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Information on EC 2.1.1.37 - DNA (cytosine-5-)-methyltransferase and Organism(s) Mus musculus and UniProt Accession O88508
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2.1.1.37 DNA (cytosine-5-)-methyltransferaseSpecify your search results
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- 2.1.1.37
- histone
- methyltransferases
- cpg
-
hypermethylation
-
demethylation
- chromatin
- leukemia
- myeloid
- deacetylase
-
dnmts
- 5-aza-2'-deoxycytidine
- bisulfite
- tumorigenesis
- carcinogenesis
- 5-azacytidine
-
methylation-specific
-
hematopoietic
-
myelodysplastic
-
imprint
-
unmethylated
- 5-methylcytosine
- mtases
- decitabine
- hdacs
- endonuclease
- hematologic
-
cytogenetic
-
epigenome
-
pluripotent
-
restriction-modification
-
methylome
-
trimethylation
-
trichostatin
- blastocyst
-
re-expression
- heterochromatin
- o6-methylguanine
-
centromeric
-
nanog
- p16ink4a
- cdh1
-
flt3-itd
- adomet
-
polycomb
-
methylation-sensitive
-
leukemogenesis
-
rassf1a
-
h3k9me3
- biotechnology
-
line-1
- hpaii
- drug development
- analysis
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
dnmt1, dnmt3a, dna methyltransferase, dnmt3b, dna methyltransferase 1, dnmt2, dna mtase, nsun2, dna methylase, dna methyltransferase 3a, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C5-MTase
-
-
-
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cytosine 5-methyltransferase
-
-
-
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cytosine DNA methylase
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-
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cytosine DNA methyltransferase
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-
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cytosine-specific DNA methyltransferase
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-
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DCMT
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deoxyribonucleate methylase
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deoxyribonucleate methyltransferase
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deoxyribonucleic (cytosine-5-)-methyltransferase
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deoxyribonucleic acid (cytosine-5-)-methyltransferase
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deoxyribonucleic acid methylase
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deoxyribonucleic acid methyltransferase
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deoxyribonucleic acid modification methylase
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deoxyribonucleic methylase
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DNA 5-cytosine methylase
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-
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DNA cytosine c5 methylase
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DNA cytosine methylase
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DNA methylase
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-
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DNA methyltransferase
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DNA transmethylase
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DNA-cytosine 5-methylase
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-
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DNA-cytosine methyltransferase
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DNMT3B
EcoRI methylase
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methylphosphotriester-DNA methyltransferase
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methyltransferase, deoxyribonucleate
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type II DNA methylase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + DNA containing cytosine = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
sequential ordered bi-bi kinetic mechanism in which DNA binds to the enzyme first, followed by S-adenosyl-L-homocysteine and methylated DNA are released, formation of an enzyme-DNA-DNA ternary complex
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:DNA (cytosine-5-)-methyltransferase
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CAS REGISTRY NUMBER
COMMENTARY
9037-42-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + CpA
S-adenosyl-L-homocysteine + CpA containing 5-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + CpG
S-adenosyl-L-homocysteine + CpG containing 5-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + CpA
S-adenosyl-L-homocysteine + CpA containing 5-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + CpT
S-adenosyl-L-homocysteine + CpT containing 5-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
the enzyme is a de novo-type DNA methyltransferase
-
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
P-19 cells possess catalytically active Dnmt1, Dnmt2, Dnmt3a and Dnmt3b. Dnmt1 and Dnmt3b have the greatest amount of methylation activity directed at the endogenous genome
-
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
poly(dGdC)-poly(dGdC) or poly(dIdC)-poly(dIdC)
-
-
?
DNA + S-adenosyl-L-methionine
DNA containing 5-methylcytosine + S-adenosyl-L-homocysteine
-
-
-
-
?
