Literature summary for 6.1.1.3 extracted from

Ishikura, H.; Nagaoka, Y.; Yokozawa, J.; Umehara, T.; Kuno, A.; Hasegawa, T.
Threonyl-tRNA synthetase of archaea: importance of the discriminator base in the aminoacylation of threonine tRNA (2000), Nucleic Acids Symp. Ser., 2000, 83-84.

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Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + L-threonine + tRNAThr	Haloferax volcanii	-	AMP + diphosphate + L-threonyl-tRNAThr	-	?

Organism

Organism	UniProt	Comment	Textmining
Haloferax volcanii	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-threonine + tRNAThr	-	Haloferax volcanii	AMP + diphosphate + L-threonyl-tRNAThr	-	?
ATP + L-threonine + tRNAThr	Escherichia coli threonine tRNA is not aminoacylated by the Haloferax volcanii enzyme. The Escherichia coli mutant tRNAThr having U73 is threonylated by the Haloferax volcanii enzyme. The discriminator base U73 of Haloferax volcanii tRNAThr is a strong determinant for the recognition by threonyl-tRNA synthetase	Haloferax volcanii	AMP + diphosphate + L-threonyl-tRNAThr	-	?

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Release 2023.1 (January 2023)