Information on EC 2.1.1.256 - tRNA (guanine6-N2)-methyltransferase

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The expected taxonomic range for this enzyme is: Archaea, Bacteria

EC NUMBER
COMMENTARY hide
2.1.1.256
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RECOMMENDED NAME
GeneOntology No.
tRNA (guanine6-N2)-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + guanine6 in tRNA = S-adenosyl-L-homocysteine + N2-methylguanine6 in tRNA
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (guanine6-N2)-methyltransferase
The enzyme specifically methylates guanine6 at N2 in tRNA.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
DSM 2661, gene MJ0438 or trm14
UniProt
Manually annotated by BRENDA team
DSM 2661, gene MJ0438 or trm14
UniProt
Manually annotated by BRENDA team
gene PF1002
UniProt
Manually annotated by BRENDA team
gene TTC1157
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
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 + guanine6 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine6 in tRNA
show the reaction diagram
S-adenosyl-L-methionine + guanine6 in tRNACys
S-adenosyl-L-homocysteine + N2-methylguanine6 in tRNACys
show the reaction diagram
additional information
?
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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
S-adenosyl-L-methionine + guanine6 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine6 in tRNA
show the reaction diagram
S-adenosyl-L-methionine + guanine6 in tRNACys
S-adenosyl-L-homocysteine + N2-methylguanine6 in tRNACys
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
sinefungin
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant detagged enzyme in complex with S-adenosyl-L-methionine or reaction product S-adenosyl-homocysteine, and inhibitor sinefungin, hanging drop vapor diffusion, protein in 50 mM Tris-HCl, pH 8.0, 10 mM MgCl2, 500 mM NaCl, 280 mM imidazole, and 1 mM DTT, mixing in a 1:1 ratio with crystallization solution containing 100 mM Tris-acetate, pH 8.0, 32% PEG 4000, and 15% glycerol, for the phasing, selenomethionine-derivatized PfTrm14 is crystallized in a crystallization solution containing 100 mM Tris-acetate, pH 8.0, 32% PEG 4000, 15% glycerol, after streak seeding from a native PfTrm14 crystal, crystal soaking in mother liquor containing 1 mM ligand, X-ray diffraction structure determination and analysis at 1.95-2.4 A resolution
purified recombinant His-tagged enzyme in complex with S-adenosyl-L-methionine or reaction product S-adenosyl-homocysteine, and inhibitor sinefungin, hanging drop vapor diffusion, protein in 50 mM Tris-HCl, pH 8.0, 250 mM NaCl, and 350 mM imidazole, mixing in a 1:1 ratio with crystallization solution 100 mM citrate/phosphate, pH 3.5, 15% PEG 6000, 200 mM NaCl, and 100 mM sodium citrate, crystal soaking in mother liquor containing 1 mM ligand, X-ray diffraction structure determination and analysis at 2.16 A resolution, solved in the apo state by molecular replacement to a resolution of 2.05 A
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of the N-terminally His-tagged emzyme in in Escherichia coli strain Rosetta (DE3)
expression of the N-terminally His-tagged enzyme in in Escherichia coli strain BL21 (DE3)
gene MJ0438 or trm14, DNA and amino acid sequence determination, analysis and comparisons, phylogenetic analysis