DNA + S-adenosyl-L-methionine
DNA containing 5-methylcytosine + S-adenosyl-L-homocysteine
-
both DNMT3A and DNMT3B are involved in de novo DNA methylation. 5'-Cytosine methylation is a common epigenetic modification in eukaryotic genomes
-
-
?
DNA + S-adenosyl-L-methionine
DNA containing 5-methylcytosine + S-adenosyl-L-homocysteine
-
DNMT1 participates in epigenetic reprogramming through its ability to distinguish different categories of methylated sequences. Genomic imprinting is a mammalian epigenetic process that distinguishes maternal and paternal alleles to ensure parent-specific, monoallelic expression of imprinted genes. Preimplantation DNMT1-dependent maintenance mechanism specifically targets DMD sequences, e.g. of IAP, alpha-actin, Snurf/Snrpn, H19, Gnas, and Gtl2 DMD, overview
-
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
-
both native and denatured DNA are methylated, with calf thymus DNA the double stranded form is the better substrate but the enzyme preferentially methylates single stranded E. coli DNA even in the native preparation. Homologous ascites DNA can be methylated, but only to about 5% of the level of the best substrate, undermethylated mouse L929 cell DNA. DNA isolated from growing cells or tissues is a better substrate than DNA from normal liver or pancreas or from stationary cells
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
-
methylation of double-stranded Micrococcus luteus DNA. The enzyme transfers methyl groups to both double-stranded and single-stranded natural DNAs. The methyl-accepting activity of the DNA is correlated to their GC content, homologous DNAs are poor substrates. Very low rate of methylation with poly[(dA-dC)*(dG-dT)], highest methyl-accepting ability with poly[(dG-dC)*(dG-dC)]
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
-
the purified enzyme has at least a 30fold higher catalytic efficiency with hemimethylated double-stranded oligodeoxyribonucleotide substrates than unmethylated substrates and is most active with small oligodeoxyribonucleotide substrates
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
-
poly(dIdC:dIdC) is efficiently methylated
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
-
higher methylating activity with chemically synthesized hemimethylated oligodeoxynucleotide than with poly(dI*dC)*poly(dI*dC)
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?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
-
poly(dI*dC-dI*dC) of chain length 100, 500, 2000 or 5000 base pairs
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
-
specificity is confined to the sequence 5'-CpG-3'. Any sequence-specific de novo methylation mediated by Dnmt1 is either under the control of regulatory factors that interact
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
-
isoenzymes Dnmt3a, Dnmt3b1 and Dnmt3b2 show similar activity towards poly(dG-dC)-poly(dG-dC)
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?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
Dnmt1 plays an essential role in the faithful and efficient maintenance of methylation patterns in the mammalian genome
-
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
major enzyme in maintenance of the pattern of DNA methylation after DNA replication
-
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
the enzyme is a de novo-type DNA methyltransferase
-
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
methylates DNA processively with high preference for hemimethylated target sites. Dnmt1 methylates a hemimethylated 958-mer substrate in a highly processive reaction. Fully methylated and unmethylated CG sites do not inhibit processive methylation of the DNA. Unmethylated sites embedded in a hemimethylated context are modified at an approximately 24fold reduced rate. Completely unmodified DNA is methylated even more slowly. Dnmt1 is not able to methylate hemimethylated CG sites on different strands of the DNA in a processive manner, indicating that Dnmt1 keeps its orientation with respect to the DNA while methylating the CG sites on one strand of the DNA
-
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
P-19 cells possess catalytically active Dnmt1, Dnmt2, Dnmt3a and Dnmt3b. Dnmt1 and Dnmt3b have the greatest amount of methylation activity directed at the endogenous genome
-
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
poly(dGdC)-poly(dGdC) or poly(dIdC)-poly(dIdC)
-
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
preference for single stranded DNA substrates is increased up to 50fold by the presence of a proximal 5-methyl cytosine. This modulation is distance-dependent and is due to an enhanced binding affinity and minor changes in catalytic efficiency. No modulation of activity is observed with double stranded DNA
-
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
unmethylated DNA substrates: poly(dIdC)-poly(dIdC), poly(dGdC)-poly(dGdC) or a 520-bp DNA fragment from the p2HhaBsp. Full-length Dnmt1 methylates hemimethylated DNA with high processivity and a fidelity of over 95%, but unmethylated DNA with much less processivity. Dnmt1-(2911620), the truncated form of Dnmt1, shows identical properties to full-length Dnmt1 indicating that the N-terminal 290-amino acid residue region of Dnmt1 is not required for preferential activity toward hemimethylated sites or for processivity of the enzyme. Dnmt1 methylates hemimethylated CpG sites on one strand of double-stranded DNA during a single processive run
-
-
?
