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2-chloroadenosine 5'-triphosphate + lysine + tRNALys
2-chloroadenosine 5'-monophosphate + Lys-tRNALys + diphosphate
-
-
-
-
?
AMP + ATP
diadenosine 5',5''-P1,P4-tetraphosphate + ?
-
-
-
?
AMP + diphosphate + L-arginyl-tRNALys
ATP + L-arginine + tRNALys
-
-
-
-
r
AMP + diphosphate + L-lysyl-tRNALys
ATP + L-lysine + tRNALys
-
-
-
-
r
AMP + diphosphate + L-methionyl-tRNALys
ATP + L-methionine + tRNALys
-
-
-
-
r
AMP + L-threonyl-tRNALys + diphosphate
ATP + L-threonine + tRNALys
-
-
-
-
r
ATP + 4-aminobutanoate + tRNALys
AMP + 4-aminobutyryl-tRNALys + diphosphate
-
-
-
?
ATP + ATP
diadenosine 5',5''-P1,P3-triphosphate + ?
-
-
-
-
?
ATP + ATP
diadenosine 5',5''-P1,P4-tetraphosphate + diphosphate
ATP + D-lysine + tRNALys
AMP + D-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + L-alanine + tRNALys
AMP + L-alanyl-tRNALys + diphosphate
-
264000fold lower activity than with L-lysine, deacylation of the mischarged tRNALys, addition of 2 mM L-lysine abolishes the reaction
-
r
ATP + L-arginine + tRNALys
AMP + L-arginyl-tRNALys + diphosphate
ATP + L-cysteine + tRNALys
AMP + L-cysteinyl-tRNALys + diphosphate
-
750000fold lower activity than with L-lysine, deacylation of the mischarged tRNALys, addition of 2 mM L-lysine abolishes the reaction
-
r
ATP + L-glutamate + tRNALys
AMP + L-glutamyl-tRNALys + diphosphate
-
low activity
-
?
ATP + L-leucine + tRNALys
AMP + L-leucyl-tRNALys + diphosphate
-
132000fold lower activity than with L-lysine, addition of 2 mM L-lysine abolishes the reaction
-
r
ATP + L-lysinamide + tRNALys
AMP + L-aminolysyl-tRNALys + diphosphate
-
low activity
-
?
ATP + L-lysine
?
-
a small fraction of lysine is converted to lysine lactam in absence or presence of tRNALys
-
?
ATP + L-lysine + Borellia burgdorferi tRNALys
AMP + diphosphate + L-lysyl-tRNALys
ATP + L-lysine + Escherichia coli G2.U71 tRNA
?
ATP + L-lysine + Escherichia coli G2.U71 tRNALys
AMP + diphosphate + L-lysyl-tRNALys
ATP + L-lysine + Escherichia coli tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
-
r
ATP + L-lysine + Escherichia coli tRNALys CNBr-treated
AMP + diphosphate + L-lysyl-tRNALys CNBr-treated
-
-
-
-
r
ATP + L-lysine + Escherichia coli wild type tRNA
?
ATP + L-lysine + Escherichia coli wild type tRNALys
AMP + diphosphate + L-lysyl-tRNALys
ATP + L-lysine + human tRNALys3
AMP + diphosphate + L-lysyl-tRNALys3
-
-
-
-
?
ATP + L-lysine + Methanococcus maripaludis tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
-
r
ATP + L-lysine + Methanococcus maripaludis tRNALys CNBr-treated
AMP + diphosphate + L-lysyl-tRNALys CNBr-treated
-
-
-
-
r
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
ATP + L-lysine + tRNALys from rat liver
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
-
?
ATP + L-lysine + tRNALysCUU
AMP + L-lysyl-tRNALysCUU + diphosphate
ATP + L-lysine + tRNALysGUU
AMP + L-lysyl-tRNALysGUU + diphosphate
ATP + L-lysine + tRNALysUCU
AMP + L-lysyl-tRNALysUCU + diphosphate
-
-
-
-
?
ATP + L-lysine + tRNALysUGU
AMP + L-lysyl-tRNALysUGU + diphosphate
ATP + L-lysine + tRNALysUUC
AMP + L-lysyl-tRNALysUUC + diphosphate
ATP + L-lysine + tRNALysUUG
AMP + L-lysyl-tRNALysUUG + diphosphate
-
-
-
-
?
ATP + L-lysine + tRNALysUUU
AMP + L-lysyl-tRNALysUUU + diphosphate
ATP + L-lysine + tRNALysUUUmodified
AMP + L-lysyl-tRNALysUUUmodified + diphosphate
-
anticodon variant tRNA substrate from Escherichia coli, t6 modification of base A37
-
?
ATP + L-lysine + tRNATyrCUA
AMP + L-lysyl-tRNATyrCUA + diphosphate
-
has a weak activity to tRNATyrCUA with L-lysine
-
-
?
ATP + L-lysine + yeast tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
-
?
ATP + L-lysine amide + tRNALys
AMP + L-amino-lysyl-tRNALys + diphosphate
-
-
-
r
ATP + L-lysine ethyl ester + tRNALys
AMP + ethyl-L-lysyl-tRNALys + diphosphate
ATP + L-lysine hydroxamate + tRNALys
AMP + L-lysine hydroxamoyl-tRNALys + diphosphate
ATP + L-lysine methyl ester + tRNALys
AMP + methyl-L-lysyl-tRNALys + diphosphate
ATP + L-methionine + tRNALys
AMP + L-methionyl-tRNALys + diphosphate
-
32000fold lower activity than with L-lysine, addition of 2 mM L-lysine abolishes the reaction
-
r
ATP + L-ornithine
?
-
L-ornithine is converted to ornithine lactam in absence or presence of tRNALys
-
?
ATP + L-serine + tRNALys
AMP + L-seryl-tRNALys + diphosphate
-
562000fold lower activity than with L-lysine, deacylation of the mischarged tRNALys, addition of 2 mM L-lysine abolishes the reaction
-
r
ATP + L-threonine + tRNALys
AMP + L-threonyl-tRNALys + diphosphate
-
16000fold lower activity than with L-lysine, addition of 2 mM L-lysine abolishes the reaction
-
r
ATP + lysine + tRNALys
?
-
primary role is the translation of genetic information into protein structure
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
ATP + lysine + tRNALys,3'-59mer
AMP + L-lysyl-tRNALys, 3'-59mer + diphosphate
-
human tRNALys mutant
-
?
ATP + lysine + tRNALysU35A
AMP + L-lysyl-tRNALysU35A + diphosphate
-
human tRNALys mutant, from in vitro translation, very low activity
-
?
ATP + lysine + tRNALysU35C
AMP + L-lysyl-tRNALysU35C + diphosphate
-
human tRNALys mutant, from in vitro translation, 153fold decreased activity compared to the wild-type
-
?
ATP + lysine + tRNALysU36A
AMP + L-lysyl-tRNALysU36A + diphosphate
-
human tRNALys mutant, from in vitro translation, 182fold decreased activity compared to the wild-type
-
?
ATP + lysine + tRNALysU36C
AMP + L-lysyl-tRNALysU36C + diphosphate
-
human tRNALys mutant, from in vitro translation, 11fold decreased activity compared to the wild-type
-
?
ATP + ornithine + tRNALys
AMP + ornithyl-tRNALys + diphosphate
dATP + lysine + tRNALys
dAMP + L-lysyl-tRNALys + diphosphate
-
-
-
-
?
formycin 5'-triphosphate + L-lysine + tRNALys
formycin 5'-monophosphate + diphosphate + L-lysyl-tRNALys
-
-
-
-
?
additional information
?
-
ATP + ATP
diadenosine 5',5''-P1,P4-tetraphosphate + diphosphate
-
-
-
-
?
ATP + ATP
diadenosine 5',5''-P1,P4-tetraphosphate + diphosphate
-
-
-
-
?
ATP + ATP
diadenosine 5',5''-P1,P4-tetraphosphate + diphosphate
-
the mechanism of the the enzyme in the 18S multienzyme complex is ordered bi uni uni bi ping-pong, the mechanism of the free enzyme is random
-
?
ATP + L-arginine + tRNALys
AMP + L-arginyl-tRNALys + diphosphate
-
low activity
-
?
ATP + L-arginine + tRNALys
AMP + L-arginyl-tRNALys + diphosphate
-
best noncognate amino acid substrate, 1600fold lower activity than with L-lysine, addition of 2 mM L-lysine abolishes the reaction
-
r
ATP + L-lysine + Borellia burgdorferi tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
-
?
ATP + L-lysine + Borellia burgdorferi tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
-
?
ATP + L-lysine + Escherichia coli G2.U71 tRNA
?
-
-
-
-
?
ATP + L-lysine + Escherichia coli G2.U71 tRNA
?
-
-
-
-
?
ATP + L-lysine + Escherichia coli G2.U71 tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
-
r
ATP + L-lysine + Escherichia coli G2.U71 tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
-
r
ATP + L-lysine + Escherichia coli wild type tRNA
?
-
-
-
-
?
ATP + L-lysine + Escherichia coli wild type tRNA
?
-
-
-
-
?
ATP + L-lysine + Escherichia coli wild type tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
-
r
ATP + L-lysine + Escherichia coli wild type tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
-
r
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
the reaction catalyzed by the enzyme plays an important role in the transport of aminoacylated tRNAs from the nucleus to the cytoplasm
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
conformational changes in KRS structures upon lysine binding, structural basis of lysyl-adenylate formation, overview
-
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
-
r
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
-
r
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
the reaction catalyzed by the enzyme plays an important role in the transport of aminoacylated tRNAs from the nucleus to the cytoplasm
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
-
r
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
?
ATP + L-lysine + tRNALys
AMP + diphosphate + L-lysyl-tRNALys
-
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
r
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
substrate recognition mechanism
-
r
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
2-step reaction, the first step comprises the activation of the amino acid to form an enzyme-bound aminoacyl adenylate, the second step involves binding of this complex by tRNA, whose 3'-end is esterified with the aminoacyl-moiety followed by release of the resulting aminoacyl-tRNA, aminoacylation cannot be performed in absence of the tRNA
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
tRNA substrate from Borrelia burgdorferi or Escherichia coli, predicted secondary structure of the tRNALys from Borrelia burgdorferi
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
activity with tRNALys variants, transfer RNA recognition
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
-
r
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
2-step reaction, the first step comprises the activation of the amino acid to form an enzyme-bound aminoacyl adenylate, the second step involves binding of this complex by tRNA, whose 3'-end is esterified with the aminoacyl-moiety followed by release of the resulting aminoacyl-tRNA, aminoacylation can be performed in absence of the tRNA
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
cognate amino acid, best substrate, two-step reaction mechanism, limited selectivity in the aminoacylation reaction due to inefficient editing of some amino acids, e.g. Met, Leu, Cys, Ala, Thr, by pre-transfer mechanism or the absence of post-transfer editing of other amino acids e.g. Arg, Ser, a small fraction of lysine is converted to lysine lactam
-
r
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
tRNA substrate from Borrelia burgdorferi or Escherichia coli, predicted secondary structure of tRNAlys from Escherichia coli
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
the L-lysine binding process is much faster than the ATP binding process
-
r
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
tRNA substrate from Escherichia coli, bases U35 and U36 play an important role in tRNA substrate recognition
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
-
r
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
isozyme shows different activities with cytoplasmic and mitochondrial tRNALys
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
during early assembly of human immunodeficiency virus type 1, an assembly complex is formed, the components of which include genomic RNA, Gag, Gag-Pol, tRNALys, and lysyl tRNA synthetase. Directly increasing or decreasing cellular expression of LysRS results in corresponding changes in viral infectivity and in the viral concentrations of LysRS, tRNALys, and reverse transcriptase. Overexpression of LysRS in the cell reduces viral protease activity
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
enzyme facilitates the selective packaging of tRNA3 Lys. Newly synthesized LysRS is associated with Gag protein after a 10 minute pulse with [35 S]cysteine/methionine. Incorporation of LysRS into HIV-1 is very sensitive to the inhibition of new synthesis of LysRS
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
the enzyme is secreted to trigger proinflammatory response. TNF-alpha induces secretion of lysyl-tRNA synthetase. The secreted enzyme binds to macrophages and peripheral blood mononuclear cell to enhance the TNF-alpha production and their migration. The mitogen-activated protein kinases, extracellular signal-regulated kinase, p38 mitogen-activated protein kinase and inhibitory protein Galphai are involved in the signal transduction triggered by lysyl-tRNA synthetase. Lysyl-tRNA synthetase may work as a signaling molecule, inducing immune response through the activation of monocyte/macrophages
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
LysRS plays a key role via Ap4A as an important signaling molecule in transcriptional activity of microphthalmia transcription factor
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
pathology-related human mitochondrial tRNA(Lys) variants as substrates. G8313A or G8328A mutations in tRNA(Lys) lead to drastic decreases (500fold to 7000fold) in lysylation efficiency. Mutations in tRNA(Lys) that have no effect on aminoacylation: A8296G, U8316G, G8342A, U8356C, U8362G, G8363A
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
predicted secondary structure of the tRNALys from Methanococcus maripaludis
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
tRNA substrate from Escherichia coli, bases N73, and U36 play an important role in tRNA substrate recognition
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
-
?
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
?
ATP + L-lysine + tRNALysCUU
AMP + L-lysyl-tRNALysCUU + diphosphate
-
-
-
-
?
ATP + L-lysine + tRNALysCUU
AMP + L-lysyl-tRNALysCUU + diphosphate
-
anticodon variant tRNA substrate from Escherichia coli
-
?
ATP + L-lysine + tRNALysCUU
AMP + L-lysyl-tRNALysCUU + diphosphate
-
-
-
-
?
ATP + L-lysine + tRNALysCUU
AMP + L-lysyl-tRNALysCUU + diphosphate
-
-
-
-
?
ATP + L-lysine + tRNALysCUU
AMP + L-lysyl-tRNALysCUU + diphosphate
-
-
-
?
ATP + L-lysine + tRNALysCUU
AMP + L-lysyl-tRNALysCUU + diphosphate
-
-
-
?
ATP + L-lysine + tRNALysCUU
AMP + L-lysyl-tRNALysCUU + diphosphate
-
-
-
-
?
ATP + L-lysine + tRNALysGUU
AMP + L-lysyl-tRNALysGUU + diphosphate
-
anticodon variant tRNA substrate from Escherichia coli
-
?
ATP + L-lysine + tRNALysGUU
AMP + L-lysyl-tRNALysGUU + diphosphate
-
-
-
-
?
ATP + L-lysine + tRNALysUGU
AMP + L-lysyl-tRNALysUGU + diphosphate
-
anticodon variant tRNA substrate from Escherichia coli
-
?
ATP + L-lysine + tRNALysUGU
AMP + L-lysyl-tRNALysUGU + diphosphate
-
-
-
-
?
ATP + L-lysine + tRNALysUUC
AMP + L-lysyl-tRNALysUUC + diphosphate
-
anticodon variant tRNA substrate from Escherichia coli
-
?
ATP + L-lysine + tRNALysUUC
AMP + L-lysyl-tRNALysUUC + diphosphate
-
-
-
-
?
ATP + L-lysine + tRNALysUUU
AMP + L-lysyl-tRNALysUUU + diphosphate
-
-
-
-
?
ATP + L-lysine + tRNALysUUU
AMP + L-lysyl-tRNALysUUU + diphosphate
-
anticodon variant tRNA substrate from Escherichia coli
-
?
ATP + L-lysine + tRNALysUUU
AMP + L-lysyl-tRNALysUUU + diphosphate
-
-
-
-
?
ATP + L-lysine + tRNALysUUU
AMP + L-lysyl-tRNALysUUU + diphosphate
-
-
-
-
?
ATP + L-lysine + tRNALysUUU
AMP + L-lysyl-tRNALysUUU + diphosphate
-
-
-
?
ATP + L-lysine + tRNALysUUU
AMP + L-lysyl-tRNALysUUU + diphosphate
-
-
-
?
ATP + L-lysine + tRNALysUUU
AMP + L-lysyl-tRNALysUUU + diphosphate
-
-
-
-
?
ATP + L-lysine ethyl ester + tRNALys
AMP + ethyl-L-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + L-lysine ethyl ester + tRNALys
AMP + ethyl-L-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + L-lysine hydroxamate + tRNALys
AMP + L-lysine hydroxamoyl-tRNALys + diphosphate
-
-
-
?
ATP + L-lysine hydroxamate + tRNALys
AMP + L-lysine hydroxamoyl-tRNALys + diphosphate
-
-
-
r
ATP + L-lysine methyl ester + tRNALys
AMP + methyl-L-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + L-lysine methyl ester + tRNALys
AMP + methyl-L-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
tRNALys from Saccharomyces cerevisiae, recombinant N-terminal extension provides the enzyme with RNA binding properties, the N-terminally truncated enzyme is no longer able to bind the RNA substrate
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
the enzymes major function is to provide Lys-tRNALys fpr protein biosynthesis
-
r
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
r
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
two-step reaction mechansim, the first step of formation of the aminoacylated enzyme-AMP intermediate is reversible, the second of amino acid transfer to the tRNA is not, binding of L-lysine alone influences the fluorescence of the enzyme, while binding of ATP does not
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
accepts tRNA nucleotide 73 variants: G73, A73, C73 and U73, E. coli tRNA is aminoacylated
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
human tRNALys wild-type
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
-
?
ATP + lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
-
?
ATP + ornithine + tRNALys
AMP + ornithyl-tRNALys + diphosphate
-
low activity
-
?
ATP + ornithine + tRNALys
AMP + ornithyl-tRNALys + diphosphate
-
-
-
?
additional information
?
-
the enzyme also performs the ATP-diphosphate exchange reaction, class I lysine-tRNA synthetases recognize the same elements in tRNALys as their class II counterparts, namely the discriminator base N73 and the anticodon, but vary in the recognition of the G2.U71 wobble pair of spirochete tRNALys, which acts as a determinant for class II enzymes, but not for class I enzymes
-
?
additional information
?
-
-
substrate recognition specificity, the enzyme also performs the ATP-diphosphate exchange reaction, class I lysine-tRNA synthetases recognize the same elements in tRNALys as their class II counterparts, namely the discriminator base N73 and the anticodon, but vary in the recognition of the G2.U71 wobble pair of spirochete tRNALys, which acts as a determinant for class II enzymes, but not for class I enzymes
-
?
additional information
?
-
-
phylogenetic comparison
-
?
additional information
?
-
-
aminoacyl-tRNA is channeled in vivo by probably direct transfer to elongation factor I
-
?
additional information
?
-
binding strutcure analysis of enzyme KRS with ATP, AMP, Lys, and analogue AMPPNP
-
-
?
additional information
?
-
-
binding strutcure analysis of enzyme KRS with ATP, AMP, Lys, and analogue AMPPNP
-
-
?
additional information
?
-
-
lysine-dependent ATP-diphosphate exchange reaction: lysine + ATP + enzyme/lysine-AMP-enzyme + diphosphate
-
-
?
additional information
?
-
-
synthesis of mixed dinucleoside 5',5'''-P1,P4-triphosphates or 5',5''''-P1,P4-tetraphosphates resulting from the reaction of lysyl adenylate with a variety of ribonucleotide 5'-triphosphates, ribonucleotide 5'-diphosphates, deoxyribonucleotide 5'-diphosphates or deoxyribonucleotide 5'-triphosphates
-
-
?
additional information
?
-
-
L-lysine-dependent synthesis of 5',5'-diadenosine tetraphosphate (Ap4A)
-
-
?
additional information
?
-
-
substrate recognition specificity, the enzyme also performs the ATP-diphosphate exchange reaction, class II lysine-tRNA synthetases recognize the same elements in tRNALys as their class I counterparts, namely the discriminator base N73 and the anticodon, but vary in the recognition of the G2.U71 wobble pair of spirochete tRNALys, which acts as a determinant for class II enzymes, but not for class I enzymes
-
?
additional information
?
-
-
the enzyme possesses an efficient pre-transfer editing mechanism which prevents misacylation of tRNALys with ornithine, which results in cyclization to ornithine lactam
-
?
additional information
?
-
-
the enzyme also converts ATP to diadenosine tri- and tetraphosphates in the presence of L-lysine/Mg2+/Zn2+
-
-
?
additional information
?
-
LysU-based preparation of potentially important ApnA analogues, overview. Dimeric LysU has dual diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) and diadenosine-5',5'''-P1,P3-triphosphate (Ap3A) synthase activities. Syntheses of both take place through the formation of a lysyl-adenylate 1 intermediate from ATP and L-lysine. Thereafter, the terminal phosphate of a second nucleotide substrate combines with the enzyme-bound lysyl-adenylate, thereby liberating free L-lysine and generating either Ap4A or Ap3A depending upon the identity of the second nucleotide substrate. The first step involving lysyladenylate intermediate formation is highly specific but reversible. Therefore inorganic diphosphatase-mediated controlled hydrolysis of diphosphate is required in order to prevent the back-reaction taking place, and thereby essentially rendering this first step committed. Fortunately, the second product formation step is highly promiscuous and a wide variety of nucleotide di-, tri-, and tetraphosphates are acceptable as second nucleotide substrates. This promiscuity also extends to inorganic phosphate and to tripolyphosphate. Surface mechanism of LysU catalyzed Ap4A and Ap3A synthase activities, reaction scheme and mechanism, overview. Bulkier putative diphosphate analogue substrates preclude molecular recognition and binding by LysU, hence preventing their use as bona fide LysU substrates able to couple to the ATP derived lysyl adenylate 1 intermediate with LysU assistance. Synthesis of analogues beta,gamma-methylene-P1,P4-bis(5'-adenosyl) tetraphosphate, beta,gamma-imido-P1,P4-bis(5'-adenosyl) tetraphosphate, (open-ring-ribosyl)2-beta,gamma-methylene-P1,P4-bis(5'-adenosyl) tetraphosphate, (open-ring-ribosyl)2-beta,gamma-imido-P1,P4-bis(5'-adenosyl) tetraphosphate, (open-ring-ribosyl)-beta,gamma-methylene-P1,P4-bis(5'-adenosyl) tetraphosphate, (open-ring-ribosyl)-beta,gamma-imido-P1,P4-bis(5'-adenosyl) tetraphosphate, alpha,beta-methylene 5'-P1,P3-bis(5'-adenosyl) triphosphate, alpha,beta-methylene-guanosine 5'-P1-triphospho-P3-5''-adenosine, beta,gamma-methylene-P1,P5-bis(5'-adenosyl) pentaphosphate, beta,gamma-imido-adenosine 5'-P1-pentaphospho-P5-5''-uridine, beta,gamma-methylene-adenosine 5'-P1-tretraphospho-P4-5''-guanosine, beta,gamma-imido-adenosine 5'-P1-tretraphospho-P4-5''-guanosine, and beta,gamma-delta,epsilon-dimethylene-P1,P6-bis(5'-adenosyl) hexaphosphate
-
-
?
additional information
?
-
-
LysU-based preparation of potentially important ApnA analogues, overview. Dimeric LysU has dual diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) and diadenosine-5',5'''-P1,P3-triphosphate (Ap3A) synthase activities. Syntheses of both take place through the formation of a lysyl-adenylate 1 intermediate from ATP and L-lysine. Thereafter, the terminal phosphate of a second nucleotide substrate combines with the enzyme-bound lysyl-adenylate, thereby liberating free L-lysine and generating either Ap4A or Ap3A depending upon the identity of the second nucleotide substrate. The first step involving lysyladenylate intermediate formation is highly specific but reversible. Therefore inorganic diphosphatase-mediated controlled hydrolysis of diphosphate is required in order to prevent the back-reaction taking place, and thereby essentially rendering this first step committed. Fortunately, the second product formation step is highly promiscuous and a wide variety of nucleotide di-, tri-, and tetraphosphates are acceptable as second nucleotide substrates. This promiscuity also extends to inorganic phosphate and to tripolyphosphate. Surface mechanism of LysU catalyzed Ap4A and Ap3A synthase activities, reaction scheme and mechanism, overview. Bulkier putative diphosphate analogue substrates preclude molecular recognition and binding by LysU, hence preventing their use as bona fide LysU substrates able to couple to the ATP derived lysyl adenylate 1 intermediate with LysU assistance. Synthesis of analogues beta,gamma-methylene-P1,P4-bis(5'-adenosyl) tetraphosphate, beta,gamma-imido-P1,P4-bis(5'-adenosyl) tetraphosphate, (open-ring-ribosyl)2-beta,gamma-methylene-P1,P4-bis(5'-adenosyl) tetraphosphate, (open-ring-ribosyl)2-beta,gamma-imido-P1,P4-bis(5'-adenosyl) tetraphosphate, (open-ring-ribosyl)-beta,gamma-methylene-P1,P4-bis(5'-adenosyl) tetraphosphate, (open-ring-ribosyl)-beta,gamma-imido-P1,P4-bis(5'-adenosyl) tetraphosphate, alpha,beta-methylene 5'-P1,P3-bis(5'-adenosyl) triphosphate, alpha,beta-methylene-guanosine 5'-P1-triphospho-P3-5''-adenosine, beta,gamma-methylene-P1,P5-bis(5'-adenosyl) pentaphosphate, beta,gamma-imido-adenosine 5'-P1-pentaphospho-P5-5''-uridine, beta,gamma-methylene-adenosine 5'-P1-tretraphospho-P4-5''-guanosine, beta,gamma-imido-adenosine 5'-P1-tretraphospho-P4-5''-guanosine, and beta,gamma-delta,epsilon-dimethylene-P1,P6-bis(5'-adenosyl) hexaphosphate
-
-
?
additional information
?
-
-
lysine-dependent ATP-diphosphate exchange reaction: lysine + ATP + enzyme/lysine-AMP-enzyme + diphosphate
-
-
?
additional information
?
-
-
lysine-dependent ATP-diphosphate exchange reaction: lysine + ATP + enzyme/lysine-AMP-enzyme + diphosphate
-
-
?
additional information
?
