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Information on EC 6.1.1.6 - lysine-tRNA ligase and Organism(s) Plasmodium falciparum and UniProt Accession Q8IDJ8

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Plasmodium falciparum
UNIPROT: Q8IDJ8 not found.
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The taxonomic range for the selected organisms is: Plasmodium falciparum
The enzyme appears in selected viruses and cellular organisms
Synonyms
lysyl-trna synthetase, lysrs, lysrs1, lysrs2, lysyl trna synthetase, mitochondrial lysyl-trna synthetase, cytoplasmic lysyl-trna synthetase, class i lysrs, premsk1p, pfkrs, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Lysyl-tRNA synthetase
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L-Lysine-transfer RNA ligase
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Lysine translase
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Lysine--tRNA ligase
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Lysine-tRNA synthetase
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LysRS
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Lysyl-transfer ribonucleate synthetase
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Lysyl-transfer RNA synthetase
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Lysyl-tRNA synthetase
Synthetase, lysyl-transfer ribonucleate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
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Aminoacylation
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
L-lysine:tRNALys ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9031-26-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
show the reaction diagram
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?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
show the reaction diagram
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-
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?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
show the reaction diagram
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-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
show the reaction diagram
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cladosporin
has the ability to mimic the natural substrate adenosine and thereby colonize the PfKRS active site, binding structure analysis, overview. Plasmodium falciparum lysyl-tRNA synthetase (PfKRS) as the cellular target for cladosporin activity. Structural basis of inhibition by cladosporin, overview. The isocoumarin moiety of cladosporin stacks between Ph342 and Arg559 in PfKRS. In addition, His338 provides edge-toface interaction with hydroxybenzene ring of isocoumarin moiety. The THP ring points towards L-Lys binding pocket and its methyl group faces Ser344
cladosporin
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30% inhibition at 0.11 mM
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000454 - 0.0000896
cladosporin
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65000
2 * 65000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 65000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.1 M Bis-Tris pH 6.5, 2% (v/v) tascimate pH 6.0, 20% (w/v) PEG 3350
purified enzyme PfKRS in complex with lysine and cladosporin, hanging drop vapour diffusion method, mixing of 0.001 ml of highly pure enzyme in 50 mM Tris-HCl, pH 8.0, 200 mM NaCl, 10 mM 2-mercaptoethanol, 0.5 mM cladosporin, and 2 mM L-lysine, with 0.001 ml of crstallization solution containing 0.1 M Bis-Tris, pH 6.5, 2% v/v Tascimate, pH 6.0, 20% w/v PEG 3350, 20°C, 10 days, X-ray diffraction structure determination and analysis at 2.7 A resolution, molecular homology modeling using the human enzyme structure as template
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
amylose bead chromatography and S200 gel filtration
Ni-affinity column chromatography, and MonoQ column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli Tuner (DE3) cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pharmacology
Plasmodium falciparum lysyl-tRNA synthetase (PfKRS) as the cellular target for cladosporin activity. Targeting parasitic aminoacyl-tRNA synthetases (aaRSs) can provide an additional component in the present multi-drug cocktail therapy against malaria
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Khan, S.; Garg, A.; Camacho, N.; Van Rooyen, J.; Kumar Pole, A.; Belrhali, H.; Ribas de Pouplana, L.; Sharma, V.; Sharma, A.
Structural analysis of malaria-parasite lysyl-tRNA synthetase provides a platform for drug development
Acta Crystallogr. Sect. D
69
785-795
2013
Plasmodium falciparum (Q8IDJ8), Plasmodium falciparum
Manually annotated by BRENDA team
Hoepfner, D.; McNamara, C.W.; Lim, C.S.; Studer, C.; Riedl, R.; Aust, T.; McCormack, S.L.; Plouffe, D.M.; Meister, S.; Schuierer, S.; Plikat, U.; Hartmann, N.; Staedtler, F.; Cotesta, S.; Schmitt, E.K.; Petersen, F.; Supek, F.; Glynne, R.J.; Tallarico, J.A.; Porter, J.A.; Fishman, M.C.; Bodenreider, C.; Di, D.i.a.
Selective and specific inhibition of the Plasmodium falciparum lysyl-tRNA synthetase by the fungal secondary metabolite cladosporin
Cell Host Microbe
11
654-663
2012
Plasmodium falciparum, Plasmodium falciparum FCB, Plasmodium falciparum NF54, Plasmodium falciparum Camp R, Plasmodium falciparum FCR3, Plasmodium falciparum D1, Plasmodium falciparum D6
Manually annotated by BRENDA team
Khan, S.; Sharma, A.; Belrhali, H.; Yogavel, M.; Sharma, A.
Structural basis of malaria parasite lysyl-tRNA synthetase inhibition by cladosporin
J. Struct. Funct. Genomics
15
63-71
2014
Plasmodium falciparum (Q8IDJ8), Plasmodium falciparum
Manually annotated by BRENDA team