Information on EC 2.1.1.113 - site-specific DNA-methyltransferase (cytosine-N4-specific)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.113
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RECOMMENDED NAME
GeneOntology No.
site-specific DNA-methyltransferase (cytosine-N4-specific)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + DNA cytosine = S-adenosyl-L-homocysteine + DNA N4-methylcytosine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
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CAS REGISTRY NUMBER
COMMENTARY hide
169592-50-1
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90371-46-3
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92228-39-2
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98982-80-0
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99637-25-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
enzyme M.AvaI
SwissProt
Manually annotated by BRENDA team
strain H
SwissProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
M.BcnIA and M.BcnIB
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-
Manually annotated by BRENDA team
strain A with enzyme M.CsyAIP
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Manually annotated by BRENDA team
strain B with enzyme M.CsyBIP
SwissProt
Manually annotated by BRENDA team
strain 4111, plasmid pZE8
SwissProt
Manually annotated by BRENDA team
enzyme M.BalI
SwissProt
Manually annotated by BRENDA team
strain JN2091, enzyme M.BsoBI
SwissProt
Manually annotated by BRENDA team
enzyme M.NcoI
SwissProt
Manually annotated by BRENDA team
enzyme M.PhiHII
SwissProt
Manually annotated by BRENDA team
strain 26695 with the enzyme M.HpyAIIP; strain 26695 with the enzyme M.HpyAXIIBP
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Manually annotated by BRENDA team
enzyme M.PhiGIP
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Manually annotated by BRENDA team
enzyme M.MjaIP; enzyme M.MjaV
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Manually annotated by BRENDA team
strain Z-250, enzyme M.MthZI
SwissProt
Manually annotated by BRENDA team
strain Z-250, enzyme M.MthZI
SwissProt
Manually annotated by BRENDA team
enzyme M.MwoI
SwissProt
Manually annotated by BRENDA team
strain ATCC 10900, gene mboIIR
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Manually annotated by BRENDA team
strain ATCC 14688, gene ncuIM2
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Manually annotated by BRENDA team
strain ME11, enzyme M.NgoMXV
SwissProt
Manually annotated by BRENDA team
strain ME11, enzyme M.NgoMXV
SwissProt
Manually annotated by BRENDA team
strain NCIB 986, enzyme M.Pac25I
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Manually annotated by BRENDA team
strain NCIB 986, enzyme M.Pac25I
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Manually annotated by BRENDA team
strain OT3, enzyme M.PhoIIIP
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Manually annotated by BRENDA team
strain OT3, enzyme M.PhoIIIP
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Manually annotated by BRENDA team
strain GI-H, enzyme M.PspGI
SwissProt
Manually annotated by BRENDA team
enzymes M.SapIA and M.SapIB
SwissProt
Manually annotated by BRENDA team
strain CT18, enzyme M.StyCIP
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-
Manually annotated by BRENDA team
strain CT18, enzyme M.StyCIP
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Manually annotated by BRENDA team
enzyme M.SmaI
SwissProt
Manually annotated by BRENDA team
enzyme M. ScaI
SwissProt
Manually annotated by BRENDA team
enzyme M.SfiI
SwissProt
Manually annotated by BRENDA team
pv. vesicatoria, strains Xcv7-1, Xv2 and Xv64 and ATCC 35937 strain
SwissProt
Manually annotated by BRENDA team
enzyme M.XcyI
SwissProt
Manually annotated by BRENDA team
enzyme M.XmaI
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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 cytosine
S-adenosyl-L-homocysteine + DNA N4-methylcytosine
show the reaction diagram
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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 + DNA cytosine
S-adenosyl-L-homocysteine + DNA N4-methylcytosine
show the reaction diagram
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
show the reaction diagram
additional information
?
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the enzyme also displays promiscuous activity catalyzing methylation of adenine at the N6 position in DNA
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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stimulates
Mg2+
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stimulates
additional information
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the enzyme's catalytic activity is strongly stimulated by addition of Ca2+ or Mg2+, but not by Mn2+, Co2+ or Cd2+, however, divalent metal ions are not required for its base-flipping activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-homocysteine
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competitive with regard to S-adenosylmethionine and non-competitive with respect to unmethylated 20-mer duplex
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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the enzyme's catalytic activity is strongly stimulated by addition of Ca2+ or Mg2+, but not by Mn2+, Co2+ or Cd2+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00035
5'-CAGTTTAGGATCCATTTCAC-3'/3'-GTCAAATCCTAGGTAAAAGAG-5'
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0.000196
5'-GTGAAAT*GGATCC*TAAACTG-3'/3'-CACTTTA*CCTAGG*ATTTGAC-5'
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0.00122 - 0.0016
S-adenosyl-L-methionine
additional information
additional information
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Km-values for several oligonucleotides
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4
Ca2+
Moraxella bovis
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pH 7.0, 37C, recombinant enzyme
5
Mg2+
Moraxella bovis
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pH 7.0, 37C, recombinant enzyme
0.4
Mn2+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
genetic organization of novel restriction-modification (R-M) system, tail-to-tail gene orientation with 12 base pairs overlapping, protection and activity assays, classified as member of beta-class of m4C-methyltransferases, predicted amino acid sequence reveals 41.9% identity with SmaI, no SmaI-like restriction activity in cell extracts of the Xcv7-1 strain
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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assay at
7.9
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18300
truncated protein predicted due to translation termination codon in the open reading frame
337000
299-amino acid protein, predicted by sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
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enzyme in a free state exists as a dimer. Introduction of substoichiometric amounts of DNA into the reaction mixture results in pronounced multimerization of the enzyme. However, addition of SAM in saturating concentration at an excess of the oligonucleotide duplex over BamHI Mtase converts most of the enzyme into a monomeric state
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
determination of the structure of PvuII methyltransferase complexed with S-adenosyl-L-methionine by multiwavelength anomalous diffraction using a crystal of the selenomethionine substituted protein
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native and selenomethionyl M.PvuII crystallized separately as binary complexs of the methyl donor S-adenosyl-L-methionine in the monoclinic space group P2. Hanging-drop vapor-diffusion technique
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gel filtration, recombinant protein for in vitro methyltransferase activity assay
native and selenomethionyl M.PvuII
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Ni-NTA column chromatography
purified from E. coli cells expressing the genes for M.BcnIA and M.BcnIB
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recombinant M2.MboII 3.6fold to electrophoretic homogeneity using a four-step chromatographic procedure, involving adsorption and hydroxylapatite chromatography followed by hydroophobic interaction and heparin affinity chromatography, from Escherichia coli
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recombinant M2.NcuI 3.6fold to electrophoretic homogeneity using a four-step chromatographic procedure, involving adsorption and hydroxylapatite chromatography followed by hydrophobic interaction and heparin affinity chromatography, from Escherichia coli
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recombinant wild-type enzyme from Escherichia coli by adsorption chromatography and dialysis to homogeneity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21-CodonPlus(DE3)-RIPL cells
expressed in Escherichia coli ER2796 cells
gene mboIIR, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli using the constitutive promoter, PtetA
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gene ncuIM2, DNA and amino acid sequence determination and analysis, expression in Escherichia coli
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obtained from genomic library, amplified in Escherichia coli XL1-Blue, strain ER2566 for expression of the M.XveII carrying a C-terminal His6-tag
overexpression in Escherichia coli DH10B
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recombinant expression of wild-type enzyme in Escherichia coli
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Show AA Sequence (613 entries)
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