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Information on EC 2.1.1.B43 - tRNA (cytosine49-C5)-methyltransferase and Organism(s) Pyrococcus abyssi and UniProt Accession Q9V106

for references in articles please use BRENDA:EC2.1.1.B43
preliminary BRENDA-supplied EC number
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EC Tree
     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.B43 tRNA (cytosine49-C5)-methyltransferase
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This record set is specific for:
Pyrococcus abyssi
UNIPROT: Q9V106 not found.
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The taxonomic range for the selected organisms is: Pyrococcus abyssi
The expected taxonomic range for this enzyme is: Pyrococcus abyssi
Reaction Schemes
hide
S-adenosyl-L-methionine
+
cytosine49 in tRNA
=
S-adenosyl-L-homocysteine
+
5-methylcytosine49 in tRNA
+
cytosine49 in tRNA
=
+
5-methylcytosine49 in tRNA
Synonyms
PAB1946, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (cytosine49-C5)-methyltransferase
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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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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35747
x * 35747, calculated from sequence
35750
calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 35747, calculated from sequence
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
J. Biol. Chem.
282
18711-18721
2007
Pyrococcus abyssi (Q9V106)
Manually annotated by BRENDA team