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Literature summary for 6.1.1.6 extracted from

  • Motzik, A.; Nechushtan, H.; Foo, S.Y.; Razin, E.
    Non-canonical roles of lysyl-tRNA synthetase in health and disease (2013), Trends Mol. Med., 19, 726-731.
    View publication on PubMed
Search for more literature for 6.1.1.6

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-lysine + tRNALys Homo sapiens
-
 AMP + diphosphate + L-lysyl-tRNALys
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-lysine + tRNALys
-
 Homo sapiens AMP + diphosphate + L-lysyl-tRNALys
-
 ?

Synonyms

Synonyms Comment Organism
LysRS
-
 Homo sapiens
Lysyl-tRNA synthetase
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Homo sapiens

General Information

General Information Comment Organism
malfunction loss of function mutations in the catalytic domain of the enzyme are found in Charcot-Marie-Tooth disease patients. Mitochondrial enzyme binds to mutant superoxide dismutase 1, forming protein aggregates that damage mitochondrial activity and lead to disease onset in amoytophic lateral sclerosis Homo sapiens
physiological function the enzyme plays an essential role in HIV replication, transcriptional regulation, cytokine-like signaling, and transport of proteins to the cell membrane. The enzyme can induce cancer cell migration through interaction with the 67 kDa laminin receptor. The enzyme facilitates the translocation and surface exposure of calreticulin, activating the CRT pathway which leads to death of stressed cells Homo sapiens