-
-
L-lysine-dependent synthesis of 5',5'-diadenosine tetraphosphate (Ap4A)
-
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
lysine-dependent ATP-diphosphate exchange reaction: lysine + ATP + enzyme/lysine-AMP-enzyme + diphosphate
-
-
?
additional information
?
-
-
L-lysine-dependent synthesis of 5',5'-diadenosine tetraphosphate (Ap4A)
-
-
?
additional information
?
-
-
phylogenetic comparison
-
?
additional information
?
-
-
substrate specificity, no activity with human tRNALysU35G mutant
-
?
additional information
?
-
-
enzyme is selectively packaged into virions during assembly of the human immunodeficiency virus type 1, i.e. HIV-1, through interaction with the viral Pr55gag protein, overview
-
?
additional information
?
-
-
the enzyme signals and mediates the selective recognition and packaging of tRNALys isoacceptors into HIV particles, the human enzyme is selectively packaged into virions of the human immunodeficiency virus during virus assembly, along with and independent of its cognate tRNALys isoacceptors, packaging is mediated by the viral protein Gag, which alone is sufficient for the incorporation, determination of interaction regions
-
?
additional information
?
-
-
enzyme KRS accomplishes catalysis in two steps. The first reaction involves the activation of lysine, where KRS selectively binds lysine by using one molecule of ATP. The second reaction involves the transfer of the activated lysine (lysine-AMP) to the acceptor end of tRNALys
-
-
?
additional information
?
-
selective binding of the C-terminal region of 37 kDa laminin receptor precursor 37LRP to the KRS anticodon-binding domain, surface plasmon resonance
-
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction, class I lysine-tRNA synthetases recognize the same elements in tRNALys as their class II counterparts, namely the discriminator base N73 and the anticodon, but vary in the recognition of the G2.U71 wobble pair of spirochete tRNALys, which acts as a determinant for class II enzymes, but not for class I enzymes
-
?
additional information
?
-
-
phylogenetic comparison
-
?
additional information
?
-
lysyl-tRNA synthetase from Myxococcus xanthus catalyzes the formation of diadenosine penta- and hexaphosphates from adenosine tetraphosphate
-
-
?
additional information
?
-
-
lysyl-tRNA synthetase from Myxococcus xanthus catalyzes the formation of diadenosine penta- and hexaphosphates from adenosine tetraphosphate
-
-
?
additional information
?
-
enzyme LysS produces diadenosine tetraphosphate (Ap4A) from ATP in the presence of Mn2+, it also generates Ap4 from ATP and triphosphate. When ATP and Ap4 are incubated with LysS and diphosphatase, first Ap4A, Ap5A, and ADP, and then Ap5, Ap6A, and Ap3A are generated. In the first reaction step, LysS can form lysyl-AMP and lysyl-ADP intermediates from Ap4 and release triphosphate and diphosphate, respectively, whereas in the second step, it can produce Ap5 from lysyl-ADP with triphosphate, and Ap6A from lysyl-ADP with Ap4. In addition, in the presence of Ap4 and diphosphatase, but absence of ATP, LysS also generates diadenosine oligophosphates (ApnAs: n = 3-6). The formation of diadenosine tetraphosphate (Ap4A) by LysS is inhibited by tRNA(Lys) in the presence of 1 mM ATP
-
-
?
additional information
?
-
-
enzyme LysS produces diadenosine tetraphosphate (Ap4A) from ATP in the presence of Mn2+, it also generates Ap4 from ATP and triphosphate. When ATP and Ap4 are incubated with LysS and diphosphatase, first Ap4A, Ap5A, and ADP, and then Ap5, Ap6A, and Ap3A are generated. In the first reaction step, LysS can form lysyl-AMP and lysyl-ADP intermediates from Ap4 and release triphosphate and diphosphate, respectively, whereas in the second step, it can produce Ap5 from lysyl-ADP with triphosphate, and Ap6A from lysyl-ADP with Ap4. In addition, in the presence of Ap4 and diphosphatase, but absence of ATP, LysS also generates diadenosine oligophosphates (ApnAs: n = 3-6). The formation of diadenosine tetraphosphate (Ap4A) by LysS is inhibited by tRNA(Lys) in the presence of 1 mM ATP
-
-
?
additional information
?
-
lysyl-tRNA synthetases efficiently produce diadenosine tetraphosphate (Ap4A) from lysyl-AMP with ATP in the absence of tRNA. When incubated with ATP, Mn2+, lysine, and inorganic diphosphatase, LysS first produces Ap4A and ADP, then converts Ap4A to diadenosine triphosphate (Ap3A), and finally converts Ap3A to ADP, the end product of the reaction. Recombinant LysS retains Ap4A synthase activity without lysine addition. When incubated with Ap4A (minus pyrophosphatase), LysS converts Ap4A mainly ATP and AMP, or ADP in the presence or absence of lysine, respectively. LysS converts Ap4A to yield ATP and AMP when Mn2+ and lysine are present, formation of ATP is higher than that of AMP. LysS hydrolyzes Ap4A symmetrically yielding ADP
-
-
?
additional information
?
-
-
lysyl-tRNA synthetases efficiently produce diadenosine tetraphosphate (Ap4A) from lysyl-AMP with ATP in the absence of tRNA. When incubated with ATP, Mn2+, lysine, and inorganic diphosphatase, LysS first produces Ap4A and ADP, then converts Ap4A to diadenosine triphosphate (Ap3A), and finally converts Ap3A to ADP, the end product of the reaction. Recombinant LysS retains Ap4A synthase activity without lysine addition. When incubated with Ap4A (minus pyrophosphatase), LysS converts Ap4A mainly ATP and AMP, or ADP in the presence or absence of lysine, respectively. LysS converts Ap4A to yield ATP and AMP when Mn2+ and lysine are present, formation of ATP is higher than that of AMP. LysS hydrolyzes Ap4A symmetrically yielding ADP
-
-
?
additional information
?
-
lysyl-tRNA synthetases efficiently produce diadenosine tetraphosphate (Ap4A) from lysyl-AMP with ATP in the absence of tRNA. When incubated with ATP, Mn2+, lysine, and inorganic diphosphatase, LysS first produces Ap4A and ADP, then converts Ap4A to diadenosine triphosphate (Ap3A), and finally converts Ap3A to ADP, the end product of the reaction. Recombinant LysS retains Ap4A synthase activity without lysine addition. When incubated with Ap4A (minus pyrophosphatase), LysS converts Ap4A mainly ATP and AMP, or ADP in the presence or absence of lysine, respectively. LysS converts Ap4A to yield ATP and AMP when Mn2+ and lysine are present, formation of ATP is higher than that of AMP. LysS hydrolyzes Ap4A symmetrically yielding ADP
-
-
?
additional information
?
-
lysyl-tRNA synthetase from Myxococcus xanthus catalyzes the formation of diadenosine penta- and hexaphosphates from adenosine tetraphosphate
-
-
?
additional information
?
-
enzyme LysS produces diadenosine tetraphosphate (Ap4A) from ATP in the presence of Mn2+, it also generates Ap4 from ATP and triphosphate. When ATP and Ap4 are incubated with LysS and diphosphatase, first Ap4A, Ap5A, and ADP, and then Ap5, Ap6A, and Ap3A are generated. In the first reaction step, LysS can form lysyl-AMP and lysyl-ADP intermediates from Ap4 and release triphosphate and diphosphate, respectively, whereas in the second step, it can produce Ap5 from lysyl-ADP with triphosphate, and Ap6A from lysyl-ADP with Ap4. In addition, in the presence of Ap4 and diphosphatase, but absence of ATP, LysS also generates diadenosine oligophosphates (ApnAs: n = 3-6). The formation of diadenosine tetraphosphate (Ap4A) by LysS is inhibited by tRNA(Lys) in the presence of 1 mM ATP
-
-
?
additional information
?
-
-
aminoacyl-tRNA is channeled in vivo by probably direct transfer to elongation factor I
-
?
additional information
?
-
the enzyme is also capable of synthesizing the signalling molecule diadenosine tetraphosphate using ATP as a substrate in the presence of L-Lys and Zn2+
-
-
?
additional information
?
-
-
the enzyme is also capable of synthesizing the signalling molecule diadenosine tetraphosphate using ATP as a substrate in the presence of L-Lys and Zn2+
-
-
?
additional information
?
-
-
L-lysine-dependent synthesis of 5',5'-diadenosine tetraphosphate (Ap4A)
-
-
?
additional information
?
-
-
lysine-dependent ATP-diphosphate exchange reaction: lysine + ATP + enzyme/lysine-AMP-enzyme + diphosphate
-
-
?
additional information
?
-
-
discrimination of amino acids by native and phosphorylated enzyme species, relative low discrimination factors
-
-
?
additional information
?
-
-
substrate specificity in the ATP-diphosphate exchange with regard to ATP analogs
-
-
?
additional information
?
-
pneumococcal LysRS mischarges both tRNALys isoacceptors with multiple amino acids requiring a posttransfer editing mechanism
-
-
?
additional information
?
-
analysis of the aminoacylation profiles of class II lysyl-tRNA synthetase (LysRS)
-
-
?
additional information
?
-
pneumococcal LysRS mischarges both tRNALys isoacceptors with multiple amino acids requiring a posttransfer editing mechanism
-
-
?
additional information
?
-
analysis of the aminoacylation profiles of class II lysyl-tRNA synthetase (LysRS)
-
-
?
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Acidosis, Lactic
Inhibition of mitochondrial translation in fibroblasts from a patient expressing the KARS p.(Pro228Leu) variant and presenting with sensorineural deafness, developmental delay, and lactic acidosis.
Carcinogenesis
Function of membranous lysyl-tRNA synthetase and its implication for tumorigenesis.
Carcinoma
Correction: Serine 207 phosphorylated lysyl-tRNA synthetase predicts disease-free survival of non-small-cell lung carcinoma.
Carcinoma
Lysyl-tRNA Synthetase (KRS) Expression in Gastric Carcinoma and Tumor-Associated Inflammation.
Carcinoma
Serine 207 phosphorylated lysyl-tRNA synthetase predicts disease-free survival of non-small-cell lung carcinoma.
Carcinoma, Non-Small-Cell Lung
Correction: Serine 207 phosphorylated lysyl-tRNA synthetase predicts disease-free survival of non-small-cell lung carcinoma.
Carcinoma, Non-Small-Cell Lung
Serine 207 phosphorylated lysyl-tRNA synthetase predicts disease-free survival of non-small-cell lung carcinoma.
Cardiomyopathies
Inhibition of mitochondrial translation in fibroblasts from a patient expressing the KARS p.(Pro228Leu) variant and presenting with sensorineural deafness, developmental delay, and lactic acidosis.
Charcot-Marie-Tooth Disease
Loss-of-function mutations in Lysyl-tRNA synthetase cause various leukoencephalopathy phenotypes.
Colonic Neoplasms
Erratum: Noncanonical roles of membranous lysyl-tRNA synthetase in transducing cell-substrate signaling for invasive dissemination of colon cancer spheroids in 3D collagen I gels.
Colonic Neoplasms
Noncanonical roles of membranous lysyl-tRNA synthetase in transducing cell-substrate signaling for invasive dissemination of colon cancer spheroids in 3D collagen I gels.
Colonic Neoplasms
Plasma Lysyl-tRNA Synthetase 1 (KARS1) as a Novel Diagnostic and Monitoring Biomarker for Colorectal Cancer.
Colorectal Neoplasms
Plasma Lysyl-tRNA Synthetase 1 (KARS1) as a Novel Diagnostic and Monitoring Biomarker for Colorectal Cancer.
Cryptosporidiosis
Lysyl-tRNA synthetase as a drug target in malaria and cryptosporidiosis.
Deafness
Inhibition of mitochondrial translation in fibroblasts from a patient expressing the KARS p.(Pro228Leu) variant and presenting with sensorineural deafness, developmental delay, and lactic acidosis.
Hearing Loss
Leopard-like retinopathy and severe early-onset portal hypertension expand the phenotype of KARS1-related syndrome: a case report.
Hearing Loss
Loss-of-function mutations in Lysyl-tRNA synthetase cause various leukoencephalopathy phenotypes.
Hearing Loss
Mutations in KARS, encoding lysyl-tRNA synthetase, cause autosomal-recessive nonsyndromic hearing impairment DFNB89.
Hearing Loss
Novel mutations in KARS cause hypertrophic cardiomyopathy and combined mitochondrial respiratory chain defect.
Hearing Loss
Structural analyses of a human lysyl-tRNA synthetase mutant associated with autosomal recessive nonsyndromic hearing impairment.
Infections
HIV-1 exploits dynamic multi-aminoacyl-tRNA synthetase complex to enhance viral replication.
Infections
Production of New Cladosporin Analogues by Reconstitution of the Polyketide Synthases Responsible for the Biosynthesis of this Antimalarial Agent.
Influenza, Human
High-yield soluble expression of recombinant influenza virus antigens from Escherichia coli and their potential uses in diagnosis.
Leukoencephalopathies
Loss-of-function mutations in Lysyl-tRNA synthetase cause various leukoencephalopathy phenotypes.
