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S-adenosyl-L-methionine + (CGG*CCG)73 oligodeoxynucleotide duplexes 5'-GATC/5'-GATC
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Tequatrovirus T4
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S-adenosyl-L-methionine + adenine in DNA
S-adenosyl-L-homocysteine + DNA containing N6-methyladenine
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the enzyme specifically binds double-stranded DNA
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S-adenosyl-L-methionine + adenine in DNA
S-adenosyl-L-homocysteine + N6-methyladenine in DNA
S-adenosyl-L-methionine + adenine in T4 gt- dam- DNA
S-adenosyl-L-homocysteine + N6-methyladenine in T4 gt- dam- DNA
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
S-adenosyl-L-methionine + DNA duplex carrying the 5'-AAGCUU-3'/3'-TTCGAA-5' target sequence
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S-adenosyl-L-methionine + double stranded DNA adenine
S-adenosyl-L-homocysteine + double stranded DNA 6-methyladenine
S-adenosyl-L-methionine + Int1 DNA
S-adenosyl-L-homocysteine + Int1 DNA containing N6-methyladenine
S-adenosyl-L-methionine + lambda phage DNA
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S-adenosyl-L-methionine + mRNA
S-adenosyl-L-homocysteine + mRNA containing N6-methyladenine
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S-adenosyl-L-methionine + oligodeoxynucleotide duplexes
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Tequatrovirus T4
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substrate contains one single specific recognition site as 5'-GATC/5'-GATC, or modified variants
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S-adenosyl-L-methionine + pUC19 DNA adenine
S-adenosyl-L-homocysteine + pUC19 DNA 6-methyladenine
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S-adenosyl-L-methionine + RNA/DNA heteroduplex carrying the 5'-AAGCUU-3'/3'-TTCGAA-5' target sequence
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S-adenosyl-L-methionine + single stranded DNA adenine
S-adenosyl-L-homocysteine + single stranded DNA 6-methyladenine
S-adenosyl-L-methionine + T7 DNA adenine
S-adenosyl-L-homocysteine + T7 DNA 6-methyladenine
S-adenosyl-L-methionine + T7 phage DNA
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additional information
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S-adenosyl-L-methionine + adenine in DNA
S-adenosyl-L-homocysteine + N6-methyladenine in DNA
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S-adenosyl-L-methionine + adenine in DNA
S-adenosyl-L-homocysteine + N6-methyladenine in DNA
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S-adenosyl-L-methionine + adenine in DNA
S-adenosyl-L-homocysteine + N6-methyladenine in DNA
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S-adenosyl-L-methionine + adenine in DNA
S-adenosyl-L-homocysteine + N6-methyladenine in DNA
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S-adenosyl-L-methionine + adenine in DNA
S-adenosyl-L-homocysteine + N6-methyladenine in DNA
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S-adenosyl-L-methionine + adenine in DNA
S-adenosyl-L-homocysteine + N6-methyladenine in DNA
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r
S-adenosyl-L-methionine + adenine in T4 gt- dam- DNA
S-adenosyl-L-homocysteine + N6-methyladenine in T4 gt- dam- DNA
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S-adenosyl-L-methionine + adenine in T4 gt- dam- DNA
S-adenosyl-L-homocysteine + N6-methyladenine in T4 gt- dam- DNA
Tequatrovirus T4
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the DNA target sequence is GATC, the natural substrate for the enzyme is hemimethylated DNA, where one strand is methylated and the other is not
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the DNA target sequence is GATC, the natural substrate for the enzyme is hemimethylated DNA, where one strand is methylated and the other is not
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the sams1 gene is methylated at an internal adenine residue of GATC site in symbiont-bearing amoebae but not in symbiont-free amoebae, suggesting that the modification may have caused the inactivation of sams1 at the transcriptional level
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the sams1 gene is methylated at an internal adenine residue of GATC site in symbiont-bearing amoebae but not in symbiont-free amoebae, suggesting that the modification may have caused the inactivation of sams1 at the transcriptional level
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the DNA target sequence is GANTC
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the DNA target sequence is GATC, the natural substrate for the enzyme is hemimethylated DNA, where one strand is methylated and the other is not
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the DNA target sequence is GANTC, CcrM is more active on hemimethylated than unmethylated DNA
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the target sequence is 5'GATC3'
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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129-mer DNA or pUC19 DNA are used as substrates
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
the enzyme methylates the adenine of hemimethylated GANTC after replication
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Dam catalyzes the methylation of N-6 of the adenine residue in GATC sequences
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Dam catalyzes the methylation of N-6 of the adenine residue in GATC sequences
