Literature summary extracted from

Shugart, L.; Chastain, B.
Escherichia coli tRNA (uracil-5-)-methyltransferase: Inhibition by analogues of adenosylhomocysteine (1979), Enzyme, 24, 353-357.

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
2.1.1.35	S-adenosyl-L-homocysteine	product inhibition, competitive to S-adenosyl-L-methionine	Escherichia coli
2.1.1.35	structural analogues of S-adenosyl-L-homocysteine	inhibition competitive to S-adenosyl-L-methionine	Escherichia coli

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.1.1.35	Escherichia coli	-	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2.1.1.35	S-adenosyl-L-methionine + uridine54 in tRNA	S-adenosyl-L-methionine/S-adenosyl-L-homocysteine binding site, terminal NH2-group of the amino acid moiety is nessecary for activity	Escherichia coli	S-adenosyl-L-homocysteine + 5-methyluridine54 in tRNA	-	?

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
2.1.1.35	S-adenosyl-L-methionine	-	Escherichia coli

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Release 2023.1 (January 2023)