Liver Failure
Leopard-like retinopathy and severe early-onset portal hypertension expand the phenotype of KARS1-related syndrome: a case report.
Loiasis
Protein Translation Enzyme lysyl-tRNA Synthetase Presents a New Target for Drug Development against Causative Agents of Loiasis and Schistosomiasis.
Lung Neoplasms
Serine 207 phosphorylated lysyl-tRNA synthetase predicts disease-free survival of non-small-cell lung carcinoma.
Lyme Disease
Archaeal-type lysyl-tRNA synthetase in the Lyme disease spirochete Borrelia burgdorferi.
Lyme Disease
Differentiation of Borrelia burgdorferi sensu lato strains using class I lysyl-tRNA synthetase-encoding genes.
Lyme Disease
Nonorthologous replacement of lysyl-tRNA synthetase prevents addition of lysine analogues to the genetic code.
Lyme Disease
Transfer RNA recognition by class I lysyl-tRNA synthetase from the Lyme disease pathogen Borrelia burgdorferi.
Lymphatic Metastasis
Serine 207 phosphorylated lysyl-tRNA synthetase predicts disease-free survival of non-small-cell lung carcinoma.
Lymphoma
Inhibition of Plasmodium falciparum Lysyl-tRNA synthetase via an anaplastic lymphoma kinase inhibitor.
Malaria
Lysyl-tRNA synthetase as a drug target in malaria and cryptosporidiosis.
Malaria
Side chain rotameric changes and backbone dynamics enable specific cladosporin binding in Plasmodium falciparum lysyl-tRNA synthetase.
Malaria
Structural analysis of malaria-parasite lysyl-tRNA synthetase provides a platform for drug development.
Malaria
Structural basis of malaria parasite lysyl-tRNA synthetase inhibition by cladosporin.
Microcephaly
Leopard-like retinopathy and severe early-onset portal hypertension expand the phenotype of KARS1-related syndrome: a case report.
Microcephaly
Loss-of-function mutations in Lysyl-tRNA synthetase cause various leukoencephalopathy phenotypes.
Microcephaly
Novel mutations in KARS cause hypertrophic cardiomyopathy and combined mitochondrial respiratory chain defect.
Microphthalmos
Diadenosine tetraphosphate hydrolase is part of the transcriptional regulation network in immunologically activated mast cells.
Microphthalmos
Mutation in KARS: A novel mechanism for severe anaphylaxis.
Microphthalmos
Nonconventional involvement of LysRS in the molecular mechanism of USF2 transcriptional activity in FcepsilonRI-activated mast cells.
Microphthalmos
Structural context for mobilization of a human tRNA synthetase from its cytoplasmic complex.
Myocardial Ischemia
[Seasonal differences in activity of tRNA and aminoacyl-tRNA synthetases of rabbit liver in myocardial ischemia]
Neoplasm Metastasis
Characterization of the interaction between lysyl-tRNA synthetase and laminin receptor by NMR.
Neoplasm Metastasis
Chemical inhibition of prometastatic lysyl-tRNA synthetase-laminin receptor interaction.
Neoplasm Metastasis
Discovery of novel potent migrastatic Thiazolo[5,4-b]pyridines targeting Lysyl-tRNA synthetase (KRS) for treatment of Cancer metastasis.
Neoplasm Metastasis
Serine 207 phosphorylated lysyl-tRNA synthetase predicts disease-free survival of non-small-cell lung carcinoma.
Neoplasm Metastasis
Suppression of lysyl-tRNA synthetase, KRS, causes incomplete epithelial-mesenchymal transition and ineffective cell?extracellular matrix adhesion for migration.
Neoplasms
Caspase-8 controls the secretion of inflammatory lysyl-tRNA synthetase in exosomes from cancer cells.
Neoplasms
Characterization of the interaction between lysyl-tRNA synthetase and laminin receptor by NMR.
Neoplasms
Chemical inhibition of prometastatic lysyl-tRNA synthetase-laminin receptor interaction.
Neoplasms
Discovery of novel potent migrastatic Thiazolo[5,4-b]pyridines targeting Lysyl-tRNA synthetase (KRS) for treatment of Cancer metastasis.
Neoplasms
Function of membranous lysyl-tRNA synthetase and its implication for tumorigenesis.
Neoplasms
Interaction of two translational components, lysyl-tRNA synthetase and p40/37LRP, in plasma membrane promotes laminin-dependent cell migration.
Neoplasms
KRS: A cut away from release in exosomes.
Neoplasms
Suppression of lysyl-tRNA synthetase, KRS, causes incomplete epithelial-mesenchymal transition and ineffective cell?extracellular matrix adhesion for migration.
Neoplasms
The biological process of lysine-tRNA charging is therapeutically targetable in liver cancer.
Osteosarcoma
Nuclear localization of aminoacyl-tRNA synthetases using single-cell capillary electrophoresis laser-induced fluorescence analysis.
Peripheral Nervous System Diseases
Compound heterozygosity for loss-of-function lysyl-tRNA synthetase mutations in a patient with peripheral neuropathy.
Polyneuropathies
Novel mutations in KARS cause hypertrophic cardiomyopathy and combined mitochondrial respiratory chain defect.
Schistosomiasis
Protein Translation Enzyme lysyl-tRNA Synthetase Presents a New Target for Drug Development against Causative Agents of Loiasis and Schistosomiasis.
Starvation
Exosomal secretion of truncated cytosolic lysyl-tRNA synthetase induces inflammation during cell starvation.
Syphilis
Comparative modeling of class 1 lysyl tRNA synthetase from Treponema pallidum.
Tuberculosis
Essentiality Assessment of Cysteinyl and Lysyl-tRNA Synthetases of Mycobacterium smegmatis.
Vision Disorders
Loss-of-function mutations in Lysyl-tRNA synthetase cause various leukoencephalopathy phenotypes.
Vision Disorders
Novel mutations in KARS cause hypertrophic cardiomyopathy and combined mitochondrial respiratory chain defect.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.1
2-Chloroadenosine 5'-triphosphate
-
aminoacylation
1.5
AMP
-
5',5'''-P1,P4-tetraphosphate formation
0.002 - 0.0043
Borellia burgdorferi tRNALys
-
0.0039 - 0.0063
Escherichia coli G2.U71 tRNA
-
0.0015 - 0.0019
Escherichia coli wild type tRNA
-
0.2
Formycin 5'-triphosphate
-
aminoacylation
0.003 - 0.0117
human tRNALys3
-
0.000007 - 0.0057
tRNALys
0.00057
tRNALys from rat liver
-
-
-
0.00056 - 1.4
tRNALysCUU
-
0.00033 - 1.5
tRNALysGUU
-
0.0078
tRNALysU35C
-
human mutant tRNALys, 30°C
-
0.0095
tRNALysU36A
-
human mutant tRNALys, 30°C
-
0.0037
tRNALysU36C
-
human mutant tRNALys, 30°C
-
0.0004 - 5.1
tRNALysUUU
-
0.0015
tRNALysUUUmodified
-
-
-
0.002 - 0.0028
yeast tRNALys
-
additional information
additional information
-
0.00015
ATP
-
-
0.0078
ATP
-
pH 7.2, 37°C, mutant enzyme E278Q
0.0078
ATP
-
pH 7.2, 37°C, mutant enzyme E428Q
0.01
ATP
-
lysylation, 28S synthetase complex
0.011
ATP
-
pH 7.2, 37°C, mutant enzyme E240D
0.012
ATP
-
pH 7.2, 37°C, wild-type enzyme
0.014
ATP
-
pH 7.2, 37°C, mutant enzyme E240Q
0.016
ATP
-
pH 7.2, 37°C, mutant enzyme E278D
0.019
ATP
-
pH 7.2, 37°C, mutant enzyme F426H
0.02
ATP
-
pH 7.2, 37°C, mutant enzyme E428D
0.021
ATP
-
pH 7.2, 37°C, mutant enzyme N424D
0.023
ATP
native enzyme, pH 8.0, 30°C
0.0232
ATP
-
aminoacylation
0.037
ATP
-
aminoacylation, enzyme form EII
0.038
ATP
-
aminoacylation reaction, recombinant mutant W332F, pH 8.0, 37°C
0.041
ATP
recombinant T7-tagged enzyme, pH 8.0, 30°C
0.043
ATP
-
aminoacylation reaction, recombinant wild-type enzyme, pH 8.0, 37°C
0.043
ATP
recombinant enzyme without t7-tag
0.049
ATP
-
aminoacylation reaction, recombinant mutant W314F, pH 8.0, 37°C
0.062
ATP
-
pH 7.2, 37°C, mutant enzyme Y280F
0.0651
ATP
-
ATP-diphosphate exchange
0.066
ATP
-
aminoacylation reaction, recombinant mutant W314F/W332F, pH 8.0, 37°C
0.11
ATP
-
pH 7.2, 37°C, mutant enzyme F426W
0.147
ATP
-
pH 7.2, 37°C, mutant enzyme Y280S
0.195
ATP
-
recombinant N-terminally truncated enzyme, pH 7.5, 25°C
0.195
ATP
-
pH 7.2, 37°C, mutant enzyme G216A
0.25
ATP
-
recombinant wild-type enzyme, pH 7.5, 25°C
0.33
ATP
-
aminoacylation, enzyme form EI
0.83
ATP
-
pH 7.2, 37°C, mutant enzyme N424Q
1.3
ATP
-
wild type enzyme
1.6
ATP
-
mutant enzyme Y269F
1.7
ATP
-
mutant enzyme T31S
2.1
ATP
-
5',5'''-P1,P4-tetraphosphate formation
6.9
ATP
-
mutant enzyme Y269S
9.5
ATP
-
mutant enzyme T31G
0.002
Borellia burgdorferi tRNALys
-
recombinant enzyme, pH 7.2, 37°C
-
0.0043
Borellia burgdorferi tRNALys
-
recombinant enzyme, pH 7.2, 37°C
-
0.0039
Escherichia coli G2.U71 tRNA
-
recombinant enzyme, pH 7.2, 37°C
-
0.0063
Escherichia coli G2.U71 tRNA
-
recombinant enzyme, pH 7.2, 37°C
-
0.0015
Escherichia coli wild type tRNA
-
recombinant enzyme, pH 7.2, 37°C
-
0.0019
Escherichia coli wild type tRNA
-
recombinant enzyme, pH 7.2, 37°C
-
0.003
human tRNALys3
-
recombinant wild-type enzyme, pH 7.5, 25°C
-
0.0117
human tRNALys3
-
recombinant N-terminally truncated enzyme, pH 7.5, 25°C
-
0.0025
L-Lys
-
-
0.005
L-Lys
-
ATP, , lysylation, free enzyme
0.005
L-Lys
-
aminoacylation, enzyme form EII
0.006
L-Lys
-
aminoacylation, enzyme form EI
0.0164
L-Lys
-
aminoacylation
0.0236
L-Lys
-
ATP-diphosphate exchange
0.0013
L-lysine
-
pH 7.2, 37°C, mutant enzyme E428Q
0.0014
L-lysine
-
pH 7.2, 37°C, mutant enzyme E278Q
0.0026
L-lysine
-
pH 7.2, 37°C, wild-type enzyme
0.0033
L-lysine
-
pH 7.2, 37°C, mutant enzyme E240D
0.0036
L-lysine
-
pH 7.2, 37°C, mutant enzyme E240Q
0.0052
L-lysine
-
pH 7.2, 37°C, mutant enzyme N424D
0.0066
L-lysine
-
at 25°C, in 250 mM KCl, 100 mM HEPES, pH 7.5, 10 mM dithiothreitol, 10 mM MgCl2, 0.05 mg/ml bovine serum albumin
0.009
L-lysine
-
ATP-diphosphate exchange reaction, recombinant wild-type enzyme and mutant W314F/W332F, pH 8.0, 37°C
0.01
L-lysine
-
ATP-diphosphate exchange reaction, recombinant mutant W314F, pH 8.0, 37°C
0.016
L-lysine
-
aminoacylation reaction, recombinant wild-type enzyme, pH 8.0, 37°C
0.016
L-lysine
native enzyme, pH 8.0, 30°C
0.016
L-lysine
-
pH 7.2, 37°C, mutant enzyme F426W
0.017
L-lysine
-
aminoacylation reaction, recombinant mutants W314F and W314F/W332F, pH 8.0, 37°C
0.018
L-lysine
-
ATP-diphosphate exchange reaction, recombinant mutant W332F, pH 8.0, 37°C
0.022
L-lysine
-
aminoacylation reaction, recombinant mutant W332F, pH 8.0, 37°C
0.022
L-lysine
-
pH 7.2, 37°C, mutant enzyme E428D
0.023
L-lysine
recombinant T7-tagged enzyme, pH 8.0, 30°C
0.024
L-lysine
recombinant enzyme without t7-tag
0.024
L-lysine
-
pH 7.2, 37°C, mutant enzyme Y280F
0.052
L-lysine
-
pH 7.2, 37°C, mutant enzyme N424Q
0.092
L-lysine
-
recombinant wild-type enzyme, pH 7.5, 25°C
0.104
L-lysine
-
recombinant N-terminally truncated enzyme, pH 7.5, 25°C
0.114
L-lysine
-
pH 7.2, 37°C, mutant enzyme Y280S
0.16
L-lysine
-
wild type enzyme, in 100 mM HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, at 37°C
0.18
L-lysine
-
mutant enzyme H242L
0.196
L-lysine
-
pH 7.2, 37°C, mutant enzyme G216A
0.2 - 1
L-lysine
-
mutant enzyme A233S, in 100 mM HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, at 37°C
0.203
L-lysine
-
pH 7.2, 37°C, mutant enzyme F426H
0.23
L-lysine
-
wild type enzyme
0.254
L-lysine
-
pH 7.2, 37°C, mutant enzyme E278D
0.33
L-lysine
-
mutant enzyme W220A
0.4
L-lysine
-
mutant enzyme Y269F
0.76
L-lysine
-
mutant enzyme T31S
2.8
L-lysine
-
mutant enzyme Y269S
3.3
L-lysine
-
mutant enzyme H242A
3.3
L-lysine
-
mutant enzyme W220L
3.9
L-lysine
-
mutant enzyme G469A, in 100 mM HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, at 37°C
4.4
L-lysine
-
mutant enzyme T31G
4.7
L-lysine
-
mutant enzyme W220Y
6.3
L-lysine
-
mutant enzyme G29A
8.1
L-lysine
-
ATP-diphosphate exchange reaction, recombinant mutant Y271F, pH 8.0, 37°C
0.0024
Lys
-
-
0.0037
Lys
-
lysylation, 18S synthetase complex
0.004
Lys
-
aminoacylation
0.0047
Lys
-
lysylation, free enzyme
0.000007
tRNALys
-
lysylation, free enzyme
0.00002
tRNALys
-
lysylation, 18S synthetase complex
0.00074
tRNALys
-
at 25°C, in 250 mM KCl, 100 mM HEPES, pH 7.5, 10 mM dithiothreitol, 10 mM MgCl2, 0.05 mg/ml bovine serum albumin
0.002
tRNALys
-
aminoacylation, enzyme form EI
0.0034
tRNALys
-
human wild-type tRNALys, 30°C, wild-type and N-terminally truncated mutant enzymes
0.0037
tRNALys
-
human wild-type tRNALys, 20°C, wild-type enzyme
0.0057
tRNALys
-
aminoacylation, enzyme form EII
0.00056
tRNALysCUU
-
-
-
1.4
tRNALysCUU
-
wild type enzyme, at 37°C in 100 mM HEPES (pH 7.2), 25 mM KCl, 10 mM MgCl2, 4 mM dithiothreitol, and 5 mM ATP
