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Information on EC 2.1.1.37 - DNA (cytosine-5-)-methyltransferase and Organism(s) Haemophilus aegyptius and UniProt Accession P20589

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EC Tree
     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.37 DNA (cytosine-5-)-methyltransferase
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Select one or more organisms in this record: ?
This record set is specific for:
Haemophilus aegyptius
UNIPROT: P20589 not found.
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Word Map
The taxonomic range for the selected organisms is: Haemophilus aegyptius
The enzyme appears in selected viruses and cellular organisms
Synonyms
dnmt1, dnmt3a, dna methyltransferase, dnmt3b, dna methyltransferase 1, dnmt2, dna mtase, nsun2, dna methylase, dna methyltransferase 3a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C5-MTase
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cytosine 5-methyltransferase
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cytosine DNA methylase
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cytosine DNA methyltransferase
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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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-
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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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DNA cytosine c5 methylase
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DNA cytosine methylase
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DNA methylase
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DNA methyltransferase
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DNA transmethylase
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DNA-cytosine 5-methylase
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DNA-cytosine methyltransferase
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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 TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:DNA (cytosine-5-)-methyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9037-42-7
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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 + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
show the reaction diagram
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-
-
?
S-adenosyl-L-methionine + unmethylated 30-mer DNA containing cytosine
S-adenosyl-L-homocysteine + unmethylated 30-mer DNA containing 5-methylcytosine
show the reaction diagram
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-
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?
S-adenosyl-L-methionine + DNA
S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
show the reaction diagram
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?
additional information
?
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enzyme induces DNA bending, a mechanism to establish specific interface between proteins and DNA. Enzymes recognizing a cytosine 3' to the target cytosine tend to induce greater bends than enzymes with guanine in this position
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
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enzyme induces DNA bending, a mechanism to establish specific interface between proteins and DNA. Enzymes recognizing a cytosine 3' to the target cytosine tend to induce greater bends than enzymes with guanine in this position
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5'-(3-aminopropylthio)-5'-deoxyadenosine
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5'-(3-carboxypropylthio)-5'-deoxyadenosine
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S-(2'-deoxy-b -D-ribofuranosyladenosin-5'-yl)-L-homocysteine
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S-(N6-benzoyladenosin-5'-yl)-L-homocysteine
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S-adenosin-5'-yl-L-homocysteine methylamide
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S-adenosyl-L-homocysteine
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S-cytid-5'-yl-L-homocysteine
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S-inosin-5'-yl-L-homocysteine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00028
S-adenosyl-L-methionine
pH 8.5, 37°C
0.0000037
unmethylated 30-mer DNA containing cytosine
pH 8.5, 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0068
S-adenosyl-L-methionine
pH 8.5, 37°C
0.0068
unmethylated 30-mer DNA containing cytosine
pH 8.5, 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.037
5'-(3-aminopropylthio)-5'-deoxyadenosine
pH 8.5, 37°C
0.23
5'-(3-carboxypropylthio)-5'-deoxyadenosine
pH 8.5, 37°C
0.069
S-(2'-deoxy-b -D-ribofuranosyladenosin-5'-yl)-L-homocysteine
pH 8.5, 37°C
0.032
S-(N6 -benzoyladenosin-5'-yl)-L-homocysteine
pH 8.5, 37°C
0.29
S-adenosin-5'-yl-L-homocysteine methylamide
pH 8.5, 37°C
0.000069
S-adenosyl-L-homocysteine
pH 8.5, 37°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MTH3_HAEAE
330
0
37686
Swiss-Prot
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rasko, T.; Finta, C.; Kiss, A.
DNA bending induced by DNA (cytosine-5) methyltransferases
Nucleic Acids Res.
28
3083-3091
2000
Lysinibacillus sphaericus, Haemophilus aegyptius, Haemophilus haemolyticus, Haemophilus parainfluenzae, Staphylococcus aureus, Salmonella enterica subsp. enterica serovar Infantis
Manually annotated by BRENDA team
Cohen, H.M.; Griffiths, A.D.; Tawfik, D.S.; Loakes, D.
Determinants of cofactor binding to DNA methyltransferases: insights from a systematic series of structural variants of S-adenosylhomocysteine
Org. Biomol. Chem.
3
152-161
2005
Haemophilus parahaemolyticus (P05102), Haemophilus aegyptius (P20589)
Manually annotated by BRENDA team