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

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The enzyme appears in viruses and cellular organisms

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
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
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Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
no activity in Trypanosoma brucei
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
S-adenosyl-L-methionine + cytosine38 in tRNAAsp precursor
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp precursor
show the reaction diagram
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp(GTC)
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp(GTC)
show the reaction diagram
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-
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAspGTC
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAspGTC
show the reaction diagram
S-adenosyl-L-methionine + cytosine38 in tRNAGlu
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAGlu
show the reaction diagram
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25% of the activity with tRNAAsp, the activity with tRNAGlu is not affected by the presence of peptone
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?
S-adenosyl-L-methionine + cytosine38 in tRNAGly precursor
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAGly precursor
show the reaction diagram
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?
S-adenosyl-L-methionine + cytosine38 in tRNAGly(GCC)
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAGly(GCC)
show the reaction diagram
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-
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?
S-adenosyl-L-methionine + cytosine38 in tRNAGlyGCC
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAGlyGCC
show the reaction diagram
S-adenosyl-L-methionine + cytosine38 in tRNAVal precursor
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAVal precursor
show the reaction diagram
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-
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?
S-adenosyl-L-methionine + cytosine38 in tRNAValAAC
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAValAAC
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 + 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
S-adenosyl-L-methionine + cytosine38 in tRNAAsp precursor
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp precursor
show the reaction diagram
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-
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAsp(GTC)
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp(GTC)
show the reaction diagram
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-
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?
S-adenosyl-L-methionine + cytosine38 in tRNAAspGTC
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAspGTC
show the reaction diagram
S-adenosyl-L-methionine + cytosine38 in tRNAGly precursor
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAGly precursor
show the reaction diagram
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-
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?
S-adenosyl-L-methionine + cytosine38 in tRNAGly(GCC)
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAGly(GCC)
show the reaction diagram
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-
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?
S-adenosyl-L-methionine + cytosine38 in tRNAGlyGCC
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAGlyGCC
show the reaction diagram
S-adenosyl-L-methionine + cytosine38 in tRNAVal precursor
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAVal precursor
show the reaction diagram
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-
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?
S-adenosyl-L-methionine + cytosine38 in tRNAValAAC
S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAValAAC
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-aza-2'-deoxycytidine
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the catalytic mechanism is disrupted by the suicide inhibitor
5-azacytidine
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the catalytic mechanism is disrupted by the suicide inhibitor
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
queuine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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 is consistently upregulated in hundreds of tumor samples
Manually annotated by BRENDA team
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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
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Lin(neg) Sca1+cKit+ haematopoietic progenitor cells that represent a heterogeneous cell population containing the most primitive haematopoietic cells that have self-renewal capacity and haematopoietic progenitors that give rise to all mature cell types found in peripheral blood for a lifetime
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
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 strain BL21(DE3)
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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
alternative splicing of the full-length DNMT2 premRNA occurs in preimplantation embryos
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expression in Escherichia coli
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expression in NIH3T3 cells
overexpression of GFP-tagged DnmA in Dictyostelium discoideum
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phylogenetic analysis, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli
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recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cultivation of Schizosaccharomyces pombe in minimal medium leads to approximately 23% of tRNAAsp methylation
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methylation is not enhanced by stress conditions such as glucose starvation, heat stress or oxidative stress
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tRNAAsp methylation is induced to 100% when cells are grown in the presence of peptone
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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
D217H
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site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
D226Y
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site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
D255Y
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site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
E185K
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site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
E202Q
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site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
E317G
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site-directed mutagenesi, the mutant shows activity similar to the wild-type enzyme
E63K
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site-directed mutagenesis, the mutation causes a twofold increase in activity compared to the wild-type enzyme
G155S
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site-directed mutagenesis, the mutation causes an over fourfold decrease in activity compared to the wild-type enzyme
G155V
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site-directed mutagenesis, almost inactive mutant
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
L257V
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site-directed mutagenesis, the mutation causes an over fourfold decrease in activity compared to the wild-type enzyme
M72I
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site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
N264S
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site-directed mutagenesi, the mutant shows activity similar 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
R371H
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site-directed mutagenesis, almost inactive mutant
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
additional information