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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Dam belongs to the alpha-class of adenine methyltransferases and transfers a methyl group to the N-6 position of the adenine in the DNA sequence 5'-GATC-3'
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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Dam methylates a GATC recognition site
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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Dam methylates the adenine residue in GATC sites
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Dam methylates the N-6 position of adenine in the DNA sequence 5'-GATC-3' and is highly processive, catalyzing multiple methyltransfers prior to dissociating from the DNA
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Dam methylates the N-6 position of the adenine in the sequence 5'-GATC-3', Dam shows a dramatic preference for the in vitro methylation of certain GATC sequences in plasmids and PCR-derived DNAfragments
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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DNA adenine methyltransferase methylates the N6 positions of adenines in the sequence 5'-GATC-3'
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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EcoP15I MTase adds a methyl group to the second adenine in the recognition sequence 5'-CAGCAG-3' in the presence of S-adenosyl-L-methionine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the DNA target sequence is GATC, the natural substrate for the enzyme is hemimethylated DNA, where one strand is methylated and the other is not
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the target sequence is 5'GATC3'
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the wild type enzyme shows target specificity for GATC sites
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the EcoRV DNA methyltransferase methylates the first adenine in the GATATC recognition sequence
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the enzyme methylates adenines at the N6 position of palindromic 5-GATC-3 sites. The enzyme ethylates both strands of the same site prior to fully dissociating from the DNA, a process referred to as intrasite processivity. Intrasite processivity is disrupted when the DNA flanking a single GATC site is longer than 400 bp on either side. The introduction of a second GATC site within this flanking DNA reinstates intrasite methylation of both sites
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the enzyme recognizes the palindromic specific sequence 5'-AAGCTT-3' and catalyzes formation of N6-methyladenine at the first A-residue. The enzyme prefers DNA containing a hemimethylated target site
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the enzyme recognizes the palindromic specific sequence 5'-AAGCTT-3' and catalyzes formation of N6-methyladenine at the first A-residue. The enzyme prefers DNA containing a hemimethylated target site
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the enzyme modifies adenine in the nickase recognition site 5'-GAGTC-3' and is specific for 5'-GASTC-3' substrates
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the enzyme modifies adenine in the nickase recognition site 5'-GAGTC-3' and is specific for 5'-GASTC-3' substrates
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the Hin1523 protein causes the methylation of 29.6% of the adenines in lambda DNA
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the enzyme recognizes the palindromic specific sequence 5'-AAGCTT-3' and catalyzes formation of N6-methyladenine at the first A-residue. The enzyme prefers DNA containing a hemimethylated target site
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
the Hia5 protein causes the methylation of 61% of the adenines in lambda DNA
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
the Hia5 protein causes the methylation of 61% of the adenines in lambda DNA
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the enzyme recognizes the palindromic specific sequence 5'-AAGCTT-3' and catalyzes formation of N6-methyladenine at the first A-residue. The enzyme prefers DNA containing a hemimethylated target site
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the Hin1523 protein causes the methylation of 29.6% of the adenines in lambda DNA
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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M.HpyAXII targets GTAC sites
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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duplex 2 DNA, 5'-GCAG-3' is the recognition site for the enzyme
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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HP0050 methyltransferase methylates one adenine at a time in the sequence 5'-GAAG-3'
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the enzyme recognizes the sequences of 5'-GAGG-3', 5'-GGAG-3' or 5'-GAAG-3'
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the enzyme recognizes the sequences of 5'-GAGG-3', 5'-GGAG-3' or 5'-GAAG-3'
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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M.HpyAXII targets GTAC sites
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the enzyme complex is active on single-stranded and unpaired DNA in vitro and methylates GGACT in single-strand DNA and double-strand DNA-containing mismatches
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the DNA target sequence is GATC, the natural substrate for the enzyme is hemimethylated DNA, where one strand is methylated and the other is not