-
0.00033
tRNALysGUU
-
-
-
1.5
tRNALysGUU
-
wild type enzyme, at 37°C in 100 mM HEPES (pH 7.2), 25 mM KCl, 10 mM MgCl2, 4 mM dithiothreitol, and 5 mM ATP
-
0.0004
tRNALysUUU
-
-
-
0.83
tRNALysUUU
-
mutant enzyme Y269F
-
0.87
tRNALysUUU
-
wild type enzyme, at 37°C in 100 mM HEPES (pH 7.2), 25 mM KCl, 10 mM MgCl2, 4 mM dithiothreitol, and 5 mM ATP
-
1
tRNALysUUU
-
mutant enzyme H242A
-
1.1
tRNALysUUU
-
mutant enzyme W220L
-
1.1
tRNALysUUU
-
mutant enzyme Y269S
-
1.2
tRNALysUUU
-
mutant enzyme W220Y
-
1.3
tRNALysUUU
-
mutant enzyme H242L
-
2
tRNALysUUU
-
wild type enzyme
-
2.1
tRNALysUUU
-
mutant enzyme T31G
-
2.1
tRNALysUUU
-
mutant enzyme T31S
-
2.5
tRNALysUUU
-
mutant enzyme W220A
-
5.1
tRNALysUUU
-
mutant enzyme G29A
-
0.002
yeast tRNALys
-
recombinant wild-type enzyme, pH 7.5, 25°C
-
0.0028
yeast tRNALys
-
recombinant N-terminally truncated enzyme, pH 7.5, 25°C
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
Km values of ATP analogues in ATP-diphosphate exchange
-
additional information
additional information
-
binding kinetics of acceptor stem and anticodon domains of the tRNALys
-
additional information
additional information
-
Km-values of tRNALys variants
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0035 - 6.08
Borellia burgdorferi tRNALys
-
0.0025 - 0.0035
Escherichia coli G2.U71 tRNA
-
0.004
Escherichia coli tRNALys
-
recombinant enzyme, pH 7.2, 37°C
-
0.002
Escherichia coli tRNALys CNBr-treated
-
recombinant enzyme, pH 7.2, 37°C
-
0.004 - 0.055
Escherichia coli wild type tRNALys
-
6.2 - 7.8
human tRNALys3
-
0.00067
L-arginyl-tRNALys
-
deacylation reaction, pH 7.4, 37°C, in absence or presence of 50 mM DTT
14.5
L-Lysine amide
-
forward reaction, pH 8.0, 30°C
221
L-Lysine hydroxamate
-
forward reaction, pH 8.0, 30°C
0.00023 - 0.0088
L-lysyl-tRNALys
0.00056
L-methionyl-tRNALys
-
deacylation reaction, pH 7.4, 37°C, in absence or presence of 50 mM DTT
-
0.00076
L-threonyl-tRNALys
-
deacylation reaction, pH 7.4, 37°C, in absence or presence of 50 mM DTT
-
0.2
Methanococcus maripaludis tRNALys
-
recombinant enzyme, pH 7.2, 37°C
-
0.05
Methanococcus maripaludis tRNALys CNBr-treated
-
recombinant enzyme, pH 7.2, 37°C
-
0.00026 - 6.08
tRNALys,3'-59mer
-
0.014 - 0.062
tRNALysCUU
-
0.0095 - 0.043
tRNALysGUU
-
0.0079
tRNALysU35C
-
human mutant tRNALys, 30°C, N-terminally truncated mutant enzyme
-
0.0068
tRNALysU36A
-
human mutant tRNALys, 30°C, N-terminally truncated mutant enzyme
-
0.046
tRNALysU36C
-
human mutant tRNALys, 30°C, N-terminally truncated mutant enzyme
-
0.00012 - 0.68
tRNALysUUU
-
0.12
tRNALysUUUmodified
-
-
-
6.3 - 7.1
yeast tRNALys
-
additional information
additional information
-
0.00051
ATP
-
mutant enzyme Y269S
0.0011
ATP
-
mutant enzyme T31G
0.013
ATP
-
pH 7.2, 37°C, mutant enzyme E240Q
0.017
ATP
-
pH 7.2, 37°C, mutant enzyme E278Q
0.017
ATP
-
pH 7.2, 37°C, mutant enzyme E428Q
0.017
ATP
-
mutant enzyme Y269F
0.054
ATP
-
pH 7.2, 37°C, mutant enzyme E278D
0.14
ATP
-
pH 7.2, 37°C, mutant enzyme E240D
0.17
ATP
-
pH 7.2, 37°C, mutant enzyme Y280F
0.3
ATP
-
ATP-diphosphate exchange reaction, recombinant mutant Y271F, pH 8.0, 37°C
0.35
ATP
-
pH 7.2, 37°C, mutant enzyme Y280S
0.57
ATP
-
wild type enzyme
0.67
ATP
-
pH 7.2, 37°C, mutant enzyme F426H
0.8
ATP
-
pH 7.2, 37°C, mutant enzyme G216A
1
ATP
-
pH 7.2, 37°C, mutant enzyme E428D
1
ATP
-
pH 7.2, 37°C, mutant enzyme N424D
1.7
ATP
-
mutant enzyme T31S
2.2
ATP
-
pH 7.2, 37°C, mutant enzyme N424Q
2.4
ATP
-
pH 7.2, 37°C, mutant enzyme F426W
3.4
ATP
-
pH 7.2, 37°C, wild-type enzyme
5
ATP
-
recombinant wild-type enzyme, pH 7.5, 25°C
5.1
ATP
-
recombinant N-terminally truncated enzyme, pH 7.5, 25°C
34.7
ATP
-
ATP-diphosphate exchange reaction, recombinant mutant Y271F, pH 8.0, 37°C
36.4
ATP
-
ATP-diphosphate exchange reaction, recombinant mutant W332F, pH 8.0, 37°C
37.3
ATP
-
ATP-diphosphate exchange reaction, recombinant mutant W314F/W332F, pH 8.0, 37°C
38.6
ATP
-
ATP-diphosphate exchange reaction, recombinant mutant W314F, pH 8.0, 37°C
40.9
ATP
-
ATP-diphosphate exchange
42.8
ATP
-
ATP-diphosphate exchange reaction, recombinant wild-type enzyme, pH 8.0, 37°C
0.0035
Borellia burgdorferi tRNALys
-
recombinant enzyme, pH 7.2, 37°C
-
0.79
Borellia burgdorferi tRNALys
-
recombinant enzyme, pH 7.2, 37°C
-
6.08
Borellia burgdorferi tRNALys
-
recombinant enzyme, pH 7.2, 37°C
-
0.0025
Escherichia coli G2.U71 tRNA
-
recombinant enzyme, pH 7.2, 37°C
-
0.0035
Escherichia coli G2.U71 tRNA
-
recombinant enzyme, pH 7.2, 37°C
-
0.004
Escherichia coli wild type tRNALys
-
recombinant enzyme, pH 7.2, 37°C
-
0.055
Escherichia coli wild type tRNALys
-
recombinant enzyme, pH 7.2, 37°C
-
6.2
human tRNALys3
-
recombinant wild-type enzyme, pH 7.5, 25°C
-
7.8
human tRNALys3
-
recombinant N-terminally truncated enzyme, pH 7.5, 25°C
-
0.00012
L-lysine
-
mutant enzyme H242A
0.00017
L-lysine
-
mutant enzyme W220L
0.00065
L-lysine
-
L-lysine lactam formation, pH 7.4, 37°C
0.00075
L-lysine
-
mutant enzyme W220A
0.0026
L-lysine
-
mutant enzyme Y269S
0.0046
L-lysine
-
mutant enzyme T31G
0.0087
L-lysine
-
pH 7.2, 37°C, mutant enzyme E240Q
0.0143
L-lysine
-
at 25°C, in 250 mM KCl, 100 mM HEPES, pH 7.5, 10 mM dithiothreitol, 10 mM MgCl2, 0.05 mg/ml bovine serum albumin
0.015
L-lysine
-
pH 7.2, 37°C, mutant enzyme E278Q
0.02
L-lysine
-
pH 7.2, 37°C, mutant enzyme E428D
0.031
L-lysine
-
pH 7.2, 37°C, mutant enzyme Y280F
0.086
L-lysine
-
pH 7.2, 37°C, mutant enzyme E240D
0.099
L-lysine
-
mutant enzyme Y269F
0.13
L-lysine
-
mutant enzyme W220Y
0.16
L-lysine
-
pH 7.2, 37°C, mutant enzyme E278D
0.29
L-lysine
-
mutant enzyme H242L
0.34
L-lysine
-
wild type enzyme
0.45
L-lysine
-
mutant enzyme G29A
0.53
L-lysine
-
mutant enzyme T31S
0.6
L-lysine
-
pH 7.2, 37°C, mutant enzyme F426W
0.65
L-lysine
-
pH 7.2, 37°C, mutant enzyme N424Q
1
L-lysine
-
pH 7.2, 37°C, mutant enzyme E428D
1.6
L-lysine
-
pH 7.2, 37°C, mutant enzyme N424D
1.6
L-lysine
-
pH 7.2, 37°C, mutant enzyme Y280S
1.8
L-lysine
-
pH 7.2, 37°C, wild-type enzyme
2.4
L-lysine
-
pH 7.2, 37°C, mutant enzyme F426H
3 - 6
L-lysine
-
aminoacylation reaction, recombinant mutant W332F, pH 8.0, 37°C
3.13
L-lysine
-
aminoacylation reaction, recombinant mutant W314F, pH 8.0, 37°C
3.13
L-lysine
-
aminoacylation reaction, recombinant wild-type enzyme, pH 8.0, 37°C
3.2
L-lysine
native enzyme, pH 8.0, 30°C
3.23
L-lysine
-
aminoacylation reaction, recombinant mutant W332F, pH 8.0, 37°C
3.3
L-lysine
-
aminoacylation reaction, recombinant mutant W314F/W332F, pH 8.0, 37°C
3.4
L-lysine
-
pH 7.2, 37°C, mutant enzyme G216A
3.53
L-lysine
-
aminoacylation reaction, recombinant wild-type enzyme, pH 8.0, 37°C
3.58
L-lysine
-
aminoacylation reaction, recombinant mutant W314F, pH 8.0, 37°C
3.6
L-lysine
recombinant enzyme without t7-tag
4.1
L-lysine
recombinant T7-tagged enzyme, pH 8.0, 30°C
5.1
L-lysine
-
recombinant N-terminally truncated enzyme, pH 7.5, 25°C
5.8
L-lysine
-
recombinant wild-type enzyme, pH 7.5, 25°C
8.2
L-lysine
-
mutant enzyme G469A, in 100 mM HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, at 37°C
41.7
L-lysine
-
wild type enzyme, in 100 mM HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, at 37°C
45.7
L-lysine
-
forward reaction, pH 8.0, 30°C
85
L-lysine
-
mutant enzyme A233S, in 100 mM HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, at 37°C
0.00023
L-lysyl-tRNALys
-
deacylation reaction, pH 7.4, 37°C, in absence of DTT
0.0088
L-lysyl-tRNALys
-
deacylation reaction, pH 7.4, 37°C, in presence of 50 mM DTT
0.34
tRNALys
-
wild-type tRNALys
0.38
tRNALys
-
human wild-type tRNALys, 30°C, N-terminally truncated mutant enzyme
1.7
tRNALys
-
human wild-type tRNALys, 20°C, wild-type enzyme
2
tRNALys
-
human wild-type tRNALys, 30°C, wild-type enzyme
2.7
tRNALys
-
18S synthetase complex
5.5
tRNALys
-
free enzyme
0.00026
tRNALys,3'-59mer
-
human tRNALys mutant + human tRNALys,3'-7mer mutant, 20°C, wild-type enzyme
-
0.88
tRNALys,3'-59mer
-
human tRNALys mutant + human tRNALys,3'-14mer mutant, 20°C, wild-type enzyme
-
1.5
tRNALys,3'-59mer
-
human tRNALys mutant + human tRNALys,3'-17mer mutant, 20°C, wild-type enzyme
-
6.08
tRNALys,3'-59mer
-
human tRNALys mutant + human tRNALys,3'-14mer mutant, 20°C, wild-type enzyme
-
0.014
tRNALysCUU
-
-
-
0.062
tRNALysCUU
-
wild type enzyme, at 37°C in 100 mM HEPES (pH 7.2), 25 mM KCl, 10 mM MgCl2, 4 mM dithiothreitol, and 5 mM ATP
-
0.0095
tRNALysGUU
-
-
-
0.043
tRNALysGUU
-
wild type enzyme, at 37°C in 100 mM HEPES (pH 7.2), 25 mM KCl, 10 mM MgCl2, 4 mM dithiothreitol, and 5 mM ATP
-
0.00012
tRNALysUUU
-
mutant enzyme W220L
-
0.00013
tRNALysUUU
-
mutant enzyme H242A
-
0.00056
tRNALysUUU
-
mutant enzyme W220A
-
0.0023
tRNALysUUU
-
mutant enzyme Y269S
-
0.005
tRNALysUUU
-
mutant enzyme T31G
-
0.14
tRNALysUUU
-
mutant enzyme Y269F
-
0.23
tRNALysUUU
-
mutant enzyme W220Y
-
0.29
tRNALysUUU
-
mutant enzyme H242L
-
0.33
tRNALysUUU
-
wild type enzyme
-
0.44
tRNALysUUU
-
wild type enzyme, at 37°C in 100 mM HEPES (pH 7.2), 25 mM KCl, 10 mM MgCl2, 4 mM dithiothreitol, and 5 mM ATP
-
0.59
tRNALysUUU
-
mutant enzyme G29A
-
0.68
tRNALysUUU
-
mutant enzyme T31S
-
6.3
yeast tRNALys
-
recombinant wild-type enzyme, pH 7.5, 25°C
-
7.1
yeast tRNALys
-
recombinant N-terminally truncated enzyme, pH 7.5, 25°C
-
additional information
additional information
-
hyperbolic dependence of kapp on the initial ATP concentration
-
additional information
additional information
-
turnover numbers of tRNALys variants
-
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evolution
-
all sequenced strains of Bacillus cereus, except strain AH820, encode both a class I and a class II LysRSs
evolution
multiple genes encode for aminoacyl-tRNA synthetases from Mycobacterium smegmatis, e.g. glutamyl (GluRS), cysteinyl (CysRS), prolyl (ProRS) and lysyl (LysRS) tRNA synthetases. Conditional expression strains of lysyl-tRNA synthetases generated in Mycobacterium smegmatis reveals that the canonical aminoacyl-tRNA synthetase are essential, while the additional ones are not essential for the growth of Mycobacterium smegmatis. The lysyl-tRNA synthetase of Mycobacterium smegmatis belongs to the class II amino acid tRNA synthetases
evolution
the enzyme belongs to the class II amino acyl-tRNA synthetases (aaRS)
evolution
the enzyme belongs to the class II aminoacyl-tRNA synthetases
evolution
the lysyl-tRNA synthetase of Mycobacterium smegmatis belongs to the class II amino acid tRNA synthetases
evolution
-
the lysyl-tRNA synthetase of Mycobacterium smegmatis belongs to the class II amino acid tRNA synthetases
-
evolution
-
all sequenced strains of Bacillus cereus, except strain AH820, encode both a class I and a class II LysRSs
-
evolution
-
multiple genes encode for aminoacyl-tRNA synthetases from Mycobacterium smegmatis, e.g. glutamyl (GluRS), cysteinyl (CysRS), prolyl (ProRS) and lysyl (LysRS) tRNA synthetases. Conditional expression strains of lysyl-tRNA synthetases generated in Mycobacterium smegmatis reveals that the canonical aminoacyl-tRNA synthetase are essential, while the additional ones are not essential for the growth of Mycobacterium smegmatis. The lysyl-tRNA synthetase of Mycobacterium smegmatis belongs to the class II amino acid tRNA synthetases
-
evolution
-
the enzyme belongs to the class II amino acyl-tRNA synthetases (aaRS)
-
malfunction
-
depletion of KARS with small interfering RNAs suppresses calreticulin exposure on the cell surface induced by anthracyclines or UVC light
malfunction
-
loss of function mutations in the catalytic domain of the enzyme are found in Charcot-Marie-Tooth disease patients. Mitochondrial enzyme binds to mutant superoxide dismutase 1, forming protein aggregates that damage mitochondrial activity and lead to disease onset in amoytophic lateral sclerosis
malfunction
