6.1.1.4: leucine-tRNA ligase

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

Reaction

Synonyms

AaLeuRS, alphabeta-LeuRS, b0642, cytoplasmic LeuRS, EcLeuRS, GlLeuRS, HcleuRS, hs mt LeuRS, JW0637, LARS, LARS1, LARS2, Leucine translase, Leucine--tRNA ligase, Leucyl-transfer ribonucleate synthetase, Leucyl-transfer ribonucleic acid synthetase, Leucyl-transfer RNA synthetase, leucyl-tRNA ligase, leucyl-tRNA syntethase, Leucyl-tRNA synthetase, leucyl-tRNA synthetase 1, leucyl�tRNA synthetase, LeuRS, LeuRS1, LeuRS2, LeuRSTT, leuS, LRS, MmLeuRS, More, mt leucyl-tRNA synthetase, mt-LeuRS, mtLeuRS, PhLeuRS, Synthetase, leucyl-transfer ribonucleate, ycLeuRS

ECTree

     6 Ligases

         6.1 Forming carbon-oxygen bonds

             6.1.1 Ligases forming aminoacyl-tRNA and related compounds

                6.1.1.4 leucine-tRNA ligase

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Results	in table
11	Activating Compound
58778	AA Sequence
7	Application
1	CAS Registry Number
64	Cloned(Commentary)
62	Cofactor
13	Crystallization (Commentary)
249	Disease/ Diagnostics
1	Expression
65	General Information
7	General Stability
47	IC50 Value
155	Inhibitors
173	kcat/KM [mM/s]
369	KM Value [mM]
48	Localization
71	Metals/Ions
49	Molecular Weight [Da]
78	Natural Substrates/ Products (Substrates)
372	Organism
4	Pathway
118	PDB ID
61	pH Optimum
1	pH Range
3	Posttranslational Modification
348	Protein Variants
65	Purification (Commentary)
10	Reaction
40	Reaction Type
153	Reference
2	Renatured (Commentary)
32	Source Tissue
45	Specific Activity [micromol/min/mg]
8	Storage Stability
265	Substrates and Products (Substrate)
55	Subunits
329	Synonyms
1	Systematic Name
48	Temperature Optimum [°C]
3	Temperature Range [°C]
9	Temperature Stability [°C]
342	Turnover Number [1/s]

Posttranslational Modification

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Posttranslational Modification on EC 6.1.1.4 - leucine-tRNA ligase

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POSTTRANSLATIONAL MODIFICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

lipoprotein

Rattus norvegicus

-

high molecular weight aminoacyl-tRNA synthetase complex contains lipid. Delipidation does not affect the size or activity of the complex, but a variety of functional and structural properties of individual synthetases in the complex are altered: sensitivity to salts plus detergents, temperature inactivation, hydrophobicity, sensitivity to protease digestion

127

proteolytic modification

Homo sapiens

-

processing of the mitochondrial isozyme by removing of the mitochondrial targeting presequence in the mitochondria of insect cells

653766

additional information

Escherichia coli

-

the enzyme contains proteolytic cleavage sites at the peptide bonds between T252 and F253, E292 and A293, K327 and A328, and P368 and D369

649867