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the enzyme recognizes the palindromic specific sequence 5'-AAGCTT-3' and catalyzes formation of N6-methyladenine at the first A-residue. The enzyme prefers DNA containing a hemimethylated target site
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the enzyme recognizes the palindromic specific sequence 5'-AAGCTT-3' and catalyzes formation of N6-methyladenine at the first A-residue. The enzyme prefers DNA containing a hemimethylated target site
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Marinobacter nauticus
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
MmeI modifies only the adenine in the top strand, 5-TCCRAC-3, MmeI endonuclease activity is blocked by this top strand adenine methylation and is unaffected by methylation of the adenine in the complementary strand, 5-GTYGGA-3'
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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M1.MboII modifies the last adenine in the recognition sequence 5'-GAAGA-3' to N6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the specific sequence recognized by M.NgoAXP is 5'-CCACC-3', in which the adenine residue is methylated
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the specific sequence recognized by M.NgoAXP is 5'-CCACC-3', in which the adenine residue is methylated
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the enzyme consists of two MT-A70 proteins and two homeobox-like DNA-binding proteins and specifically methylates ApT dinucleotides in double stranded DNA. The enzyme activity is 3-3.5fold higher on hemimethylated substrates, relative to unmethylated double stranded DNA
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the enzyme consists of two MT-A70 proteins and two homeobox-like DNA-binding proteins and specifically methylates ApT dinucleotides in double stranded DNA. The enzyme activity is 3-3.5fold higher on hemimethylated substrates, relative to unmethylated double stranded DNA
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the DNA target sequence is GATC, the natural substrate for the enzyme is hemimethylated DNA, where one strand is methylated and the other is not
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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Dam catalyzes postreplicative methylation of adenosine moieties located in 5'-GATC-3' sites
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the DNA target sequence is GATC, the natural substrate for the enzyme is hemimethylated DNA, where one strand is methylated and the other is not
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the target sequence is 5'GATC3'
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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recognition sequence GATC
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Tequatrovirus T4
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the enzyme consists of two MT-A70 proteins and two homeobox-like DNA-binding proteins and specifically methylates ApT dinucleotides in double stranded DNA. The enzyme activity is 3-3.5fold higher on hemimethylated substrates, relative to unmethylated double stranded DNA
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the enzyme consists of two MT-A70 proteins and two homeobox-like DNA-binding proteins and specifically methylates ApT dinucleotides in double stranded DNA. The enzyme activity is 3-3.5fold higher on hemimethylated substrates, relative to unmethylated double stranded DNA
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the DNA target sequence is GATC, the natural substrate for the enzyme is hemimethylated DNA, where one strand is methylated and the other is not
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the DNA target sequence is GATC, the natural substrate for the enzyme is hemimethylated DNA, where one strand is methylated and the other is not
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the target sequence is 5'GATC3'
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme preferentially binds DNA before S-adenosylmethionine. S-Adenosylhomocysteine is preferentially released from the enzyme before fully methylated DNA. Binding of both substrates and methylation occurs first in a rapid step followed by regeneration of enzyme in a second rate-limiting step
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme is involved in cell cycle regulation of Caulobacter crescentus
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
a biotinylated double stranded 23mer oligodeoxynucleotide with one hemimethylated GANTC site is used as substrate
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
substrate and product binding site structures
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
canonical 14mers and various substituted duplexes. Non-selfcomplementary tetradecamer duplex d[GCCGGATCTAGACG]*d[CGTCTAGATCCGGC] containing the hemimethylated GATC target sequence on one or the other strand and modifications in the GATC target sequence of the complementary strands. Large differences in DNA methylation of duplexes containing single dI or dG substitutions of the Dam recognition site are observed compared with the canonical substrate, if the substitution involves the top strand, on the G-C rich side. Substitution in either strand by uracil or 5-ethyluracil result in small perturbation of the methylation patterns. When 2,6-diamino-purine replaces the adenine to be methylated, small but significant methylation is observed