additional information
?
-
-
intrinsic sequence-specificity of Dnmt1 on linear duplex DNA is unlikely to be important in the establishment of genomic methylation patterns
-
-
?
additional information
?
-
-
the enzyme is essential for viable mammalian development and has a central function in the determination and maintenance of epigenetic methalation pattern
-
-
?
additional information
?
-
-
enzymatic DNA methylation of carbon 5 of cytosines is an epigenetic modification that plays a role in regulating gene expression, differentiation, and tumorigenesis. DNA (cytosine-C5)-methyltransferase-1 is the enzyme responsible for maintaining established methylation patterns during replication in mammalian cells
-
-
?
additional information
?
-
interactions between Dnmt3b and both Tdg and Mbd4, i.e. G/T mismatch-specific thymine-DNA glycosylase and methyl-CpG binding domain protein 4, two thymine glycosylases involved in reduction of the impact of 5mC deamination, that can both excise uracil or thymine at U-G and T-G mismatches to initiate base excision repair, overview. Interaction with Tdg via two separate Dnmt3b domains, but MTase motif I of the catalytic domain of Dnmt3b is sufficient for interaction with Tdg and Mbd4
-
-
?
additional information
?
-
-
upon activation of ER? target gene expression, CpG dinucleotides of promoters undergo cyclical demethylation and remethylation with a cycle time of roughly 2 h, cyclical recruitment of DNMT3A and DNMT3B DNA methyltransferases to the promoter regions of estrogen receptoralpha target genes. In cancer cells, DNMT3A and DNMT3B might posses deaminase activity and be involved in a dynamic demethylation-methylation pathway that operates during gene transcription, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
the enzyme is a de novo-type DNA methyltransferase
-
-
?
DNA + S-adenosyl-L-methionine
DNA containing 5-methylcytosine + S-adenosyl-L-homocysteine
-
-
-
-
?
DNA + S-adenosyl-L-methionine
DNA containing 5-methylcytosine + S-adenosyl-L-homocysteine
-
both DNMT3A and DNMT3B are involved in de novo DNA methylation. 5'-Cytosine methylation is a common epigenetic modification in eukaryotic genomes
-
-
?
DNA + S-adenosyl-L-methionine
DNA containing 5-methylcytosine + S-adenosyl-L-homocysteine
-
DNMT1 participates in epigenetic reprogramming through its ability to distinguish different categories of methylated sequences. Genomic imprinting is a mammalian epigenetic process that distinguishes maternal and paternal alleles to ensure parent-specific, monoallelic expression of imprinted genes. Preimplantation DNMT1-dependent maintenance mechanism specifically targets DMD sequences, e.g. of IAP, alpha-actin, Snurf/Snrpn, H19, Gnas, and Gtl2 DMD, overview
-
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
Dnmt1 plays an essential role in the faithful and efficient maintenance of methylation patterns in the mammalian genome
-
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
major enzyme in maintenance of the pattern of DNA methylation after DNA replication
-
-
?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
the enzyme is a de novo-type DNA methyltransferase
-
-
?
additional information
?
