Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 6.1.1.12 extracted from

  • Messmer, M.; Florentz, C.; Schwenzer, H.; Scheper, G.C.; van der Knaap, M.S.; Marechal-Drouard, L.; Sissler, M.
    A human pathology-related mutation prevents import of an aminoacyl-tRNA synthetase into mitochondria (2011), Biochem. J., 433, 441-446.
    View publication on PubMed
Search for more literature for 6.1.1.12

Protein Variants

Protein Variants Comment Organism
S45G a naturally occuring mutation identified in patients suffering leukoencephalopathy with brain stem and spinal cord involvement and lactate elevation. The mutant enzyme is not processed due to nontranslocation of the protein Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Homo sapiens 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q6PI48 gene DARS2
-

Source Tissue

Source Tissue Comment Organism Textmining
HEK-293T cell
-
 Homo sapiens
-

Synonyms

Synonyms Comment Organism
Aspartyl-tRNA synthetase
-
 Homo sapiens
mitochondrial aspartyl-tRNA synthetase
-
 Homo sapiens
mt-AspRS
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3
-
 assay at Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Homo sapiens

General Information

General Information Comment Organism
malfunction LBSL, i.e. leukoencephalopathy with brain stem and spinal cord involvement and lactate elevation, is a monogenic disease associated with a large variety of mutations affecting the human nuclear gene DARS2, encoding mt-AspRS, overview Homo sapiens
physiological function the mitochondrial aspartyl-tRNA synthetase is a key enzyme for mitochondrial translation and is correlated with leukoencephalopathy Homo sapiens