a tobacco etch virus (TEV) protease cut site and a six histidine affinity tag, in Escherichia coli strain BL21-Star (DE3), recombinnat expression of wild-type and truncated mutant enzymes in lipoylation-deficient Escherichia coli strain JEG3. Structure comparisons, overview Plasmodium falciparum

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.3.1.20 purified recombinant lipoyl-PfLipL1D243-279 complex, mixing of 0.001 ml of 5 mg/ml protein, 1.2 mol equiv of lipoate, and excess ATP with 0.001 ml of reservoir solution containing 100 mM HEPES, pH 7.0, 1.5 M (NH4)2SO4, and 20% ethylene glycol, 20°C, method optimization, X-ray diffraction structure determination and analysis at 2.32 A resolution Plasmodium falciparum

Protein Variants

EC Number Protein Variants Comment Organism
6.3.1.20 additional information construction of truncated mutants of enzyme PfLipL1, PfLipL1DELTA259-269, PfLipL1DELTA254-274, and PfLipL1D249-279 Plasmodium falciparum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
6.3.1.20 mitochondrion
-
Plasmodium falciparum 5739
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.1.20 Mg2+ required Plasmodium falciparum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.1.20 ATP + (R)-lipoate + a [lipoyl-carrier protein]-L-lysine Plasmodium falciparum
-
a [lipoyl-carrier protein]-N6-(lipoyl)lysine + AMP + diphosphate
-
?

Organism

EC Number Organism UniProt Comment Textmining
6.3.1.20 Plasmodium falciparum Q8IEG9
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.1.20 recombinant His-tagged truncated mutant enzymes from Escherichia coli strain BL21-Star (DE3) by nickel affinity chromatography, MBP tag cleavage by TEV protease, cation exchange chromatography, and gel filtration Plasmodium falciparum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.1.20 ATP + (R)-lipoate + a [lipoyl-carrier protein]-L-lysine
-
Plasmodium falciparum a [lipoyl-carrier protein]-N6-(lipoyl)lysine + AMP + diphosphate
-
?
6.3.1.20 additional information cell-based lipoylation assays using wild-type and truncated mutant enzymes recombinantly expressed in lipoylation-deficient Escherichia coli strain JEG3 Plasmodium falciparum ?
-
?

Subunits

EC Number Subunits Comment Organism
6.3.1.20 More the lipoate-bound PfLipL1DELTA243-279 structure consists of a large N-terminal domain (NTD, residues 21-276), a linker region lacking defined secondary structure (residues 277-289), and a small C-terminal domain (CTD, residues 290-370). The NTD contains two beta-sheets, a large mixed beta-sheet made up of seven beta-strands (beta1, beta2, beta6, beta7, beta8, beta9, and beta10) and a small mixed-sheet made up of three strands (beta3, beta4, and beta5). There are six alpha-helical elements surrounding the beta-sheets (alpha1–6). The CTD consists of one anti-parallel beta-sheet made up of three strands (beta11, beta12, and beta13) and three alpha-helices (alpha7, alpha8, and alpha9). The two monomers in the asymmetric unit of similar conformations Plasmodium falciparum

Synonyms

EC Number Synonyms Comment Organism
6.3.1.20 LipL1
-
Plasmodium falciparum
6.3.1.20 lipoate-bound lipoate ligase 1
-
Plasmodium falciparum
6.3.1.20 PfLipL1
-
Plasmodium falciparum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.3.1.20 37
-
assay at Plasmodium falciparum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3.1.20 7.5
-
assay at Plasmodium falciparum

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.1.20 ATP
-
Plasmodium falciparum

General Information

EC Number General Information Comment Organism
6.3.1.20 evolution lipoate protein ligase 1 (PfLipL1) is an ATP-dependent ligase that belongs to the biotin/lipoate A/B protein ligase family (PFAM PF03099) Plasmodium falciparum
6.3.1.20 physiological function PfLipL1 is the only known canonical lipoate ligase in Plasmodium falciparum and functions as a redox switch between two lipoylation routes in the parasite mitochondrion Plasmodium falciparum