-
-
intrinsic sequence-specificity of Dnmt1 on linear duplex DNA is unlikely to be important in the establishment of genomic methylation patterns
-
-
?
additional information
?
-
-
the enzyme is essential for viable mammalian development and has a central function in the determination and maintenance of epigenetic methalation pattern
-
-
?
additional information
?
-
-
enzymatic DNA methylation of carbon 5 of cytosines is an epigenetic modification that plays a role in regulating gene expression, differentiation, and tumorigenesis. DNA (cytosine-C5)-methyltransferase-1 is the enzyme responsible for maintaining established methylation patterns during replication in mammalian cells
-
-
?
additional information
?
-
interactions between Dnmt3b and both Tdg and Mbd4, i.e. G/T mismatch-specific thymine-DNA glycosylase and methyl-CpG binding domain protein 4, two thymine glycosylases involved in reduction of the impact of 5mC deamination, that can both excise uracil or thymine at U-G and T-G mismatches to initiate base excision repair, overview. Interaction with Tdg via two separate Dnmt3b domains, but MTase motif I of the catalytic domain of Dnmt3b is sufficient for interaction with Tdg and Mbd4
-
-
?
additional information
?
-
-
upon activation of ER? target gene expression, CpG dinucleotides of promoters undergo cyclical demethylation and remethylation with a cycle time of roughly 2 h, cyclical recruitment of DNMT3A and DNMT3B DNA methyltransferases to the promoter regions of estrogen receptoralpha target genes. In cancer cells, DNMT3A and DNMT3B might posses deaminase activity and be involved in a dynamic demethylation-methylation pathway that operates during gene transcription, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
NaCl
-
incubation of native calf thymus DNA in presence of 40 mM NaCl results in 50% inhibition, more than 90% inhibition at 200 mM. With denatured calf thymus DNA, low concentrations of NaCl, up to 90 mM stimulate, 50% inhibition at 175 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NaCl
Dnmt3a, inhibits activity around physiological ionic strength
Nicotine
-
decreases glutamic acid decarboxylase 67 promoter methylation by DMT1 in GABAergic interneurons
NaCl
-
incubation of native calf thymus DNA in presence of 40 mM NaCl results in 50% inhibition, more than 90% inhibition at 200 mM. With denatured calf thymus DNA, low concentrations of NaCl, up to 90 mM stimulate, 50% inhibition at 175 mM
NaCl
Dnmt3b, inhibits activity around physiological ionic strength
additional information
Dnmt3a is fully active at physiological potassium concentration of K+
-
additional information
Dnmt3a is fully active at physiological potassium concentration of K+
-
additional information
-
Dnmt3a is fully active at physiological potassium concentration of K+
-
additional information
-
stimulating proteins from murine P815 mastocytoma cells stimulate both de novo and maintenance activity of DNA methyltransferase about 3fold. They enhance the methylation of any natural DNA and of poly[(dI-dC)*(dI-dC)] but inhibit methylation of poly[(dG-dC)*(dG-dC)]
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
DNA(cytosine-S)-methyltransferase 3-like protein
i.e. Dnmt3L, UniProt Acc Q09CWR8. Dnmt3L stimulates activity of the Dnmt3A by directly binding to the catalytic domain via its own C-terminal domain. The catalytic activity is stimulated about 15fold. Dnmt3L directly binds to DNA but not to S-adenosyl-L-methionine. Complex formation between Dnmt3A and Dnmt3L accelerates DNA binding by Dnmt3A 20fold and lowers its Km for DNA. Interaction of Dnmt3L with Dnmt3A increases the binding of AdoMet to Dnmt3A, and lowers the Km-value of Dnmt3A for AdoMet. Interaction of Dnmt3A and Dnmt3L is transient, and after DNA binding to Dnmt3A, Dnmt3L dissociates from the complex. Following dissociation of Dnmt3L, Dnmt3A adopts a closed conformation leading to slow rates of DNA release. Therefore, Dnmt3L acts as a substrate exchange factor that accelerates DNA and AdoMet binding
-
5-methyl cytosine
preference for single stranded DNA substrates is increased up to 50fold by the presence of a proximal 5-methyl cytosine. This modulation is distance-dependent and is due to an enhanced binding affinity and minor changes in catalytic efficiency. No modulation of activity is observed with double stranded DNA