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
non-self-complementary tetradecanucleotide duplexes that contain the GATC target sequence. The enzyme is rather tolerant to base modification, binding of the enzyme is inversely proportional to the thermodynamic stability of the duplex in the ternary complex
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
methylation of DNA in a sequence specific manner, low substrate specificity with respect to the target base. Cytosine residues can be methylated if they are located in a C:T mismatch base pair at the target position of the enzyme, modification of cytosine residues at position N4
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
enzyme is a critical regulator of bacterial virulence
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
methylation of the site GATCprox proximal to the promotor is required for transition to the phase On state by specifically blocking PapI-dependent binding of Lrp to promotor proximal sites 4-6, expression of pyelonephritis-associated pili, i.e. Pap, in uropathogenic Escherichia coli is epigenetically controlled by a reversible OFF to ON switch, overview
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme is cell cycle regulated and essential for viability
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
DNA substrate from calf thymus, methylation of adjacent GATC sites is distributive with DNA derived from a genetic element that controls the transcription of the adjacent genes, the first methylation event is followed by enzyme release
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
enzyme methylates the first adenine in the sequence ATGCAT
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
methylation of target sequence GATC
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
required substrate recognition target sequence is GATC, occuring base flipping in absence of S-adenosyl-L-methionine is a biphasic process and very fast, but binding of the flipped base into the active site pocket requiring S-adenosyl-L-methionine is slow, active site contains the conserved DPPY motif, whose tyrosine184 residue stacks to the flipped target base
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
specific for methylation site sequence GATC and structure, an intact GA sequence is essential for activity, altered structural symmetry of the DNA substrate decreases kcat sharply, the best contact between enzyme and DNA is a palindromic interaction site covering the 5'-symmetric residues, which is located in the major groove, and another one in the 3'-half covering the 3'-symmetric residues is located in the minor groove, overview
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
transition of enzyme-DNA interaction from nonspecific to specific interaction utilizing different substrates, identification of discriminatory contacts stabilizing the transition state, and antidiscriminatory contacts not affecting the methylation of the cognate site but disfavor activity at noncognate sites, involved are Y119, N120, L122, R124, and P134, overview
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme recognizes 5'-GATC-3'
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
nonglucosylated, hydroxymethylcytosine-containing T2gt- virion DNA has a higher level of methylation than T4gt virion DNA does
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Hapunavirus VP882
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
enzyme is not important in mismatch repair and for adherence of the bacterium to host cells, e.g. HEp-2 cells
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
enzyme is a member of a restriction-modification system, R-M system, plasmid DNA, and hemi- or unmethylated duplex DNA, preference for hemimethylated DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
enzyme recognizes the sequence 5'-GGTACC-3', methylation at position N6, enzyme utilizes plasmid DNA, and hemi- or unmethylated duplex DNA, preference for hemimethylated DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme catalyzes the methylation of adenine at the N-6 position within its DNA recognition sequence GATC. Enzymatic methylation of the hemimethylated GATC site results in destabilisation of the duplex, increasing the proportion of dissociated DNA, and producing an observable increase in fluorescence. By using a suitable oligonucleotide substrate, labeled on adjacent strands with a fluorophore (fluorescein) and quencher (dabcyl), the destabilization of duplex DNA due to adenine methylation can be monitored by fluorescence measurements. The separation of fluorophore and quencher during strand dissociation causes an observable increase in fluorescence, providing a reproducible, direct, and real-time activity assay
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Tequatrovirus T4
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Tequatrovirus T4
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Tequatrovirus T4
-
the enzyme mediates methyl group transfer reaction from S-adenosyl-L-methionine to adenine in the palindromic recognition sequence, GATC, of a 20-mer oligonucleotide duplex
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Tequatrovirus T4
-
in unmethylated target (2A/A duplex), the enzyme alone randomly binds to the asymetric 2A/A duplex, S-adenosyl-L-methionine induces an allosteric T4 conformational change that promotes reorientation of the enzyme to the strand containing the native base. S-Adenosyl-L-methionine increases enzyme binding-specificity, in addition to serving as the methyl donor, the enzyme recognizes the palindromic sequence GATC
