Literature summary 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.

Natural Substrates/ Products (Substrates)

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

Organism

EC Number	Organism	UniProt	Comment	Textmining
6.1.1.21	Homo sapiens	-	-	-

Oxidation Stability

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

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
6.1.1.21	JURKAT cell	-	Homo sapiens	-

Substrates and Products (Substrate)

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

Synonyms

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

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
6.1.1.21	ATP	-	Homo sapiens

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Release 2023.1 (January 2023)