DNA(cytosine-S)-methyltransferase 3-like protein
i.e. Dnmt3L, UniProt Acc Q09CWR8. Dnmt3L stimulates activity of Dnmt3B by directly binding to the catalytic domain via its own C-terminal domain. The catalytic activity is stimulated about 15fold. Dnmt3L directly binds to DNA but not to S-adenosyl-L-methionine. Dnmt3L acts as a substrate exchange factor that accelerates DNA and AdoMet binding
-
stimulating proteins
-
the proteins from murine P815 mastocytoma cells stimulate both de novo and maintenance activity of DNA methyltransferase about 3fold. They enhance the methylation of any natural DNA and of poly[(dI-dC)*(dI-dC)] but inhibit methylation of poly[(dG-dC)*(dG-dC)]
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00096
S-adenosyl-L-methionine
enzyme Dnmt3A, in presence of Dnmt3L
0.00255
S-adenosyl-L-methionine
enzyme Dnmt3A, in absence of Dnmt3L
0.0003
S-adenosyl-L-methionine
-
isoenzyme Dnmt3a, reaction with poly(dG-dC)-poly(dG-dC)
0.0004
S-adenosyl-L-methionine
-
isoenzyme Dnmt3a, reaction with poly(dI-dC)-poly(dI-dC)
0.0008
S-adenosyl-L-methionine
-
isoenzyme Dnmt3b2, reaction with poly(dG-dC)-poly(dG-dC)
0.0009
S-adenosyl-L-methionine
-
isoenzyme Dnmt3b2, reaction with poly(dI-dC)-poly(dI-dC)
0.0012
S-adenosyl-L-methionine
-
isoenzyme Dnmt3b1, reaction with poly(dI-dC)-poly(dI-dC) por poly(dG-dC)*poly(dG-dC)
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
turnover-numbers for hybrid enzymes
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
an asynchronously proliferating population of carcinoma cells
-
the somatic form of Dnmt1 is present in association with chromatin in MII-stage oocytes as well as in the nucleus throughout preimplantation development. At the early one-cell stage, somatic Dnmt1 is asymmetrically localized in the maternal pronuclei. Thereafter, somatic Dnmt1 is recruited to the paternal genome during pronuclear maturation. During the first two cell cycles after fertilization, Dnmt1s is exported from the nucleus in the G2 phase in a CRM1/exportin-dependent manner
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the somatic form of Dnmt1 is present in association with chromatin in MII-stage oocytes as well as in the nucleus throughout preimplantation development. At the early one-cell stage, somatic Dnmt1 is asymmetrically localized in the maternal pronuclei. Thereafter, somatic Dnmt1 is recruited to the paternal genome during pronuclear maturation. During the first two cell cycles after fertilization, Dnmt1s is exported from the nucleus in the G2 phase in a CRM1/exportin-dependent manner
both Tdg and Dnmt3b are colocalized to heterochromatin
-
the somatic form of Dnmt1 is present in association with chromatin in MII-stage oocytes as well as in the nucleus throughout preimplantation development. At the early one-cell stage, somatic Dnmt1 is asymmetrically localized in the maternal pronuclei. Thereafter, somatic Dnmt1 is recruited to the paternal genome during pronuclear maturation. During the first two cell cycles after fertilization, Dnmt1s is exported from the nucleus in the G2 phase in a CRM1/exportin-dependent manner
-
the somatic form of Dnmt1 is present in association with chromatin in MII-stage oocytes as well as in the nucleus throughout preimplantation development. At the early one-cell stage, somatic Dnmt1 is asymmetrically localized in the maternal pronuclei. Thereafter, somatic Dnmt1 is recruited to the paternal genome during pronuclear maturation. During the first two cell cycles after fertilization, Dnmt1s is exported from the nucleus in the G2 phase in a CRM1/exportin-dependent manner
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
DNA methylation at cytosine residues in CpG dinucleotides is a component of epigenetic marks crucial to mammalian development, maintenance of genomic methylation patterns during preimplantation development requires the somatic form of DNA methyltransferase 1
physiological function
-
DNMT1 cytosine methyltransferase governs maintenance methylation in mammals, rearrangements of non-DMD, but not DMD methylation in preimplantation embryos
physiological function
