Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrion | - |
Homo sapiens | 5739 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-leucine + tRNAIle | Homo sapiens | - |
AMP + diphosphate + L-leucyl-tRNALeu | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q15031 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-leucine + tRNAIle | - |
Homo sapiens | AMP + diphosphate + L-leucyl-tRNALeu | - |
? |
Synonyms | Comment | Organism |
---|---|---|
leucyl-tRNA syntethase | - |
Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
malfunction | mutations in mitochondrial DNA determine important human diseases. The majority of the known pathogenic mutations are located in transfer RNA (tRNA) genes and are responsible for a wide range of currently untreatable disorders. The detrimental effects of mt-tRNA point mutations can be attenuated by increasing the expression of the cognate mt-aminoacyl-tRNA synthetases (aaRSs). The isolated C-terminal domain of human mt-leucyl-tRNA synthetase (LeuRS-Cterm) localizes to mitochondria and ameliorates the energetic defect in trans-mitochondrial cybrids carrying mutations either in the cognate mt-tRNALeu(UUR) or in the non-cognate mt-tRNAIle gene.Since the mt-LeuRS-Cterm does not possess catalytic activity, its rescuing ability is most likely mediated by a chaperon-like effect, consisting in the stabilization of the tRNA structure altered by the mutation | Homo sapiens |
additional information | analysis of the bacterial LeuRS structures (PDB IDs 2BTE and 4AS1) reveals that the isolated C-terminal domain of human mt-leucyl-tRNA synthetase (LeuRS-Cterm) interacts with the elbow region of the cognate tRNA and establishes a higher number of contacts with the sugar-phosphate backbone than with nucleotide-specific chemical groups, preferred interaction of human mt-LeuRS-Cterm with ribose and phosphate oxygen atoms | Homo sapiens |