Literature summary for 2.1.1.200 extracted from

Somme, J.; Van Laer, B.; Roovers, M.; Steyaert, J.; Versees, W.; Droogmans, L.
Characterization of two homologous 2'-O-methyltransferases showing different specificities for their tRNA substrates (2014), RNA, 20, 1257-1271.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of the catalytic domain	Sulfolobus acidocaldarius

Organism

Organism	UniProt	Comment	Textmining
Sulfolobus acidocaldarius	Q4JB16	-	-
Sulfolobus acidocaldarius DSM 639	Q4JB16	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
S-adenosyl-L-methionine + cytidine32 in tRNA	while the four canonical nucleosides are substrates of the Escherichia coli enzyme at position 32 of tRNA, the archaeal TrmJ can only methylate the ribose of a cytidine	Sulfolobus acidocaldarius	S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA	-	?
S-adenosyl-L-methionine + cytidine32 in tRNA	while the four canonical nucleosides are substrates of the Escherichia coli enzyme at position 32 of tRNA, the archaeal TrmJ can only methylate the ribose of a cytidine	Sulfolobus acidocaldarius DSM 639	S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA	-	?

Synonyms

Synonyms	Comment	Organism
Saci_0621	-	Sulfolobus acidocaldarius

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Release 2023.1 (January 2023)