NSun2 is essential for germ cell differentiation in the mouse testis. In NSun2-depleted testes, genes encoding Ddx4, Miwi, and Tudor domain-containing proteins are repressed. Loss of NSun2 specifically blocks meiotic progression of germ cells into the pachytene stage. The same phenotype is observed when NSun2 and Dnmt2, the only other cytosine-5 RNA methyltransferase characterized to date, are deleted simultaneously. Specific NSun2- and Dnmt2-methylated tRNAs decrease in abundance when both methyltransferases are deleted
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DNM3A_MOUSE
908
0
101672
Swiss-Prot
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
190000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the apparent molecular weights of the GST-fused Dnmt3a, Dnmt3b1 and Dnmt3b2 are 130000 Da, 120000 Da and 115000 Da, as determined by SDS-PAGE
additional information
Dnmt3b is composed of multiple domains. The C-terminus contains the catalytic domain which harbors conserved C-5 DNA methyltransferase motif that are necessary for catalyzing methyl transfer from the cofactor S-adenosyl-L-methionine to the target cytosine. The N-terminus contains a PWWP domain and an ATRX-like domain, so called because it shares homology with the alpha-thalassemia/mental retardation syndrome, X-linked, i.e. ATRX, protein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A609T
naturally occuring mutation causing recessive genetic disorder, ICF syndrome, the mutation does not affect the association of Dnmt3b with Mbd4 or Tdg
S277P
naturally occuring mutation causing recessive genetic disorder, ICF syndrome, the mutation does not affect the association of Dnmt3b with Mbd4 or Tdg
V612A
naturally occuring mutation causing recessive genetic disorder, ICF syndrome, the mutation does not affect the association of Dnmt3b with Mbd4 or Tdg
additional information
additional information
-
construction of Dnmt1 mutants, two alleles of the endogenous Dnmt1 locus of R1 embryonic stem cells are sequentially modified using two similar targeting vectors to generate the DOX-OFF Dnmt1tet/tet cell line. The isolated 5' portion of the mouse Dnmt1 gene is used for targeted mutagenesis. Transient absence of DNMT1 expression leads to loss of imprinted methylation. In an embryonic stem cell line endogenous DNMT1s expression is extinguished by the addition of doxycycline, phenotypes, overview
additional information
construction of several Xpress-tagged Dnmt3b C-terminal truncation mutants, Dnmt3b mutants possessing the conserved MTase motifs VI, IV or I are all capable of binding Tdg, while removal of the entire catalytic domain of Dnmt3b disrupts its interaction with Tdg. Deletion of both putative interaction regions, PWWP and I, from Dnmt3b eliminates the binding ability. Reduction of T·G mismatch repair efficiency upon loss of DNA methyltransferase expression
additional information
-
even modest increases or decreases in levels of m5C cause severe abnormalities or death in mutant mice
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant forms of full-length Dnmt1 and a truncated form of Dnmt1-(2911620) lacking the binding sites for PCNA and DNA
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
construction of three hybrid methyltransferases, containing the intact N-terminus of the murine Dnmt1 and most of the coding sequences from M.HhaI (GCGC), M.HpaII (CCGG) or M.SssI (CG). The hybrids are biologically active when expressed in a baculovirus system and show the specificity of the parental C-terminal domain
-
DNA (cytosine C5) methyltransferase-1, fused to an amino-terminal hexahistidine tag, is expressed by infecting Spodoptera frugiperda cells for 46 h with a recombinant baculovirus carrying the DNA (cytosine-C5)methyltransferase-1 cDNA
-
DNMT1, DNA and amino acid sequence determination and analysis, expression of wild-type and mutants in Escherichia coli
-
somatic Dnmt1 from liver, expression analysis of somatic and oocyte Dnmt1, recombinant expression in NIH3T3 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
nicotine decreases DNA methyltransferase 1 expression in in cortical and hippocampal but not in striatal GABAergic interneurons, while DNMT1 mRNA content in the liver fails to change after nicotine treatment, overview. Mecamylamine but not hexamethonium blocks nicotine-induced downregulation of DNMT1 expression. The downregulation proceeds via selective stimulation of nicotinic acetylcholine receptor, nAChR, overview
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Turnbull, J.F.; Adams, R.L.P.
