6.1.1.9: valine-tRNA ligase

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For detailed information about valine-tRNA ligase, go to the full flat file.

Reaction

Synonyms

G7a, glp-4, mitochondrial valyl tRNA synthetase, More, MTTV, Os03g0694900, OsValRS2, Synthetase, valyl-transfer ribonucleate, Val-tRNA synthetase, Valine transfer ribonucleate ligase, Valine translase, Valine--tRNA ligase, ValRS, ValRS1, ValRS2, valS, valyl aminoacyl tRNA synthetase, Valyl transfer ribonucleic acid synthetase, Valyl-transfer ribonucleate synthetase, Valyl-transfer RNA synthetase, Valyl-tRNA ligase, Valyl-tRNA synthetase, valyl-tRNAsynthetase, VARS, VARS-2, Vas1, Vas2, white panicle1

ECTree

     6 Ligases

         6.1 Forming carbon-oxygen bonds

             6.1.1 Ligases forming aminoacyl-tRNA and related compounds

                6.1.1.9 valine-tRNA ligase

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Results	in table
4	Activating Compound
58066	AA Sequence
1	Application
1	CAS Registry Number
15	Cloned(Commentary)
16	Cofactor
5	Crystallization (Commentary)
38	Disease/ Diagnostics
1	Expression
15	General Information
3	General Stability
16	Inhibitors
4	kcat/KM [mM/s]
5	Ki Value [mM]
72	KM Value [mM]
28	Localization
22	Metals/Ions
25	Molecular Weight [Da]
21	Natural Substrates/ Products (Substrates)
202	Organism
4	Pathway
9	PDB ID
13	pH Optimum
2	pH Range
29	Protein Variants
18	Purification (Commentary)
6	Reaction
18	Reaction Type
63	Reference
11	Source Tissue
12	Specific Activity [micromol/min/mg]
9	Storage Stability
99	Substrates and Products (Substrate)
23	Subunits
139	Synonyms
1	Systematic Name
9	Temperature Optimum [°C]
1	Temperature Range [°C]
5	Temperature Stability [°C]
30	Turnover Number [1/s]

Crystallization

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Crystallization on EC 6.1.1.9 - valine-tRNA ligase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

-

Escherichia coli

-

532

1.7 A resolution crystal structure of the ValRS editing domain and 1.7 A resolution crystal structure of the editing domain bound with [N-(L-threonyl)-sulfamoyl]adenosine, hanging drop vapor diffusion method

Thermus thermophilus

P96142

662398

enzyme complexed with tRNAVal and valyl-adenylate, hanging-drop vapour diffusion method, 20°C, 1 month, equal volumes of protein and crystallization solution: 50 mM N-(2-acetoamide)iminodiacetic acid sodium salt buffer, pH 6.5, 2% 2-propanol, 0.1 M lithium sulfate, 12% PEG4000, equilibration against reservoir solution: 50 mM N-(2-acetoamide)iminodiacetic acid sodium salt buffer, pH 6.5, 2% propanol, 0.1 M lithium sulfate, and 14% PEG 4000, ligand-free crystals by macro-seeding, X-ray diffraction structure determination at 2.9 A resolution, and analysis

Thermus thermophilus

-

653871

enzyme in complex with tRNAValCAC isoacceptor and an analogue of the Val-adenylate intermediate, hanging-drop vapour diffusion method, 2 months, 4°C, 7-10 mg/ml protein/tRNA/Val-AMS solution in a molar ration of 1:1.1:2, plus equal volume of crystallization solution containing 50 mM sodium cacodylate, pH 6.5, 1.0 ammonium sulfate, 10 mM MgSO4, 6% 1,8-diaminooctane, equilibration against a reservoir solution of 50 mM sodium cacodylate, pH 6.5, 2.8 M ammonium sulfate, 10 mM MgSO4, X-ray structure determination at 2.9 A resolution and analysis

Thermus thermophilus

-

650777

molecular dynamics simulation studies based on PDB structure ID 1wk9. Noncognate substrates Thr-AMP and Thr-A76, bind more strongly than the cognate substrates Val-AMP and Val-A76 in both pre- and post-transfer editing, respectivel

Thermus thermophilus

P96142

702702