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

BRENDA support

Literature summary for 6.1.1.6 extracted from

  • Cho, H.Y.; Ul Mushtaq, A.; Lee, J.Y.; Kim, D.G.; Seok, M.S.; Jang, M.; Han, B.W.; Kim, S.; Jeon, Y.H.
    Characterization of the interaction between lysyl-tRNA synthetase and laminin receptor by NMR (2014), FEBS Lett., 588, 2851-2858 .
    View publication on PubMed
Search for more literature for 6.1.1.6

Inhibitors

Inhibitors Comment Organism Structure
BC-K-01 the inhibitor interferes with the binding between enzyme KRS and laminin receptor 37LRP domain Homo sapiens
BC-K-YH16899 the inhibitor interferes with the binding between enzyme KRS and laminin receptor 37LRP domain Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Homo sapiens 5829
-
mitochondrion
-
 Homo sapiens 5739
-
nucleus
-
 Homo sapiens 5634
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Homo sapiens

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 Q15046
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-lysine + tRNALys
-
 Homo sapiens AMP + diphosphate + L-lysyl-tRNALys
-
 ?
additional information selective binding of the C-terminal region of 37 kDa laminin receptor precursor 37LRP to the KRS anticodon-binding domain, surface plasmon resonance Homo sapiens ?
-
 ?

Subunits

Subunits Comment Organism
More structure analysis of the flexible N-terminal extension and anticodon-binding domain, NMR analysis, overview Homo sapiens

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Homo sapiens

General Information

General Information Comment Organism
physiological function lysyl-tRNA synthetase (KRS) is a multi-functional enzyme, which, in addition to its primary function of aminoacylation of lysine onto the cognate tRNA, has various noncanonical functions. Enzyme KRS interacts with the laminin receptor (LR/RPSA) and enhances laminin-induced cell migration in cancer metastasis. The anticodon-binding domain of KRS binds directly to the C-terminal region of 37 kDa laminin receptor precursor 37LRP, and inhibitors BC-K-01 and BC-K-YH16899 interfere with KRS–37LRP binding. In addition, the anticodon-binding domain of KRS binds to laminin. Furthermore, KRS is a major source of diadenosine tetraphosphate (Ap4A) in immunologically activated mast cells, and via translocation into the nucleus, KRS controls the expression of microphthalmia-associated transcription factor (MITF)-inducible genes in allergic responses Homo sapiens