Literature summary for 2.3.2.6 extracted from

Taki, M.; Kuno, A.; Matoba, S.; Kobayashi, Y.; Futami, J.; Murakami, H.; Suga, H.; Taira, K.; Hasegawa, T.; Sisido, M.
Leucyl/phenylalanyl-tRNA-protein transferase-mediated chemoenzymic coupling of N-terminal Arg/Lys units in post-translationally processed proteins with non-natural amino acids (2006), ChemBiochem, 7, 1676-1679.

Search for more literature for 2.3.2.6

Application

Application	Comment	Organism
synthesis	use of enzyme to link non-natural amino acids to the N termini of target proteins through the use of tRNAPhes aminoacylated with various types of non-natural amino acids	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1-naphthylalanyl-tRNA + L-Lys-SoCBM13	a xylan binding domain with N-terminal Lys. Introduction of 1-naphthylalanine is more difficult than of 2-naphthylalanine	Escherichia coli	1-naphthylalanyl-L-Lys-SoCBM13 + tRNA	-	?
2-naphthylalanyl-tRNA + L-Lys-SoCBM13	a xylan binding domain with N-terminal Lys. Introduction of 1-naphthylalanine is more difficult than of 2-naphthylalanine	Escherichia coli	2-naphthylalanyl-L-Lys-SoCBM13 + tRNA	-	?
3-nitrotyrosyl-tRNA + L-Arg-casein	-	Escherichia coli	3-nitrotyrosyl-L-Arg-casein + tRNA	-	?
3-nitrotyrosyl-tRNA + L-Lys-glutathione S-transferase	-	Escherichia coli	3-nitrotyrosyl-L-Lys-glutathione S-transferase + tRNA	-	?
3-nitrotyrosyl-tRNA + L-Lys-SoCBM13	a xylan binding domain with N-terminal Lys	Escherichia coli	3-nitrotyrosyl-L-Lys-SoCBM13 + tRNA	-	?

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Release 2023.1 (January 2023)