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Information on EC 6.1.1.6 - lysine-tRNA ligase
for references in articles please use BRENDA:EC6.1.1.6
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EC Tree 6 Ligases
6.1 Forming carbon-oxygen bonds
6.1.1 Ligases forming aminoacyl-tRNA and related compounds
6.1.1.6 lysine-tRNA ligase
The enzyme appears in viruses and cellular organisms
- 6.1.1.6
- synthetases
- aminoacylation
- lysylation
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anticodon
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aarss
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isoacceptors
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diadenosine
- aspartyl-trna
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gagpol
- tetraphosphate
- trnalys3
- prors
- valrs
- leurs
- arginyl-trna
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isoleucyl-trna
- glnrs
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atp-ppi
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anticodon-binding
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prolyl-trna
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multi-trna
- asprs
- diagnostics
- pharmacology
- medicine
- drug development
- synthesis
showSynonyms
lysyl-trna synthetase, lysrs, lysrs1, lysrs2, lysyl trna synthetase, mitochondrial lysyl-trna synthetase, cytoplasmic lysyl-trna synthetase, class i lysrs, premsk1p, pfkrs, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ap4A synthase
BBA_03037
class I lysyl-tRNA synthetase
class II lysyl-tRNA synthetase
FOSTERSO_4045
KARS
KRS
KRS-1
L-Lysine-transfer RNA ligase
lysine aminoacyl-tRNA synthetase
Lysine translase
Lysine--tRNA ligase
Lysine-tRNA synthetase
LysRS
LysRS1
LysRS2
lysS
LysU
LysX
lysyl tRNA synthetase
Lysyl-transfer ribonucleate synthetase
Lysyl-transfer RNA synthetase
Lysyl-tRNA synthetase
lysylphosphatidylglycerol biosynthesis bifunctional protein
UniProt
mitochondrial lysyl-tRNA synthetase
Msk1p
MSMEG_3796
MSMEG_6094
MXAN_4731
preMsk1p
Synthetase, lysyl-transfer ribonucleate
additional information
L-Lysine-transfer RNA ligase
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Lysine translase
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Lysine--tRNA ligase
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Lysine-tRNA synthetase
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LysRS
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LysRS
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Lysyl-transfer ribonucleate synthetase
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Lysyl-transfer RNA synthetase
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Lysyl-tRNA synthetase
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Lysyl-tRNA synthetase
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Lysyl-tRNA synthetase
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Lysyl-tRNA synthetase
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Lysyl-tRNA synthetase
interacts with EF1alpha, aspartyl-tRNA synthetase (EC 6.1.1.12) and p38 in vitro
Synthetase, lysyl-transfer ribonucleate
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additional information
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lysyl-tRNA synthetase is unique within the aminoacyl-tRNA synthetase family in that both class I LysRS1 and class II LysRS2 enzymes exist
additional information
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lysyl-tRNA synthetase is unique within the aminoacyl-tRNA synthetase family in that both class I LysRS1 and class II LysRS2 enzymes exist
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additional information
enzyme has structural similarity to glutamyl-tRNA synthetase, EC 6.1.1.17, from other organisms, e.g. Thermus thermophilus
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys
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ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys
sequential ordered mechanism
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ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys
sequential ordered mechanism
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ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys
active site structure
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ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys
active site structure
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ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys
two-step reaction mechanism
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ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys
active site structure and substrate binding
ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys
bases N73, U35 and U36 play an important role in tRNA substrate recognition
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ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys
mechanism of tRNALys and L-lysine binding
ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys
Trp314 is involved in binding of L-lysine, binding renders the non-polar microenvironment of the residue more polar
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ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys
two-step binding mechanism
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ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys
residue Glu411 plays a key role in the arrangement of diphosphate for the nucleophilic attack
ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys
sequential ordered mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Aminoacylation
esterification
Aminoacylation
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esterification
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