Information on EC 2.1.1.214 - tRNA (guanine10-N2)-methyltransferase

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The expected taxonomic range for this enzyme is: Saccharomyces cerevisiae

EC NUMBER
COMMENTARY hide
2.1.1.214
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RECOMMENDED NAME
GeneOntology No.
tRNA (guanine10-N2)-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + guanine10 in tRNA = S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNA
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
tRNA methylation (yeast)
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (guanine10-N2)-methyltransferase
In contrast to the archaeal enzyme tRNA (guanine10-N2)-dimethyltransferase (EC 2.1.1.213), tRNA (guanine10-N2)-methyltransferase from yeast does not catalyse the methylation from N2-methylguanine10 to N2-dimethylguanine10 in tRNA.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
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Trm11p and Trm112p are two interacting proteins that are both required for catalyzing the formation of m2G at position 10 in several tRNAs. Trm11p is the catalytic subunit, but also Trm112p is essential for the formation of m2G10, Trm112p is essential for the activity of Trm11p, another tRNA methyltransferase, because Trm112p is capable of directing the proper folding of Trm11p, leading to the synthesis of an active complex. Trm112p is required in vivo for the formation of mcm5U34 and mcm5s2U34, overview. Trm112p is also required for the activity of Mtq2p, a protein methyltransferase that catalyzes the methylation of the glutamine of the universally conserved GGQ tripeptide of the translation termination factor eRF1/Sup45. Trm112p is associated with other partners involved in ribosome biogenesis and chromatin remodeling, suggesting that it has additional roles in the cell
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 + guanine10 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNA
show the reaction diagram
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
S-adenosyl-L-methionine + guanine10 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNA
show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zinc
the enzyme is composed of at least two subunits that are associated in vivo: Trm11p, which is the catalytic subunit, and Trm112p, a putative zinc-binding protein
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Zinc
the regulatory subunit Trm112 contains a zinc-finger
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged Trm112p, alone or with Trm9p, from Escherichia coli strain S15 (DE3-pLysS) by nickel affinity chromatography and desalting gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene TRM112, phylogenetic analysis, expression of His-tagged Trm112p, alone or with Trm9p, in Escherichia coli strain S15 (DE3-pLysS), Trm112p forms a complex with Trm9p, which renders the latter soluble
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recombinant Trm11p expressed in Escherichia coli exhibited no m2G10 formation activity. Trm112p and Trm11p are both required for the formation of m2G10 in vivo as well as in vitro
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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a plasmid containing a wild-type copy of the TRM112 gene (pBL652) is able to restore the formation of the two modified nucleosides in a trm112-0 strain