DNA methylase: purification from ascites cells and the effect of various DNA substrates on its activity
Nucleic Acids Res.
3
677-695
1976
Mus musculus
Tomassetti, A.; Driever, P.H.; Pfeifer, G.P.; Drahovsky, D.
Isolation and characterization of proteins that stimulate the activity of mammalian DNA methyltransferase
Biochim. Biophys. Acta
951
201-212
1988
Mus musculus
Pfeifer, G.P.; Grunwald, S.; Palitti, F.; Kaul, S.; Boehm, T.L.J.; Hirth, H.P.; Drahovsky, D.
Purification and characterization of mammalian DNA methyltransferases by use of monoclonal antibodies
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260
13787-13793
1985
Homo sapiens, Mus musculus
Brank, A.S.; Van Bemmel, D.M.; Christman, J.K.
Optimization of baculovirus-mediated expression and purification of hexahistidine-tagged murine DNA (cytosine-C5)-methyltransferase-1 in Spodoptera frugiperda 9 cells
Protein Expr. Purif.
25
31-40
2002
Mus musculus
Pradhan, S.; Roberts, R.J.
Hybrid mouse-prokaryotic DNA (cytosine-5) methyltransferases retain the specificity of the parental C-terminal domain
EMBO J.
19
2103-2114
2000
Mus musculus
Tollefsbol, T.O.; Hutchison, C.A.
Mammalian DNA (cytosine-5-)-methyltransferase expressed in Escherichia coli, purified and characterized
J. Biol. Chem.
270
18543-18550
1995
Mus musculus
Flynn, J.; Reich, N.
Murine DNA (cytosine-5-)methyltransferase: steady-state and substrate trapping analyses of the kinetic mechanism
Biochemistry
37
15162-15169
1989
Mus musculus
Yoder, J.A.; Soman, N.S.; Verdine, G.L.; Bestor, T.H.
DNA (cytosine-5)-methyltransferases in mouse cells and tissues. Studies with a mechanism-based probe
J. Mol. Biol.
270
385-395
1997
Mus musculus
Aoki, A.; Suetake, I.; Miyagawa, J.; Fujio, T.; Chijiwa, T.; Sasaki, H.; Tajima, S.
Enzymatic properties of de novo-type mouse DNA (cytosine-5) methyltransferases
Nucleic Acids Res.
29
3506-3512
2001
Mus musculus
Aubol, B.E.; Reich, N.O.
Murine DNA cytosine C(5)-methyltransferase: in vitro studies of de novo methylation spreading
Biochem. Biophys. Res. Commun.
310
209-214
2003
Spirulina sp., Mus musculus (P13864), Mus musculus, Spirulina sp. MW-1
Suetake, I.; Miyazaki, J.; Murakami, C.; Takeshima, H.; Tajima, S.
