Information on EC 2.1.1.B43 - tRNA (cytosine49-C5)-methyltransferase

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The expected taxonomic range for this enzyme is: Pyrococcus abyssi

EC NUMBER
COMMENTARY hide
2.1.1.B43
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
tRNA (cytosine49-C5)-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + cytosine49 in tRNA = S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (cytosine49-C5)-methyltransferase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + cytosine49 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA
show the reaction diagram
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 50C instead of 80C, methylation becomes more specific for the 4751 sequence. Addition of archease to the methylation reactions with Pyrococcus abyssi tRNAAsp at 80C increases modification within the oligonucleotide ACCCG that contains cytidine49, while reducing modification at unspecific sites. The unstructured poly(C)RNA is effectively methylated at 50C, 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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35750
calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 35747, calculated from sequence
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE