Literature summary for 2.1.1.B43 extracted from

Auxilien, S.; El Khadali, F.; Rasmussen, A.; Douthwaite, S.; Grosjean, H.
Archease from Pyrococcus abyssi improves substrate specificity and solubility of a tRNA m5C methyltransferase (2007), J. Biol. Chem., 282, 18711-18721.

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Activating Compound

Activating Compound	Comment	Organism	Structure
archaease	in vitro, the purified recombinant methyltransferase catalyzes 5-methylcytosine formation at several cytosines within tRNAs with preference for C49. The specificity of the methyltransferase is increased by the archease. In solution, the archease exists as a monomer, trimer, and hexamer. Only the oligomeric states bind the methyltransferase and prevent its aggregation, in addition to hindering dimerization of the methyltransferase-tRNA complex	Pyrococcus abyssi

Cloned(Commentary)

Cloned (Comment)	Organism
-	Pyrococcus abyssi

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
35747	-	x * 35747, calculated from sequence	Pyrococcus abyssi
35750	-	calculated from sequence	Pyrococcus abyssi

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus abyssi	Q9V106	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Pyrococcus abyssi

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
S-adenosyl-L-methionine + cytosine49 in tRNA	tRNAASp. In vitro, the purified recombinant methyltransferase catalyzes 5-methylcytosine formation at several cytosines within tRNAs with preference for C49. When tRNA is incubated with the PAB1947 enzyme at 50°C instead of 80°C, methylation becomes more specific for the 4751 sequence. Addition of archease to the methylation reactions with Pyrococcus abyssi tRNAAsp at 80°C increases modification within the oligonucleotide ACCCG that contains cytidine49, while reducing modification at unspecific sites. The unstructured poly(C)RNA is effectively methylated at 50°C, with most of the tritiated label from the methyl donor becoming incorporated into the RNA. However, when the recombinant PAB1947 enzyme is substituted with a Pyrococcus abyssi cell extract, no methylation of the poly(C) RNA occurs	Pyrococcus abyssi	S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA	-	?

Subunits

Subunits	Comment	Organism
?	x * 35747, calculated from sequence	Pyrococcus abyssi

Synonyms

Synonyms	Comment	Organism
PAB1946	-	Pyrococcus abyssi

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Release 2023.1 (January 2023)