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Tequatrovirus T4
-
various synthetic oligonucleotide substrates. Upon collision of an enzyme monomer with an oligonucleotide duplex, an asymmetrical complex forms in which the enzyme (randomly oriented relative to one of the strands of the specific recognition site) catalyzes a fast transfer of the methyl group from S-adenmosylmethionine to the adenosine residue. Simultaneously, a second T4MTAse subunit is added to the complex, providing for the continuation of the reaction
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Tequatrovirus T4
-
the enzyme catalyzes methyl group transfer from S-adenosyl-L-methionine to the N6-position of adenine in the palindromic sequence GATC. The rate-limiting step is release of product methylated DNA from the enzyme
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Tequatrovirus T4
-
oligonucleotide substrates containing the native or modified recognition site. The enzyme recognizes the palindromic sequence GATC and catalyzes transfer of the methyl group from S-adenosyl-L-methionine to the N6-position of adenine. The release of product is the rate-limiting step in the reaction
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Tequatrovirus T4
-
canonical 12-mer and 20-mers various defective duplexes containing some defect in the DNA-target site, e.g. the absence of an internucleotide phosphate or a nucleotide within the recognition site, or a single-stranded region
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Tequatrovirus T4
-
nonglucosylated unmethylated T4 gt- dam- DNA. The enzyme methylates the palindromic tetranucleotide, GATC, designated the canonical sequence. At high Mtase:DNA ratios, T4 Dam can methylate some noncanonical sequences belonging to GAY, where Y represents cytosine or thymine
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Tequatrovirus T4
-
synthetic oligonucleotide substrates containing the native recognition site GATC or its modified variants
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Tequatrovirus T4
-
interaction with substrates containing defective recognition sites. Deoxyguanosine residues in both strands of the modified GATC are indispensable for complex formation
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Tequatrovirus T4
-
nonglucosylated, hydroxymethylcytosine-containing T2gt- virion DNA has a higher level of methylation than T4gt virion DNA does
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Tequatrovirus T4
-
hemimethylated DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Tequatrovirus T4
methylation of DNA-adenine at certain GATC sites plays a pivotal role in bacterial and phage gene expression as well as in bacterial virulence
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Tequatrovirus T4
-
specific target sequence is GATC
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Tequatrovirus T4
-
unmethylated or hemimethylated DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Tequatrovirus T4
-
binding site is the GATC sequence, the adenine is located in the palindromic recognition site GATC, substrate binding mechanism
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Tequatrovirus T4
-
specific for methylation site sequence GATC and structure, an intact GAT sequence is essential for activity, altered structural symmetry of the DNA substrate decreases kcat sharply, the best contact between enzyme and DNA is a palindromic interaction site covering the 5'-symmetric residues, which is located in the major groove, and another one in the 3'-half covering the 3'-symmetric residues is located in the minor groove, overview
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Tequatrovirus T4
-
specific methylation of oligonucleotide duplexes containing one or two target sequence GATC sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Tequatrovirus T4
specific methylation of target sequence GATC
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Tequatrovirus T4
-
specific target sequence is GATC, transition of enzyme-DNA interaction from nonspecific to specific interaction utilizing different substrates, identification of discriminatory contacts stabilizing the transition state, and antidiscriminatory contacts not affecting the methylation of the cognate site but disfavor activity at noncognate sites, involved residues are M114, R116, P126, G128, R130, F111, S112, D171, K11, and Y174, overview, flipping of target adenine
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Tequatrovirus T4
-
unmethylated or hemimethylated DNA, two distinct stages of methylation under single turnover conditions
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
GGGTGATCAGGG
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
CCCTGATCACCC
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme de novo methylates the first adenine residue in the TGATCA sequence in the single-stranded or double-stranded DNA substrate, but it prefers single-stranded structures
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
GCGTGATCACGC
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
GGGTGATCAGGG+CCCTGATCACCC, annealed
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
lambda phage DNA
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme is responsible for mitochondrial DNA modification that might be involved in the regulation of replication of mitochondria in plants
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme modifies the third adenine within the recognition sequence 5-ATTAAT-3'
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
-
?
