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Literature summary for 6.1.1.21 extracted from

  • van Dooren, S.H.; Raijmakers, R.; Pluk, H.; Lokate, A.M.; Koemans, T.S.; Spanjers, R.E.; Heck, A.J.; Boelens, W.C.; van Venrooij, W.J.; Pruijn, G.J.
    Oxidative stress-induced modifications of histidyl-tRNA synthetase affect its tRNA aminoacylation activity but not its immunoreactivity (2011), Biochem. Cell Biol., 89, 545-553.
    View publication on PubMed
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-histidine + tRNAHis Homo sapiens
-
 AMP + diphosphate + L-histidyl-tRNAHis
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Oxidation Stability

Oxidation Stability Organism
the tRNA aminoacylation activity of the enzyme is increased upon oxidative modification by hydrogen peroxide Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
JURKAT cell
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-histidine + tRNAHis
-
 Homo sapiens AMP + diphosphate + L-histidyl-tRNAHis
-
 ?

Synonyms

Synonyms Comment Organism
HisRS
-
 Homo sapiens
Histidyl-tRNA synthetase
-
 Homo sapiens
Jo-1
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Homo sapiens