aberrant expression of aminoacyl-tRNA synthetases is associated with various human cancers. Enzyme status and clinicopathological parameters reveal that the enzyme expression is correlated with a shorter overall survival. Enzyme KRS has an oncogenic role, it binds microphthalmia-associated transcription factor (MITF), which is an oncogenic transcriptional activator observed in the development of melanoma
malfunction
congenital visual impairment and progressive microcephaly due to lysyl-transfer RNA synthetase (KARS) mutations, expanding phenotype with severe infantile visual loss, progressive microcephaly, developmental delay, seizures, and abnormal subcortical white matter, overview
malfunction
-
cytosolic KRS is released from MSC and translocates to the cell membrane, where it binds to p67LR. BC-K01 and YH16899 to KRS abolishes the KRS-LR interaction
malfunction
effects of krs deletion on radial growth, conidiation capacity, and conidial quality. No significant growth defect occurred in the mutant grown on the carbon sources of sucrose and trehalose and the nitrogen sources of ten other amino acids tested. The DELTAkrs mutant exhibits a significant decrease of conidial yield by 47% on day 5 and 15-21% on days 6-8, delayed conidiation is evidenced with transcriptional repression (62-80%) of the conidiation-required genes fluG, brlA, abaA, and wetA compared to control. the hyphal bodies of Dkrs are not present in the insect haemolymph until day 7, indicating a retard of its dimorphic transition in vivo in comparison to the control strains that form abundant hyphal bodies on day 4 after the infection passing or bypassing the insect cuticle
malfunction
KRS-suppressed HCT-116 cells show increased mesenchymal markers and decreased epithelial markers 24 h after embedding of colon cancer spheroids in 3D collagen I gels. KRS-positive cells are sensitive to laminin treatment for p67LR stabilization, KRS-suppressed cells are insensitive to the laminin treatment. KRS-expressing parental cells show disseminative margins that are positive for E-cadherin expression, whereas KRS-suppressed cells show neither. Specific effect of KRS suppression on paxillin. KRS suppression decreases the phosphorylations of vinculin Tyr822 and tensin2 Tyr483, but not of talin Ser425. KRS-suppression decreases ERK1/2 phosphorylation, ERK1/2 phosphorylation is increased by KRS overexpression. Treating SW620 cells with inhibitors U1026 or YH16899 blocks dissemination
malfunction
-
effects of krs deletion on radial growth, conidiation capacity, and conidial quality. No significant growth defect occurred in the mutant grown on the carbon sources of sucrose and trehalose and the nitrogen sources of ten other amino acids tested. The DELTAkrs mutant exhibits a significant decrease of conidial yield by 47% on day 5 and 15-21% on days 6-8, delayed conidiation is evidenced with transcriptional repression (62-80%) of the conidiation-required genes fluG, brlA, abaA, and wetA compared to control. the hyphal bodies of Dkrs are not present in the insect haemolymph until day 7, indicating a retard of its dimorphic transition in vivo in comparison to the control strains that form abundant hyphal bodies on day 4 after the infection passing or bypassing the insect cuticle
-
metabolism
LysRS enzyme phosphorylation on residue Ser207 is correlated to activity of epidermal growth factor receptor and level of lymph node metastases, e.g. in lung cancer, overview. The MAPK-ERK pathway leads to the phosphorylation of LysRS and its release from the MSC in activated mast cells. Lysyl-tRNA synthetase phosphorylated on Ser207 (P-s207 LysRS) is released from the cytoplasmic multi-tRNA synthetase complex (MSC) into the nucleus, where it activates the microphthalmia-associated transcription factor (MITF) in stimulated cultured mast cells and cardiomyocytes. This specific phosphorylation results in LysRS losing its ability to acetylate tRNA but enhances its production of the second messenger diadenosine tetraphosphate (Ap4A). Ap4A has been shown to bind to the tumor suppressor Hint-1, releasing its inhibition on MITF. Patients with EGFR mutations without lymph node metastases have a higher nuclear expression of Ser207 phosphorylated LysRS (50%) as compared to patients with lymph node metastases (27.8%)
metabolism
lysyl-tRNA synthetase (KRS) is one component of multisynthetase complex that consists of eight aminoacyl-tRNA synthetases and three nonenzymatic factors known as ARS-interacting multifunctional protein
metabolism
-
Shiga toxins trigger the dissociation and secretion of KRS from the multi-aminoacyl-tRNA synthetase complex (MSC) in toxin-sensitive human macrophage-like D-THP-1 cells to enhance proinflammatory responses
metabolism
-
the pro-metastatic functions of enzyme KRS and their pathophysiological implications, overview. KRS is released from the multi-tRNA synthetase complex (MSC) and translocates to the cell membrane, where it binds to p67LR, resulting in cell migration and metastasis. Since KRS plays a key role in the structural stability of the MSC. dissociation of KRS from the MSC may affect the cellular levels of other synthetase components within the MSC. KRS/p67LR/integrin alpha6beta1 complex formation correlates with transduction of intracellular signaling for ERK1/2 activation and paxillin expression/activation
physiological function
-
silencing of LysRS leads to reduced Ap4P production in immunologically activated cells, which results in a lower level of MITF inducible genes. Specific LysRS Ser207 phosphorylation regulates Ap4P production in immunologically stimulated mast cells
physiological function
-
KARS mediates translocation of calreticulin from endoplasmic reticulum to the plasma membrane at the cell surface
physiological function
-
the T box element controlling lysK, encoding LysRS1, expression in strain 14579 is functional, but unusually responds to depletion of charged tRNALys and tRNAAsn, making LysRS1 expression responsive to a wider range of nutritional stresses, transcriptional regulation, overview
physiological function
-
the enzyme plays an essential role in HIV replication, transcriptional regulation, cytokine-like signaling, and transport of proteins to the cell membrane. The enzyme can induce cancer cell migration through interaction with the 67 kDa laminin receptor. The enzyme facilitates the translocation and surface exposure of calreticulin, activating the CRT pathway which leads to death of stressed cells
physiological function
activity of most class II aminoacyl-tRNA synthetases absolutely requires the presence of added cognate amino acids
physiological function
-
aminoacyl-tRNA synthetases (ARSs) are essential enzymes that conjugate specific amino acids to their cognate tRNAs for protein synthesis. Among human ARSs, cytosolic lysyl-tRNA synthetase (KRS) is often highly expressed in cancer cells and tissues, and facilitates cancer cell migration and invasion through the interaction with the 67 kDa laminin receptor on the plasma membrane. Human KRS interacts with the laminin receptor (LR/RPSA) and enhances cell migration upon laminin stimulation. KRS positively regulates the membrane stability of p67LR, leading to efficient signaling for cell migration during cancer metastasis. Model for the pro-metastatic function of KRS via 67LR and integrin in the plasma membrane. Laminin binds to the integrin resulting in the activation of PI3K and p38 MAPK. Then, p38MAPK phosphorylates the KRS that is bound to the N-terminus of AIMP2 in the MSC. The phosphorylated KRS is released from MSC and translocates to the plasma membrane, where it forms the KRS/p67LR/integrin complex. KRS binding to the p67LR prevents Nedd4-mediated ubiquitination resulting in stabilization of p67LR. The KRS/p67LR/integrin complex also transduces intracellular signaling favorable for cell migration, through ERKs/c-Jun./paxillin expression and paxillin activation, leading to cancer cell dissemination and migration. KRS-mediated regulation of epithelial-mesenchymal transition, overview
physiological function
aminoacyl-tRNA synthetases provide the first step in protein synthesis quality control by discriminating cognate from noncognate amino acid and tRNA substrates. While substrate specificity is enhanced in many instances by cis- and transediting pathways, it has been revealed that in organisms such as Streptococcus pneumoniae some aminoacyl tRNA synthetases display significant tRNA mischarging activity. Pneumococcal LysRS misaminoacylates tRNALys with Ala and to a lesser extent Thr and Ser, with mischarging efficiency modulated by the presence of an unusual U4:G69 wobble pair in the acceptor stems of both pneumococcal tRNALys isoacceptors. Addition of the trans-editing factor MurM, which also functions in peptidoglycan synthesis, reduces Ala-tRNALys production by LysRS, providing evidence for cross talk between the protein synthesis and cell wall biogenesis pathways. Mischarging of tRNALys by AlaRS is also observed, and this provides additional potential MurM substrates. Adaptive misaminoacylation may contribute significantly to the viability of this pathogen during amino acid starvation. In the absence of efficient pre- and/or posttransfer editing mechanisms, the distorted region in the acceptor stem of tRNALys is able to reduce the overall mischarging capacity of pneumococcal LysRS, with an accompanying loss in cognate charging
physiological function
canonical LysRS and CysRS are essential for growth of Mycobacterium smegmatis
physiological function
class II lysyl-tRNA synthetases (KRS) attach lysine to the cognate tRNA in a two-step mechanism
physiological function
enzyme lysyl-transfer RNA synthetase is a bifunctional aminoacyl-transfer RNA synthetase catalyzing transfer RNA aminoacylation in both, cytoplasm and mitochondria
physiological function
essential role of enzyme Krs in virulence and dimorphic transition. Krs plays an important role in sustaining conidial viability, thermotolerance, and UV-B resistance crucial for the biological control potential of Beauveria bassiana. Vital role of cytosolic Krs in some cellular processes linked to the biological control potential of Beauveria bassiana against insect pests, mechanism, overview. Linkage of Krs with the developmental pathway of Beauveria bassiana
physiological function
Essentiality of lysyl and cysteinyl-tRNA synthetases of Mycobacterium smegmatis
physiological function
-
four B cell epitopes of myelin A1 and Mycobacterium leprae proteins, 50S ribosomal L2 and lysyl tRNA synthetase are cross-reactive. Further, Mycobacterium leprae sonicated antigen hyperimmunization is responsible for induction of autoantibody response in mice. Role of molecular mimicry in nerve damage in leprosy
physiological function
in addition to its translational function when associated to the a multi-aminoacyl-tRNA synthetase complex (MSC), LysRS is also recruited in nontranslational roles after dissociation from the MSC. The balance between its MSC-associated and MSC-dissociated states is essential to regulate the functions of LysRS in cellular homeostasis
physiological function
in yeast, the import of tRNALys with CUU anticodon (tRK1) relies on a complex mechanism where interaction with enolase 2 (Eno2p) dictates a deep conformational change of the tRNA. This event is believed to mask the tRNA from the cytosolic translational machinery to redirect it towards the mitochondria. Once near the mitochondrial outer membrane, the precursor of the mitochondrial lysyl-tRNA synthetase (preMsk1p) takes over enolase to carry the tRNA within the mitochondrial matrix, where it is supposed to participate in translation following correct refolding. Mechanism of mitochondrial import of the yeast lysine isoacceptor tRNA with a CUU anticodon (tRK1). tRK1 in the canonical Lform undertakes refolding (Fform) through interaction mainly with enolase 2 (Eno2p), overview. While about 95% of the tRK1 cellular pool is used in cytosolic translation, this complex shuttles the remaining about 5% to the mitochondrial surface, where it interacts with preMsk1p, which proceeds to import properly. The mitochondrial targeting sequence (MTS) is displayed as an additional appendage bound to the N-terminal end of the protein representation