S-adenosyl-L-methionine + DNA duplex carrying the 5'-AAGCUU-3'/3'-TTCGAA-5' target sequence
?
-
100% activity
-
-
-
S-adenosyl-L-methionine + DNA duplex carrying the 5'-AAGCUU-3'/3'-TTCGAA-5' target sequence
?
-
100% activity
-
-
-
S-adenosyl-L-methionine + DNA duplex carrying the 5'-AAGCUU-3'/3'-TTCGAA-5' target sequence
?
-
100% activity
-
-
-
S-adenosyl-L-methionine + DNA duplex carrying the 5'-AAGCUU-3'/3'-TTCGAA-5' target sequence
?
-
100% activity
-
-
-
S-adenosyl-L-methionine + double stranded DNA adenine
S-adenosyl-L-homocysteine + double stranded DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + double stranded DNA adenine
S-adenosyl-L-homocysteine + double stranded DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + double stranded DNA adenine
S-adenosyl-L-homocysteine + double stranded DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + double stranded DNA adenine
S-adenosyl-L-homocysteine + double stranded DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + double stranded DNA adenine
S-adenosyl-L-homocysteine + double stranded DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + double stranded DNA adenine
S-adenosyl-L-homocysteine + double stranded DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + Int1 DNA
S-adenosyl-L-homocysteine + Int1 DNA containing N6-methyladenine
-
adenine methylation occurs at a GAATTC site
-
-
?
S-adenosyl-L-methionine + Int1 DNA
S-adenosyl-L-homocysteine + Int1 DNA containing N6-methyladenine
-
adenine methylation occurs at a GAATTC site
-
-
?
S-adenosyl-L-methionine + lambda phage DNA
?
-
the enzyme modifies the adenine residue with formation of 5'-(m6A)GCT-3'
-
-
?
S-adenosyl-L-methionine + lambda phage DNA
?
-
the enzyme modifies the adenine residue with formation of 5'-(m6A)GCT-3'
-
-
?
S-adenosyl-L-methionine + RNA/DNA heteroduplex carrying the 5'-AAGCUU-3'/3'-TTCGAA-5' target sequence
?
-
low activity. Only the DNA strand of the RNA/DNA heteroduplex is methylated
-
-
-
S-adenosyl-L-methionine + RNA/DNA heteroduplex carrying the 5'-AAGCUU-3'/3'-TTCGAA-5' target sequence
?
-
low activity. Only the DNA strand of the RNA/DNA heteroduplex is methylated
-
-
-
S-adenosyl-L-methionine + RNA/DNA heteroduplex carrying the 5'-AAGCUU-3'/3'-TTCGAA-5' target sequence
?
-
low activity. Only the DNA strand of the RNA/DNA heteroduplex is methylated
-
-
-
S-adenosyl-L-methionine + RNA/DNA heteroduplex carrying the 5'-AAGCUU-3'/3'-TTCGAA-5' target sequence
?
