6.1.1.19: arginine-tRNA ligase

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

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Synonyms

Arg-tRNA synthetase, Arginine translase, Arginine--tRNA ligase, Arginine-tRNA synthetase, Arginyl transfer ribonucleic acid synthetase, Arginyl-transfer RNA synthetase, Arginyl-tRNA synthetase, arginyl�tRNA synthetase, ArgRS, ArgS2, MtArgRS, RARS, RARS2, RRS, Synthetase, arginyl-transfer ribonucleate

ECTree

     6 Ligases

         6.1 Forming carbon-oxygen bonds

             6.1.1 Ligases forming aminoacyl-tRNA and related compounds

                6.1.1.19 arginine-tRNA ligase

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Results	in table
7	Activating Compound
54070	AA Sequence
1	CAS Registry Number
28	Cloned(Commentary)
26	Cofactor
12	Crystallization (Commentary)
122	Disease/ Diagnostics
3	Expression
4	General Information
8	General Stability
2	IC50 Value
34	Inhibitors
12	kcat/KM [mM/s]
2	Ki Value [mM]
132	KM Value [mM]
9	Localization
15	Metals/Ions
30	Molecular Weight [Da]
24	Natural Substrates/ Products (Substrates)
291	Organism
4	Pathway
28	PDB ID
9	pH Optimum
1	pH Range
2	pI Value
2	Posttranslational Modification
33	Protein Variants
38	Purification (Commentary)
9	Reaction
8	Reaction Type
85	Reference
21	Source Tissue
21	Specific Activity [micromol/min/mg]
4	Storage Stability
103	Substrates and Products (Substrate)
26	Subunits
63	Synonyms
1	Systematic Name
8	Temperature Optimum [°C]
3	Temperature Range [°C]
8	Temperature Stability [°C]
42	Turnover Number [1/s]

General Stability

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General Stability on EC 6.1.1.19 - arginine-tRNA ligase

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GENERAL STABILITY

ORGANISM

UNIPROT

LITERATURE

affected by repeated freeze-thaw cycles

Escherichia coli

-

276

complexed arginyl-tRNA synthetase is more stable than the free enzyme

Oryctolagus cuniculus

-

261

degradation of the enzyme during purification may be due to the influence of the immobilized tRNA, and is enhanced by high salt concentrations

Mus musculus

-

262

not affected by four freeze-thaw cycles

Saccharomyces pastorianus

-

272

presence of ribosomes or of high concentrations of albumin oppose the conformational change of arginyl-tRNA synthetase which results in a loss of activity when the enzyme is incubated at low concentrations

Triticum aestivum

-

274

reduced glutathione effectively protects the enzyme from thermal inactivation

Oryctolagus cuniculus

-

261

tRNA reduces thermal inactivation

Oryctolagus cuniculus

-

261

zinc or Triton X-100 increases thermal inactivation

Oryctolagus cuniculus

-

261