6.1.1.6: lysine-tRNA ligase

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

Reaction

Synonyms

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

ECTree

     6 Ligases

         6.1 Forming carbon-oxygen bonds

             6.1.1 Ligases forming aminoacyl-tRNA and related compounds

                6.1.1.6 lysine-tRNA ligase

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10	Activating Compound
51219	AA Sequence
7	Application
1	CAS Registry Number
47	Cloned(Commentary)
56	Cofactor
13	Crystallization (Commentary)
181	Disease/ Diagnostics
6	Expression
58	General Information
1	General Stability
9	IC50 Value
64	Inhibitors
3	kcat/KM [mM/s]
44	Ki Value [mM]
138	KM Value [mM]
53	Localization
27	Metals/Ions
38	Molecular Weight [Da]
64	Natural Substrates/ Products (Substrates)
728	Organism
4	Pathway
173	PDB ID
15	pH Optimum
1	pH Range
1	pH Stability
2	pI Value
9	Posttranslational Modification
99	Protein Variants
46	Purification (Commentary)
13	Reaction
46	Reaction Type
170	Reference
52	Source Tissue
15	Specific Activity [micromol/min/mg]
4	Storage Stability
251	Substrates and Products (Substrate)
32	Subunits
474	Synonyms
1	Systematic Name
17	Temperature Optimum [°C]
2	Temperature Range [°C]
6	Temperature Stability [°C]
130	Turnover Number [1/s]

Crystallization

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Crystallization on EC 6.1.1.6 - lysine-tRNA ligase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

purified enzyme free or in complex with ATP, Lys-AMP, or AMPPNP, hanging drop vapor diffusion method, mixing of 0.001 ml of protein solution with 0.001 ml of reservoir solution, the latter contains: for the free enzyme KRS 100 mM HEPES pH 7.5, 10% PEG 6000, and 5% 2-methyl-2,4-pentanediol, for the KRS-Lys-AMP crystals 50 mM HEPES, pH 8.0, 50 mM NaCl, 1 mM spermine, and 8% PEG 4000, for the KRS-ATP crystals 50 mM HEPES pH 8.0, 50 mM NaCl, 7.5% PEG 4000,and 1.2 mM spermine, and for the KRS-AMPPNP crystals 50 mM HEPES pH 8.0, 50 mM NaCl, 7.5% PEG 4000, and 1.2 mM spermine, 3 days, 20°C, X-ray diffraction structure determination and analysis at 2.80-3.05 A resolution, molecular replacement using HsKRS structure, PDB ID 3BJU, as the search model, modeling

Entamoeba histolytica

C4M7X2

744902

determined to 2.8 A resolution with lysine bound to the active site

Escherichia coli

-

482

unliganded enzyme and in complex with L-lysine, vapor diffusion hanging drop method, protein solution: 20 mg/ml protein, 20 mM Tris-HCl, pH 8.0, 10 mM 2-mercaptoethanol, 10 mM MgCl2, plus equal volume of reservoir solution: 0.1 M HEPES, pH 7.5, 46-50% saturated ammonium sulfate solution, 2-4% polyethylene glycol 400, 15-20% glycerol, 4-18°C, X-ray difraction structure determination at 2.7 A resolution, and analysis

Escherichia coli

P0A8N3

649930

-

Geobacillus stearothermophilus

-

91

crystal structures of two complexes of LysRS with the adenylate of L-lysine hydroxamate and with 5'-O-[N-(L-Lysyl)sulphamoyl] adenosine. The comparisons of the two structures and the SerRS structure reveals the specific side-chain shift of Glu411 of LysRS in the complex with the adenylate of L-lysine hydroxamate. Glu411 plays a key role in the arrangement of diphosphate for the nucleophilic attack

Geobacillus stearothermophilus

Q9RHV9

704351

(alpha2)2 LysRS tetramer

Homo sapiens

-

716788

in complex with p38/AIMP2

Homo sapiens

-

728305

micrositting drop-vapor diffusion method, both DELTAS70-T584 and full length LysRS

Homo sapiens

Q15046

694885

hanging drop vapor diffusion method, using 0.1 M Bis-Tris pH 6.5, 2% (v/v) tascimate pH 6.0, 20% (w/v) PEG 3350

Plasmodium falciparum

Q8IDJ8

726591

purified enzyme PfKRS in complex with lysine and cladosporin, hanging drop vapour diffusion method, mixing of 0.001 ml of highly pure enzyme in 50 mM Tris-HCl, pH 8.0, 200 mM NaCl, 10 mM 2-mercaptoethanol, 0.5 mM cladosporin, and 2 mM L-lysine, with 0.001 ml of crstallization solution containing 0.1 M Bis-Tris, pH 6.5, 2% v/v Tascimate, pH 6.0, 20% w/v PEG 3350, 20°C, 10 days, X-ray diffraction structure determination and analysis at 2.7 A resolution, molecular homology modeling using the human enzyme structure as template

Plasmodium falciparum

Q8IDJ8

745656

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

Pyrococcus horikoshii

O57963

653323

-

Saccharomyces cerevisiae

-

487

crystal structure of lysyl-tRNA synthetase complexed with Escherichia coli tRNALys

Thermus thermophilus

-

481