-
low activity. Only the DNA strand of the RNA/DNA heteroduplex is methylated
-
-
-
S-adenosyl-L-methionine + single stranded DNA adenine
S-adenosyl-L-homocysteine + single stranded DNA 6-methyladenine
-
the level of single stranded DNA methylation is 7fold lower than double stranded DNA. However, upon star activity conditions (30% DMSO), the efficiency of single stranded DNA modification is raised by up to 50% of the relative activity
-
-
?
S-adenosyl-L-methionine + single stranded DNA adenine
S-adenosyl-L-homocysteine + single stranded DNA 6-methyladenine
-
the level of single stranded DNA methylation is 7fold lower than double stranded DNA. However, upon star activity conditions (30% DMSO), the efficiency of single stranded DNA modification is raised by up to 50% of the relative activity
-
-
?
S-adenosyl-L-methionine + T7 DNA adenine
S-adenosyl-L-homocysteine + T7 DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + T7 DNA adenine
S-adenosyl-L-homocysteine + T7 DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + T7 phage DNA
?
-
the enzyme modifies the adenine residue with formation of 5'-(m6A)GCT-3'
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S-adenosyl-L-methionine + T7 phage DNA
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the enzyme modifies the adenine residue with formation of 5'-(m6A)GCT-3'
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additional information
?
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the enzyme is part of the type II restriction-modification system AhdI, overview
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additional information
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the common methyl transfer from S-adenosyl-L-methionine to an exocyclic amino group, catalyzed by many enzymes, does not dictate a common kinetic scheme for MTases, comparison to T4Dam MTase from bacteriophage T4
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additional information
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the enzyme does not produce any detectable N4-cytosine methylation
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additional information
?
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the enzyme does not produce any detectable N4-cytosine methylation
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additional information
?
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the enzyme has a high specificity for GANTC sites, with only minor preferences at the central position. It slightly (1.5fold) prefers hemimethylated DNA over methylated DNA
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additional information
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the enzyme methylates GANTC sequences but does not specifically bind to DNA containing GANTC sequences
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additional information
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the enzyme methylates adenine residues in 5'-GANTC-3' sequences
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additional information
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the enzyme does not specifically bind to DNA containing GANTC sequences
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additional information
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the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
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the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
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the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
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the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
-
the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
-
the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
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the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
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substrate specificity with different oligonucleotides, substrate binding specificity, overview
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additional information
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catalyzes the transfer of a methyl group to the C5 position of the 3'-side cytosine of each strand of the recognition sequence, M.EcoRII binding is diminished by factors of 5-30 but the catalytic activity is either abolished or reduced 4-80fold when trans-anti-B[a]P-N2-dG lesions are introduced into the EcoRII recognition sequence, methylation rates are also diminished and in some cases entirely abolished, depending on the position of the lesion within the recognition sequence
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additional information
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DNA methylation by DAM may not globally affect gene transcription by physically blocking access of transcription factors to binding sites, Dam is down regulated in the stationary phase, which correlates with the enrichment of GATC in binding sites for CRP and Sigma 38
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additional information
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the preferred substrate consists of the annealed product of oligonucleotides 5'-CATTTACTTGATCCGGTATGC-3' and 5'-GCATACCGGATCAAGTAAATG-3', while the nonpreferred substrate consists of the annealed product of oligonucleotides 5'-CATTTAGACGATCTTTTATGC-3' and 5'-GCATAAAAGATCGTCTAAATG-3'
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additional information
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the wild type Dam shows no detectable activity at GATT sites
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additional information
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the wild type enzyme is active on hemimethylated and unmethylated DNA substrates
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additional information
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relative to GATC, three near-cognate substrates that carry a base-pair substitution at the first position are still methylated by the enzyme, although at rates reduced by 100fold (AATC) or 1000fold (CATC)
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additional information
?
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relative to GATC, three near-cognate substrates that carry a base-pair substitution at the first position are still methylated by the enzyme, although at rates reduced by 100fold (AATC) or 1000fold (CATC)
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additional information
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the DNA substrate preference for M.EcoVIII is: hemimethylated AAGCTT > AAGCTT > GAGCTT >/= CAGCTT > AATCTT > ATGCTT > ACGCTT > TAGCTT > AACCTT = single stranded AAGCTT > AGGCTT = AAACTT
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additional information
?
