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Information on EC 6.1.1.6 - lysine-tRNA ligase and Organism(s) Pyrococcus horikoshii and UniProt Accession O57963

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Pyrococcus horikoshii
UNIPROT: O57963 not found.
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The taxonomic range for the selected organisms is: Pyrococcus horikoshii
The enzyme appears in selected viruses and cellular organisms
Synonyms
lysyl-trna synthetase, lysrs, lysrs1, lysrs2, lysyl trna synthetase, mitochondrial lysyl-trna synthetase, cytoplasmic lysyl-trna synthetase, class i lysrs, premsk1p, pfkrs, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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Lysyl-transfer ribonucleate synthetase
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Lysyl-transfer RNA synthetase
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Lysyl-tRNA synthetase
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Synthetase, lysyl-transfer ribonucleate
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class I lysyl-tRNA synthetase
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L-Lysine-transfer RNA ligase
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-
-
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Lysine translase
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-
-
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Lysine--tRNA ligase
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-
-
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Lysine-tRNA synthetase
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-
-
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LysRS
Lysyl-transfer ribonucleate synthetase
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-
-
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Lysyl-transfer RNA synthetase
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-
-
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Lysyl-tRNA synthetase
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-
-
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Synthetase, lysyl-transfer ribonucleate
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-
-
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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
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys
show the reaction diagram
mechanism of tRNALys and L-lysine binding
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
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-
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Aminoacylation
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-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
L-lysine:tRNALys ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9031-26-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
show the reaction diagram
-
-
?
ATP + L-lysine + tRNALysCUU
AMP + L-lysyl-tRNALysCUU + diphosphate
show the reaction diagram
-
-
-
-
?
ATP + L-lysine + tRNALysGUU
AMP + L-lysyl-tRNALysGUU + diphosphate
show the reaction diagram
-
-
-
-
?
ATP + L-lysine + tRNALysUCU
AMP + L-lysyl-tRNALysUCU + diphosphate
show the reaction diagram
-
-
-
-
?
ATP + L-lysine + tRNALysUGU
AMP + L-lysyl-tRNALysUGU + diphosphate
show the reaction diagram
-
-
-
-
?
ATP + L-lysine + tRNALysUUC
AMP + L-lysyl-tRNALysUUC + diphosphate
show the reaction diagram
-
-
-
-
?
ATP + L-lysine + tRNALysUUG
AMP + L-lysyl-tRNALysUUG + diphosphate
show the reaction diagram
-
-
-
-
?
ATP + L-lysine + tRNALysUUU
AMP + L-lysyl-tRNALysUUU + diphosphate
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-lysine + tRNALys
AMP + L-lysyl-tRNALys + diphosphate
show the reaction diagram
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.4
tRNALysCUU
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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
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1.5
tRNALysGUU
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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
-
0.87
tRNALysUUU
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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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.062
tRNALysCUU
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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
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0.043
tRNALysGUU
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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
-
0.44
tRNALysUUU
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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
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
class I enzyme, i.e. LysRS-I
Uniprot
Manually annotated by BRENDA team
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme alone or in complex with L-lysine, 0.001 ml of protein solution 5 mg/ml, with or without 10 mM L-lysine, with an equal volume of reservoir solution: 120 mM HEPES, pH 7.5, 2.4 M ammonium sulfate, 2.4% v/v PEG 400, 20°C, X-ray diffraction structure determination at 2.6 A for the enzyme crystals and at 2.9 A for the complex crystals, structure analysis
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y491E
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exhibits significant improvement compared to the wild type in aminoacylation of a tRNALysUUG
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
MonoQ 5/5 column chromatography and Superose 12 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3+ RPC) cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Terada, T.; Nureki, O.; Ishitani, R.; Ambrogelly, A.; Ibba, M.; Soll, D.; Yokoyama, S.
Functional convergence of two lysyl-tRNA synthetases with unrelated topologies
Nat. Struct. Biol.
9
257-262
2002
Pyrococcus horikoshii (O57963), Pyrococcus horikoshii
Manually annotated by BRENDA team
Levengood, J.D.; Roy, H.; Ishitani, R.; Soell, D.; Nureki, O.; Ibba, M.
Anticodon recognition and discrimination by the alpha-helix cage domain of class I lysyl-tRNA synthetase
Biochemistry
46
11033-11038
2007
Pyrococcus horikoshii
Manually annotated by BRENDA team
Wang, S.; Prtorius-Ibba, M.; Ataide, S.; Roy, H.; Ibba, M.
Discrimination of cognate and noncognate substrates at the active site of class I lysyl-tRNA synthetase
Biochemistry
45
3646-3652
2006
Pyrococcus horikoshii
Manually annotated by BRENDA team