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 50°C instead of 80°C, methylation becomes more specific for the 47–51 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
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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
35747
x * 35747, calculated from sequence
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