physiological function
KRS at the plasma membrane is important for cancer metastasis, canonical roles of cytosolic KRS in protein translation. KRS and its downstream effectors promote the metastatic migration. Complex formation among KRS, p67LR, and integrins alpha6 and beta1 upon cell adhesion, KRS/p67LR/integrin alpha6beta1 linkage correlates for ERK1/2 activation, KRS-dependent ERK1/2 activation. KRS has prometastatic roles at the invasive margins of KRS-/+ mouse breast tumor and human colon tumor tissues
physiological function
lysyl-tRNA synthetase (KRS) is a multi-functional enzyme, which, in addition to its primary function of aminoacylation of lysine onto the cognate tRNA, has various noncanonical functions. Enzyme KRS interacts with the laminin receptor (LR/RPSA) and enhances laminin-induced cell migration in cancer metastasis. The anticodon-binding domain of KRS binds directly to the C-terminal region of 37 kDa laminin receptor precursor 37LRP, and inhibitors BC-K-01 and BC-K-YH16899 interfere with KRS37LRP binding. In addition, the anticodon-binding domain of KRS binds to laminin. Furthermore, KRS is a major source of diadenosine tetraphosphate (Ap4A) in immunologically activated mast cells, and via translocation into the nucleus, KRS controls the expression of microphthalmia-associated transcription factor (MITF)-inducible genes in allergic responses
physiological function
lysyl-tRNA synthetase (KRS) is an aminoacyl-tRNA synthetase (ARS) that is essential for protein synthesis during ligation of specific amino acids to their cognate tRNAs
physiological function
-
Shiga toxins (Stxs) produced by Shiga toxin-producing Escherichia coli (STEC) strains are major virulence factors that cause fatal systemic complications, such as hemolytic uremic syndrome and disruption of the central nervous system. Enzymatically active Stxs trigger the dissociation of lysyl-tRNA synthetase (KRS) from the multi-aminoacyl-tRNA synthetase complex (MSC) in human macrophage-like differentiated THP-1 cells and its subsequent secretion. The secreted KRS acts to increase the production of proinflammatory cytokines and chemokines. Thus, KRS may be one of the key factors that mediate transduction of inflammatory signals in the STEC-infected host
physiological function
-
activity of most class II aminoacyl-tRNA synthetases absolutely requires the presence of added cognate amino acids
-
physiological function
-
the T box element controlling lysK, encoding LysRS1, expression in strain 14579 is functional, but unusually responds to depletion of charged tRNALys and tRNAAsn, making LysRS1 expression responsive to a wider range of nutritional stresses, transcriptional regulation, overview
-
physiological function
-
canonical LysRS and CysRS are essential for growth of Mycobacterium smegmatis
-
physiological function
-
Essentiality of lysyl and cysteinyl-tRNA synthetases of Mycobacterium smegmatis
-
physiological function
-
aminoacyl-tRNA synthetases provide the first step in protein synthesis quality control by discriminating cognate from noncognate amino acid and tRNA substrates. While substrate specificity is enhanced in many instances by cis- and transediting pathways, it has been revealed that in organisms such as Streptococcus pneumoniae some aminoacyl tRNA synthetases display significant tRNA mischarging activity. Pneumococcal LysRS misaminoacylates tRNALys with Ala and to a lesser extent Thr and Ser, with mischarging efficiency modulated by the presence of an unusual U4:G69 wobble pair in the acceptor stems of both pneumococcal tRNALys isoacceptors. Addition of the trans-editing factor MurM, which also functions in peptidoglycan synthesis, reduces Ala-tRNALys production by LysRS, providing evidence for cross talk between the protein synthesis and cell wall biogenesis pathways. Mischarging of tRNALys by AlaRS is also observed, and this provides additional potential MurM substrates. Adaptive misaminoacylation may contribute significantly to the viability of this pathogen during amino acid starvation. In the absence of efficient pre- and/or posttransfer editing mechanisms, the distorted region in the acceptor stem of tRNALys is able to reduce the overall mischarging capacity of pneumococcal LysRS, with an accompanying loss in cognate charging
-
physiological function
-
essential role of enzyme Krs in virulence and dimorphic transition. Krs plays an important role in sustaining conidial viability, thermotolerance, and UV-B resistance crucial for the biological control potential of Beauveria bassiana. Vital role of cytosolic Krs in some cellular processes linked to the biological control potential of Beauveria bassiana against insect pests, mechanism, overview. Linkage of Krs with the developmental pathway of Beauveria bassiana
-
physiological function
-
in yeast, the import of tRNALys with CUU anticodon (tRK1) relies on a complex mechanism where interaction with enolase 2 (Eno2p) dictates a deep conformational change of the tRNA. This event is believed to mask the tRNA from the cytosolic translational machinery to redirect it towards the mitochondria. Once near the mitochondrial outer membrane, the precursor of the mitochondrial lysyl-tRNA synthetase (preMsk1p) takes over enolase to carry the tRNA within the mitochondrial matrix, where it is supposed to participate in translation following correct refolding. Mechanism of mitochondrial import of the yeast lysine isoacceptor tRNA with a CUU anticodon (tRK1). tRK1 in the canonical Lform undertakes refolding (Fform) through interaction mainly with enolase 2 (Eno2p), overview. While about 95% of the tRK1 cellular pool is used in cytosolic translation, this complex shuttles the remaining about 5% to the mitochondrial surface, where it interacts with preMsk1p, which proceeds to import properly. The mitochondrial targeting sequence (MTS) is displayed as an additional appendage bound to the N-terminal end of the protein representation
-
additional information
-
human lysyl-tRNA synthetase is bound to the multi-tRNA synthetase complex, mediated by the p38 scaffold protein, the complex maintains and regulates the aminoacylation and nuclear functions of LysRS. p38 mobilizes LysRS for redirection to the nucleus to interact with the microphthalmia associated transcription factor. Each of the N-terminal 48 residues of p38 binds one LysRS dimer and, in so doing, brings two copies of the LysRS dimer into the multi-tRNA synthetase complex. Structural organization of the LysRS-p38 complex, overview
additional information
-
recombinant KARS protein is unable to influence the binding of recombinant CRT to the cell surface. Moreover, recombinant KARS protein is unable to stimulate macrophages in vitro
additional information
human cytoplasmic lysyl-tRNA synthetase (LysRS) is associated within a multi-aminoacyl-tRNA synthetase complex (MSC). Within this complex, the p38 component is the scaffold protein that binds the catalytic domain of LysRS via its N-terminal region, LysRS-p38 interaction analysis, Lys356 and His364 of LysRS interact with the peptide from Pro8 to Arg26 in native p38, overview
additional information
-
human cytoplasmic lysyl-tRNA synthetase (LysRS) is associated within a multi-aminoacyl-tRNA synthetase complex (MSC). Within this complex, the p38 component is the scaffold protein that binds the catalytic domain of LysRS via its N-terminal region, LysRS-p38 interaction analysis, Lys356 and His364 of LysRS interact with the peptide from Pro8 to Arg26 in native p38, overview
additional information
-
KRS is normally located in the cytosol as a component of the multi-tRNA synthetase complex (MSC) that consists of nine different ARSs and three auxiliary factors named AIMP1, 2 and 3
additional information
LysU is 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
additional information
-
LysU is 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
additional information
noncanonical roles of membranous lysyl-tRNA synthetase in transducing cell-substrate signaling for invasive dissemination of colon cancer spheroids in 3D collagen I gels
additional information
-
similarity between the predicted B cell epitopes of 20 kDa microtubule-stabilizing protein of Bos taurus, MBP (MBP98-104), and 50S ribosomal protein L2 or lysyl-tRNA synthetase of Mycobacterium leprae. Two B cell epitopes of MBP98-104 with 50S ribosomal protein L2226-237 and MBP127-131 and MBP55-60 with 50S ribosomal protein L2 of Mycobacterium leprae41-46 are mimicking epitopes. While, 2 B cell epitopes of MBP85-98 with lysyl tRNA synthetase388-401 and MBP99-104 with lysyl tRNA synthetase472-477 are mimicking with each other
additional information
the enzyme is organized in a multi-synthetase complex (MSC)
additional information
-
the enzyme is organized in a multi-synthetase complex (MSC)
additional information
the residues involved in lysine activation are highly conserved and the active site closes around the lysyl-adenylate. A small helix bundle may contribute to tRNA binding through interaction with the tRNA hinge, modeling, overview
additional information
-
the residues involved in lysine activation are highly conserved and the active site closes around the lysyl-adenylate. A small helix bundle may contribute to tRNA binding through interaction with the tRNA hinge, modeling, overview
additional information
transcriptional profiling of key genes required for asexual development
additional information
-
transcriptional profiling of key genes required for asexual development
additional information
-
transcriptional profiling of key genes required for asexual development
-
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A233S
-
the mutant recognizes L-lysine better than wild type and shows higher catalytic efficiency
A233S/G469A
-
inactive, the mutation decreases stable L-lysyl-adenylate formation
G469A
-
very low activity, the mutation decreases stable L-lysyl-adenylate formation
E43I
-
significant decrease of catalytic activity compared to the wild type enzyme
E43Q
-
significant decrease of catalytic activity compared to the wild type enzyme
G29A
-
significant decrease of catalytic activity compared to the wild type enzyme
H242A
-
significant decrease of catalytic activity compared to the wild type enzyme
H242L
-
shows almost no change in the catalytic activity compared to the wild type enzyme
H242W
-
significant decrease of catalytic activity compared to the wild type enzyme
T31G
-
significant decrease of catalytic activity compared to the wild type enzyme
T31S
-
shows almost no change in the catalytic activity compared to the wild type enzyme
W220A
-
significant decrease of catalytic activity compared to the wild type enzyme
W220L
-
significant decrease of catalytic activity compared to the wild type enzyme
W220Y
-
significant decrease of catalytic activity compared to the wild type enzyme
Y269F
-
6fold drop in the catalytic efficiency compared to the wild type enzyme
Y269S
-
significant decrease of catalytic activity compared to the wild type enzyme
E240D
-
1.2fold increase in Km-value for Lys, 21fold decrease in turnover number for Lys, Km-value for ATP is nearly identical to wild-type value, 24fold decrease in turnover number for ATP
E240Q
-
1.4fold increase in Km-value for Lys, 207fold decrease in turnover number for Lys, 1.2fold increase in Km-value for ATP, 261fold decrease in turnover number for ATP
E246D
-
the mutant shows more than 50% loss in catalytic efficiency compared to the wild type enzyme
E246R
-
the mutant shows more than 50% loss in catalytic efficiency compared to the wild type enzyme
E264A
-
the mutant shows more than 90% loss in catalytic efficiency compared to the wild type enzyme
E264K
-
the mutant catalyses the production of glycerol-3-phosphate, powered by ATP turnover to ADP but shows little formation of diadenosine tri- and tetraphosphates under normal conditions (additional Zn2+/L-lysine/Mg2+)
E264N
-
the mutant catalyses the production of glycerol-3-phosphate, powered by ATP turnover to ADP but shows little formation of diadenosine tri- and tetraphosphates under normal conditions (additional Zn2+/L-lysine/Mg2+)
E264Q
-
the mutant catalyses the production of glycerol-3-phosphate, powered by ATP turnover to ADP but shows little formation of diadenosine tri- and tetraphosphates under normal conditions (additional Zn2+/L-lysine/Mg2+)
E273A
-
the mutant shows more than 90% loss in catalytic efficiency compared to the wild type enzyme
E278D
-
98fold increase in Km-value for Lys, 11fold decrease in turnover number for Lys, 1.3fold increase in Km-value for ATP, 63fold decrease in turnover number for ATP
E278Q
-
1.9fold decrease in Km-value for Lys, 120fold decrease in turnover number for Lys, 1.5fold decrease in Km-value for ATP, 200fold decrease in turnover number for ATP
E414A
-
the mutant shows more than 90% loss in catalytic efficiency compared to the wild type enzyme
E421A
-
the mutant shows more than 50% loss in catalytic efficiency compared to the wild type enzyme
E428D
-
8.5fold increase in Km-value for Lys, 1.8fold decrease in turnover number for Lys, 1.7fold increase in Km-value for ATP, 3.4fold decrease in turnover number for ATP
E428Q
-
2fold decrease in Km-value for Lys, 9fold decrease in turnover number for Lys, 1.5fold decrease in Km-value for ATP, 200fold decrease in turnover number for ATP
F261A
-
the mutant shows more than 50% loss in catalytic efficiency compared to the wild type enzyme
F274A
-
the mutant shows more than 90% loss in catalytic efficiency compared to the wild type enzyme
F426H
-
78fold increase in Km-value for Lys, 1.3fold decrease in turnover number for Lys, 1.6fold increase in Km-value for ATP, 5fold decrease in turnover number for ATP
F426W
-
6.2fold increase in Km-value for Lys, 3fold decrease in turnover number for Lys, 9.2fold increase in Km-value for ATP, 1.4fold decrease in turnover number for ATP
G216A
-
75fold increase in Km-value for Lys, 1.9fold increase in turnover number for Lys, 16fold increase in Km-value for ATP, 4.25fold decrease in turnover number for ATP
G265A
-
the mutant shows more than 90% loss in catalytic efficiency compared to the wild type enzyme
H270A
-
the mutant catalyses the production of glycerol-3-phosphate, powered by ATP turnover to ADP but shows little formation of diadenosine tri- and tetraphosphates under normal conditions (additional Zn2+/L-lysine/Mg2+)
I266A
-
the mutant shows more than 50% loss in catalytic efficiency compared to the wild type enzyme
N424D
-
2fold increase in Km-value for Lys, 1.1fold decrease in turnover number for Lys, 1.8fold increase in Km-value for ATP, 3.4fold decrease in turnover number for ATP
N424Q
-
20fold increase in Km-value for Lys, 2.8fold decrease in turnover number for Lys, 69fold increase in Km-value for ATP, 1.5fold decrease in turnover number for ATP
P272A
-
the mutant shows more than 90% loss in catalytic efficiency compared to the wild type enzyme
R480A
-
the mutant shows more than 50% loss in catalytic efficiency compared to the wild type enzyme
S267A
-
the mutant shows more than 50% loss in catalytic efficiency compared to the wild type enzyme
Y280F
-
9.2fold increase in Km-value for Lys, 58fold decrease in turnover number for Lys, 5.2fold increase in Km-value for ATP, 20fold decrease in turnover number for ATP
Y280S
-
44fold increase in Km-value for Lys, 1.1fold decrease in turnover number for Lys, 3.9fold increase in Km-value for ATP, 9.7fold decrease in turnover number for ATP
CAT W314F
mutant of the truncated C-terminal catalytic domain CAT
CAT W332F
mutant of the truncated C-terminal catalytic domain CAT
GsLysRS W314F
mutant of Geobacillus stearothermophilus lysyl-tRNA synthetase
GsLysRS W332F
mutant of Geobacillus stearothermophilus lysyl-tRNA synthetase
truncated N-terminal tRNA anticodon-binding domain
TAB
W314F
-
site-directed mutagenesis, activity is similar to the wild-type enzyme
W314f/W332F
-
site-directed mutagenesis, slightly reduced activity
W332F
-
site-directed mutagenesis, activity is slightly reduced, but the binding of L-lysine is altered, increased Km for L-lysine
Y271F
-
site-directed mutagenesis, highly increased Km for L-lysine in the ATP-diphosphate exchange reaction
DELTA1-65
-
mutant enzyme binds poorly to tRNALys, but does not increase tRNALys packaging into HIV-1 viruses
DELTA452-597
-
mutant enzyme binds to but does not aminoacylate tRNALys, still facilitates an increase in tRNALys packaging into virions
DELTAS70-T584
truncation at S70-T584 and full length LysRS (M1-V597) expressed, purified, and attempted for crystallization
E525K
naturally occuring mutation within a highly conserved region of the catalytic domain, the mutation is involved in neurological disorders in infants
F244A
-
the mutant shows 90% aminoacylation activity compared to the wild type enzyme
F244A/I245A
-
the mutant shows 90% aminoacylation activity compared to the wild type enzyme
hKRSDELTA1-24
deletion mutation. Construct shows significant stimulation of lysylation by EF1alpha and binding to EF1alpha
hKRSDELTA24-42
deletion mutation. Construct shows significant stimulation of lysylation by EF1alpha and binding to EF1alpha
hKRSDELTA60
removal of the amino-terminal extension
I245A
-
the mutant shows wild type aminoacylation activity
I246D
-
the mutant shows 60% aminoacylation activity compared to the wild type enzyme
I246D/R247A
-
the mutant shows 20% aminoacylation activity compared to the wild type enzyme
I250D
-
the mutant shows 40% aminoacylation activity compared to the wild type enzyme
I250D/I251D
-
the mutant shows 20% aminoacylation activity compared to the wild type enzyme
I251D
-
the mutant shows 40% aminoacylation activity compared to the wild type enzyme
I254D
-
the mutant shows 40% aminoacylation activity compared to the wild type enzyme
I254D/R255A
-
the mutant shows 30% aminoacylation activity compared to the wild type enzyme
K249A
-
the mutant shows 90% aminoacylation activity compared to the wild type enzyme
R247A
-
the mutant shows 30% aminoacylation activity compared to the wild type enzyme
R255A
-
the mutant shows 40% aminoacylation activity compared to the wild type enzyme
R438W
naturally occuring mutation within a highly conserved region of the catalytic domain, the mutation is involved in neurological disorders in infants
S248D
-
the mutant shows wild type aminoacylation activity
S248D/K249A
-
the mutant shows wild type aminoacylation activity
S270D
-
the mutant shows 800fold enhanced catalytic activity compared to the wild type enzyme, with enhanced diadenosine tetraphosphate synthetic activity, enhanced ATP hydrolysis and lost aminoacylation activity for tRNALys
Y491E
-
exhibits significant improvement compared to the wild type in aminoacylation of a tRNALysUUG
additional information
the krs gene is deleted from the wild-type strain by homogeneous recombination of its 5' and 3' coding/flanking fragments (w1500 bp each) separated by bar marker and rescued in DELTAkrs by ectopic integration of a cassette comprising its full-length coding sequence with flank regions and sur marker
additional information
-
the krs gene is deleted from the wild-type strain by homogeneous recombination of its 5' and 3' coding/flanking fragments (w1500 bp each) separated by bar marker and rescued in DELTAkrs by ectopic integration of a cassette comprising its full-length coding sequence with flank regions and sur marker
additional information
-
the krs gene is deleted from the wild-type strain by homogeneous recombination of its 5' and 3' coding/flanking fragments (w1500 bp each) separated by bar marker and rescued in DELTAkrs by ectopic integration of a cassette comprising its full-length coding sequence with flank regions and sur marker
-
additional information
-
in vitro construction of the LysRS-p38 complex, overview
additional information
incorporation of the non-natural, photo-cross-linkable amino acid p-benzoyl-L-phenylalanine (Bpa) at 27 discrete positions within the catalytic domain of LysRS. Among the 27 distinct LysRS mutants, only those with Bpa inserted in place of Lys356 or His364 are cross-linked with p38, the scaffold protein of the -aminoacyl-tRNA synthetase complex (MSC)
additional information
-
incorporation of the non-natural, photo-cross-linkable amino acid p-benzoyl-L-phenylalanine (Bpa) at 27 discrete positions within the catalytic domain of LysRS. Among the 27 distinct LysRS mutants, only those with Bpa inserted in place of Lys356 or His364 are cross-linked with p38, the scaffold protein of the -aminoacyl-tRNA synthetase complex (MSC)
additional information
generation of conditional expression strains, conditional expression plasmids are electroporated into Mycobacterium smegmatis strain mc2155, analysis of inducer dependency of conditional expression strains, overview
additional information
generation of conditional expression strains, conditional expression plasmids are electroporated into Mycobacterium smegmatis strain mc2155, analysis of inducer dependency of conditional expression strains, overview
additional information
-
generation of conditional expression strains, conditional expression plasmids are electroporated into Mycobacterium smegmatis strain mc2155, analysis of inducer dependency of conditional expression strains, overview
additional information
generation of conditional expression strains, conditional expression plasmids are electroporated intoMycobacterium smegmatis strain mc2155, analysis of inducer dependency of conditional expression strains, overview
additional information
generation of conditional expression strains, conditional expression plasmids are electroporated intoMycobacterium smegmatis strain mc2155, analysis of inducer dependency of conditional expression strains, overview
additional information
-
generation of conditional expression strains, conditional expression plasmids are electroporated intoMycobacterium smegmatis strain mc2155, analysis of inducer dependency of conditional expression strains, overview
additional information
-
generation of conditional expression strains, conditional expression plasmids are electroporated intoMycobacterium smegmatis strain mc2155, analysis of inducer dependency of conditional expression strains, overview
-
additional information
-
generation of conditional expression strains, conditional expression plasmids are electroporated into Mycobacterium smegmatis strain mc2155, analysis of inducer dependency of conditional expression strains, overview
-
additional information
introduction of a Watson-Crick base pair (G69A) into each pneumococcal tRNALys isoacceptor results in an approximately 3fold increase in lysylation activity by LysRS compared to wild-type tRNAs. The overall mischarging profile of pneumococcal LysRS remains the same with both the wild-type and the G69A tRNALys transcripts, but the yield of Ala-tRNALys produced is increased by approximately 2fold for the TTT G69A transcript and 3fold for the CTT G69A transcript in comparison to the equivalent wild-type species
additional information
-
introduction of a Watson-Crick base pair (G69A) into each pneumococcal tRNALys isoacceptor results in an approximately 3fold increase in lysylation activity by LysRS compared to wild-type tRNAs. The overall mischarging profile of pneumococcal LysRS remains the same with both the wild-type and the G69A tRNALys transcripts, but the yield of Ala-tRNALys produced is increased by approximately 2fold for the TTT G69A transcript and 3fold for the CTT G69A transcript in comparison to the equivalent wild-type species
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