Information on EC 2.1.1.213 - tRNA (guanine10-N2)-dimethyltransferase

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The expected taxonomic range for this enzyme is: Pyrococcus abyssi

EC NUMBER
COMMENTARY hide
2.1.1.213
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RECOMMENDED NAME
GeneOntology No.
tRNA (guanine10-N2)-dimethyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 S-adenosyl-L-methionine + guanine10 in tRNA = 2 S-adenosyl-L-homocysteine + N2-dimethylguanine10 in tRNA
show the reaction diagram
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S-adenosyl-L-methionine + guanine10 in tRNA = S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNA
show the reaction diagram
S-adenosyl-L-methionine + N2-methylguanine10 in tRNA = S-adenosyl-L-homocysteine + N2-dimethylguanine10 in tRNA
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (guanine10-N2)-dimethyltransferase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + guanine10 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine10 in tRNA
show the reaction diagram
S-adenosyl-L-methionine + guanine10 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNA
show the reaction diagram
additional information
?
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model for a potential binding mode for the THUMP domain, which may be common to various RNA modification enzymes that specifically modify nucleotides in the 3D-core of the tRNA molecule
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + guanine10 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine10 in tRNA
show the reaction diagram
Q9UY84
depending on the experimental conditions used, as well as the tRNA substrate tested, the enzymatic reaction leads to the formation of either N2-methyl or N2-dimethylguanosine. N2-Dimethylguanine10 accumulates during incubation at 50C, whereas the formation of N2-methylguanine10 appears to be a transient intermediate. At 30C, N2-dimethylguanine10 is efficiently formed, whereas the formation of N2-methylguanine10 is considerably slowed compared with that at higher temperatures
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?
S-adenosyl-L-methionine + guanine10 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNA
show the reaction diagram
Q9UY84
depending on the experimental conditions used, as well as the tRNA substrate tested, the enzymatic reaction leads to the formation of either N2-methyl or N2-dimethylguanosine. N2-Dimethylguanine10 accumulates during incubation at 50C, whereas the formation of N2-methylguanine10 appears to be a transient intermediate. At 30C, N2-dimethylguanine10 is efficiently formed, whereas the formation of N2-methylguanine10 is considerably slowed compared with that at higher temperatures
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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yield of G10 dimethylation in transcript of tRNAAsp greatly depends on the presence of Mg2+, with an optimal concentration around 5 mM. In contrast, formation of N2-monomethylguanine10 is not strictly dependent on the presence of Mg2+
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 39000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
86
noticeable unfolding of the protein (more than 5%) is detected above 86C
102
midpoint melting temperature
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purification of recombinant THUMPalpha module
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
construction of a N-terminal 6His-tagged THUMPalpha overexpressing plasmid, expression in Escherichia coli. THUMP i.e. (THioUridine synthases, RNA Methyltransferases and Pseudo-uridine synthases)-containing N-terminal domain
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overexpression in Escherichia coli