Information on EC 2.1.1.204 - tRNA (cytosine38-C5)-methyltransferase

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The expected taxonomic range for this enzyme is: Coelomata

EC NUMBER
COMMENTARY hide
2.1.1.204
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RECOMMENDED NAME
GeneOntology No.
tRNA (cytosine38-C5)-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + cytosine38 in tRNA = S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (cytosine38-C5)-methyltransferase
The eukaryotic enzyme catalyses methylation of cytosine38 in the anti-codon loop of tRNAAsp(GTC), tRNAVal(AAC) and tRNAGly(GCC). Methylation by Dnmt2 protects tRNAs against stress-induced cleavage by ribonuclease [3].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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DNMT2 methylates RNA by employing a DNA methyltransferase-like catalytic mechanism, which is clearly different from the mechanism of other RNA MTases. DNMT2 has changed its substrate specificity from DNA to RNA in the course of its evolution
malfunction
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 + cytosine38 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA
show the reaction diagram
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
show the reaction diagram
additional information
?
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DNMT2 induces a conformational change in the tRNA of the DNMT2-tRNA complex
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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 + cytosine38 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA
show the reaction diagram
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
8
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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Dnmt2-EGFP is highly expressed in the germarium, blastocyst and cyst stages of the female germ line with the exception of follicle cells. Dnmt2-EGFP is mostly present in the cytoplasm but can also be found in nurse cell nuclei. In the male germ line, Dnmt2-EGFP is expressed in most cells, including stem cells as well as in maturing spermatocytes with the exception of the post-mitotic hub cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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Dnmt2 is both a cytoplasmic and a nuclear protein. A significant amount of Dnmt2 is bound to the nuclear matrix. Dnmt2-EGFP(enhanced-green-fluorescent-protein) enters prophase nuclei and shows a spindle-like localization pattern during mitotic divisions. This localization is microtubule dependent. Dnmt2 can access DNA during mitotic cell divisions
Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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structural modeling of DNMT2, overview
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli to over 90% purity, except for mutant R84A, which is about 75% pure
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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expression in NIH3T3 cells
phylogenetic analysis, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C292A
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about 3fold reduction in RNA binding affinity. Significant residual activity
K122A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
K168A
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site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
K196A
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site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
K241A
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site-directed mutagenesis, the mutant shows moderately reduced activity compared to the wild-type enzyme
K251A
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site-directed mutagenesis, the mutant shows moderately reduced activity compared to the wild-type enzyme
K254A
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site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
K271A
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site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
K295A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
K346A
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site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
K363A
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site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
K367A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
K387A
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site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
R240A
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site-directed mutagenesis, the mutant shows only slightly reduced activity compared to the wild-type enzyme
R275A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R288A
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site-directed mutagenesis, the mutant shows moderately reduced activity compared to the wild-type enzyme
R289A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R369A
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site-directed mutagenesis, the mutant shows moderately reduced activity compared to the wild-type enzyme
R371A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R84A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R95A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme