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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Results	in table
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]

Subunits

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Subunits on EC 6.1.1.6 - lysine-tRNA ligase

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SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

?

2 entries

dimer

14 entries

heterotetramer

Homo sapiens

Q15046

it is not understood, how the two dimeric proteins combine to make a presumptive alpha2beta2 heterotetramer

694885

homodimer

4 entries

homotetramer

Homo sapiens

Q15046

alpha2:alpha2 tetramer. This tetramer is probably functional for aminoacylation, because docking of tRNA molecules to the tetrameric LysRS seems not to cause steric clash

694885

monomer

2 entries

tetramer

Homo sapiens

-

structure of the LysRS tetramer in solution, overview

716788

additional information

9 entries

?

Beauveria bassiana

J5K1T7

x * 66980, sequence calculation

745017

?

Beauveria bassiana ARSEF 2860

-

x * 66980, sequence calculation

-

dimer

Cricetinae

-

2 * 62000, N-terminally truncated recombinant enzyme, SDS-PAGE

652250

dimer

Escherichia coli

-

homodimer

482

dimer

Escherichia coli

-

1 * 72000 + 1 + 62000, SDS-PAGE

484

dimer

Escherichia coli

P0A8N3

2 * 58000, recombinant enzyme, crystal structure

649930

dimer

Escherichia coli B / ATCC 11303

-

1 * 72000 + 1 + 62000, SDS-PAGE

-

dimer

Geobacillus stearothermophilus

Q9RHV9

-

650620

dimer

Geobacillus stearothermophilus

-

2 * 58000, SDS-PAGE

91

dimer

Geobacillus stearothermophilus

-

2 * 57700, homodimer, SDS-PAGE, amino acid composition

479

dimer

Geobacillus stearothermophilus

-

2 * 57700, SDS-PAGE

651752

dimer

Geobacillus stearothermophilus

Q9RHV9

CAT mutants and wild-type CAT

691093

dimer

Geobacillus stearothermophilus NCA1503

-

2 * 57700, homodimer, SDS-PAGE, amino acid composition

-

dimer

Homo sapiens

Q15046

-

693146

dimer

Ovis aries

-

2 * 79000, SDS-PAGE

439

dimer

Rattus norvegicus

-

2 * 66000, SDS-PAGE

494

homodimer

Entamoeba histolytica

C4M7X2

the enzyme consists of a N-terminal anticodon-binding domain (residues 1-137), a catalytic domain (residues 150-554), a linker (residues 563-580) and the C-terminal EELP (residues 603-769). The asymmetric unit contains one EhKRS monomer, and the active dimer is formed with the symmetric monomer in the 2fold axis

744902

homodimer

Homo sapiens

-

-

674869

homodimer

Homo sapiens

Q15046

-

694885

homodimer

Plasmodium falciparum

Q8IDJ8

2 * 65000, SDS-PAGE

726591

monomer

Myxococcus xanthus

Q1D380

1 x 58000, about, recombinant His-tagged enzyme, sequence calculation, 1 * 60000, recombinant His-tagged enzyme, SDS-PAGE

744162

monomer

Myxococcus xanthus DK 1622

-

1 x 58000, about, recombinant His-tagged enzyme, sequence calculation, 1 * 60000, recombinant His-tagged enzyme, SDS-PAGE

-

additional information

Cricetinae

-

recombinant N-terminal extension is a monomer in solution with an elongated shape

652250

additional information

Homo sapiens

-

in the complex with p38, LysRs shows an alpha2beta1:beta1alpha2 organization, in which a dimeric p38 scaffold holds two LysRS alpha2 dimers in a parallel configuration, overview. The structure is designed to control both retention and mobilization of LysRS from the multi-tRNA synthetase complex

716788

additional information

Homo sapiens

Q15046

identification of protein interfaces within the multi-aminoacyl-tRNA synthetase complex including lysyl-tRNA synthetase and the scaffold protein p38, overview

744915

additional information

Homo sapiens

-

identification of protein interfaces within the multi-aminoacyl-tRNA synthetase complex including lysyl-tRNA synthetase and the scaffold protein p38, overview

744915

additional information

Homo sapiens

-

KRS is normally located in the cytosol as a component of the multitRNA synthetase complex (MSC) that consists of nine different ARSs and three auxiliary factors named AIMP1, 2 and 3. A homodimer of KRS is linked to the N-terminal peptide of AIMP2, and the MSC contains two units of the KRS homodimer-AIMP2 monomer complex. This suggests that KRS exists in the MSC as a tetramer that is present at a relatively higher stoichiometry, compared to other components that are bound to the MSC as monomers or dimers

744423

additional information

Homo sapiens

Q15046

structure analysis of the flexible N-terminal extension and anticodon-binding domain, NMR analysis, overview

744901

additional information

Homo sapiens

Q15046

the enzyme is organized in a multi-synthetase complex (MSC)

745950

additional information

Homo sapiens

-

the enzyme is organized in a multi-synthetase complex (MSC)

745950

additional information

Mus musculus

-

high molecular mass aminoacyl-tRNA synthetase complex with a coherent structure that can be visualized by electron microscopy

126