Distinct enzymatic properties of recombinant mouse DNA methyltransferases Dnmt3a and Dnmt3b
J. Biochem.
133
737-744
2003
Mus musculus (O88508), Mus musculus (O88509), Mus musculus
Hermann, A.; Goyal, R.; Jeltsch, A.
The Dnmt1 DNA-(cytosine-C5)-methyltransferase methylates DNA processively with high preference for hemimethylated target sites
J. Biol. Chem.
279
48350-48359
2004
Mus musculus (P13864)
Gowher, H.; Liebert, K.; Hermann, A.; Xu, G.; Jeltsch, A.
Mechanism of stimulation of catalytic activity of Dnmt3A and Dnmt3B DNA-(cytosine-C5)-methyltransferases by Dnmt3L
J. Biol. Chem.
280
13341-13348
2005
Mus musculus (O88508), Mus musculus (O88509)
Vilkaitis, G.; Suetake, I.; Klimasauskas, S.; Tajima, S.
Processive methylation of hemimethylated CpG sites by mouse Dnmt1 DNA methyltransferase
J. Biol. Chem.
280
64-72
2005
Mus musculus (P13864), Mus musculus
Datta, J.; Ghoshal, K.; Sharma, S.M.; Tajima, S.; Jacob, S.T.
Biochemical fractionation reveals association of DNA methyltransferase (Dnmt) 3b with Dnmt1 and that of Dnmt 3a with a histone H3 methyltransferase and Hdac1
J. Cell. Biochem.
88
855-864
2003
Mus musculus (O88508), Mus musculus (O88509), Mus musculus
Liu, K.; Wang, Y.F.; Cantemir, C.; Muller, M.T.
Endogenous assays of DNA methyltransferases: Evidence for differential activities of DNMT1, DNMT2, and DNMT3 in mammalian cells in vivo
Mol. Cell. Biol.
23
2709-2719
2003
Mus musculus (O55055), Mus musculus (O88508), Mus musculus (O88509), Mus musculus (P13864), Mus musculus
Satta, R.; Maloku, E.; Zhubi, A.; Pibiri, F.; Hajos, M.; Costa, E.; Guidotti, A.
Nicotine decreases DNA methyltransferase 1 expression and glutamic acid decarboxylase 67 promoter methylation in GABAergic interneurons
Proc. Natl. Acad. Sci. USA
105
16356-16361
2008
Mus musculus
Ooi, S.K.; Bestor, T.H.
The colorful history of active DNA demethylation
Cell
133
1145-1148
2008
Homo sapiens, Mus musculus
Kurihara, Y.; Kawamura, Y.; Uchijima, Y.; Amamo, T.; Kobayashi, H.; Asano, T.; Kurihara, H.
Maintenance of genomic methylation patterns during preimplantation development requires the somatic form of DNA methyltransferase 1
Dev. Biol.
313
335-346
2008
Mus musculus
Boland, M.J.; Christman, J.K.
Characterization of Dnmt3b:thymine-DNA glycosylase interaction and stimulation of thymine glycosylase-mediated repair by DNA methyltransferase(s) and RNA
J. Mol. Biol.
379
492-504
2008
Mus musculus (O88509)
Borowczyk, E.; Mohan, K.N.; DAiuto, L.; Cirio, M.C.; Chaillet, J.R.
Identification of a region of the DNMT1 methyltransferase that regulates the maintenance of genomic imprints
Proc. Natl. Acad. Sci. USA
106
20806-20811
2009
Mus musculus
Hussain, S.; Tuorto, F.; Menon, S.; Blanco, S.; Cox, C.; Flores, J.V.; Watt, S.; Kudo, N.R.; Lyko, F.; Frye, M.
The mouse cytosine-5 RNA methyltransferase NSun2 is a component of the chromatoid body and required for testis differentiation
Mol. Cell. Biol.
33
1561-1570
2013
Mus musculus (Q1HFZ0), Mus musculus
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