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6.1.1.6: lysine-tRNA ligase

This is an abbreviated version!
For detailed information about lysine-tRNA ligase, go to the full flat file.

Word Map on EC 6.1.1.6

Reaction

ATP
+
L-lysine
 +
tRNALys
=
AMP
 +
diphosphate
 +
L-lysyl-tRNALys

Synonyms

Ap4A synthase, BBA_03037, class 1 lysyl tRNA synthetase, class I LysRS, class I lysyl-tRNA synthetase, class II lysyl-tRNA synthetase, cyto-LysRS, cytoKARS, cytoplasmic lysyl-tRNA synthetase, FOSTERSO_4045, GsLysRS, hKRS, KARS, KRS, KRS-1, L-Lysine-transfer RNA ligase, lysine aminoacyl-tRNA synthetase, Lysine translase, Lysine--tRNA ligase, Lysine-tRNA synthetase, LysRS, LysRS-I, LysRS-II, LysRS1, LysRS2, lysS, lysS2, LysU, LysX, lysyl tRNA synthetase, Lysyl-transfer ribonucleate synthetase, Lysyl-transfer RNA synthetase, Lysyl-tRNA synthetase, lysylphosphatidylglycerol biosynthesis bifunctional protein, mito-LysRS, mitochondrial lysyl-tRNA synthetase, mitoKARS, More, Msk1p, MSMEG_3796, MSMEG_6094, MSMEI_3707, MXAN_4731, PF3D7_1350100, PfKRS, preMsk1p, Synthetase, lysyl-transfer ribonucleate, tRK1

ECTree

     6 Ligases
         6.1 Forming carbon-oxygen bonds
             6.1.1 Ligases forming aminoacyl-tRNA and related compounds
                6.1.1.6 lysine-tRNA ligase

Application

Application on EC 6.1.1.6 - lysine-tRNA ligase

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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
LysRS s207 phosphorylation plays a role as a prognostic factor in lung cancer after primary surgery
drug development
medicine
-
KRS is released from the multi-tRNA synthetase complex (MSC) and translocates to the plasma membrane, where it binds to p67LR, resulting in cell migration and metastasis. Modulation of KRS-67LR interaction by an inhibitor BC-KYH16899 may offer a strategy with which to control metastasis
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
synthesis
recombinant Escherichia coli lysyl-tRNA synthase (LysU) has been previously utilised in the production of stabile, synthetic diadenosine polyphosphate (ApnA) analogues. LysU is also useful as a tool for highly controlled phosphate-phosphate bond formation between nucleotides, avoiding the need for complex protecting group chemistries. Resulting high yielding tandem LysU-based biosynthetic-synthetic/synthetic-biosynthetic strategies emerge for the preparation of varieties of ApnA analogues directly from inexpensive natural nucleotides and nucleosides. Analogues so formed make a useful small library with which to probe ApnA activities in vitro and in vivo leading to the discovery of potentially potent biopharmaceuticals active against chronic pain and other chronic, high-burden disease states