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the enzyme is not able to methylate nucleotide sequence containing two mismatches (5'-CAGCTG-3')
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additional information
?
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the DNA substrate preference for M.EcoVIII is: hemimethylated AAGCTT > AAGCTT > GAGCTT >/= CAGCTT > AATCTT > ATGCTT > ACGCTT > TAGCTT > AACCTT = single stranded AAGCTT > AGGCTT = AAACTT
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additional information
?
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the enzyme is not able to methylate nucleotide sequence containing two mismatches (5'-CAGCTG-3')
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additional information
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the enzyme is not able to methylate nucleotide sequence containing two mismatches (5'-CAGCTG-3') and single stranded DNA adenine
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additional information
?
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the enzyme is not able to methylate nucleotide sequence containing two mismatches (5'-CAGCTG-3') and single stranded DNA adenine
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additional information
?
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the enzyme recognizes and methylates GAGG (100% activity, Km 0.00522 mM), GGAG (about 48% activity, Km 0.017 mM) and GAAG (about 30% activity, Km 0.013 mM), but does not methylate GTGG, GmAmAG or GAGA
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additional information
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purified recombinant enzyme, in the presence of S-adenosyl-L-methionine and other cofactors, is unable to methylate trivalent inorganic arsenic or monomethylarsonous acid
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additional information
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purified recombinant enzyme, in the presence of S-adenosyl-L-methionine and other cofactors, is unable to methylate trivalent inorganic arsenic or monomethylarsonous acid
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?
additional information
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the enzyme complex shows strong activity on single-stranded oligo 6 T (containing GGACT), much reduced activities on 4 T (containing GGAGT) and 4B (AGACT), and no activity on oligos having two substitutions within the recognition, e.g. 6B (AGAGT) or 5 T and 5B (GGATC). Furthermore, the enzyme complex has no activity on an oligo-containing G and C only and no activity on A-containing oligos without matching consensus sequence. The enzyme complex acts on single-stranded DNA (6 T) faster than that on the corresponding single-stranded RNA and is inactive on double-stranded DNA or RNA/DNA hybrid
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additional information
?
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the enzyme is not able to methylate nucleotide sequence containing two mismatches (5'-CAGCTG-3') and single stranded DNA adenine
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additional information
?
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the enzyme is not able to methylate nucleotide sequence containing two mismatches (5'-CAGCTG-3') and single stranded DNA adenine
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additional information
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Marinobacter nauticus
the enzyme does not produce any detectable N4-cytosine methylation
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additional information
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MmeI does not produce any detectable N4-cytosine methylation
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additional information
?
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the enzyme does not produce any detectable N4-cytosine methylation
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additional information
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no detectable activity on the single-stranded form of the phage PhiX174 DNA is observed with M1.MboII, double-stranded DNA is less efficiently methylated than pUC18 DNA
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additional information
?
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the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
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the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
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the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
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the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
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the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
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the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
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the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
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the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
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the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
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the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
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the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
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the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
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the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
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the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
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the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
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Dam-dependent regulation of secretion of pathogenicity island 1 is transmitted via transcriptional regulator HilD
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additional information
?
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the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
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the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
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the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
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plastid transcription is largely insensitive to adenine methylation of the plastid DNA
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?
additional information
?
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Tequatrovirus T4
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S-adenosyl-L-methionine plays a crucial role in reorientation of the enzyme in DNA with mutationally altered Ade residues to 2-aminopurine, overview
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?
additional information
?
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Tequatrovirus T4
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DNA substrate specificities of wild-type and mutant enzymes
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?
additional information
?
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Tequatrovirus T4
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enzyme and S-adenosyl-L-methionine form a catalytically active complex
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additional information
?
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Tequatrovirus T4
enzyme binds also nonspecific to DNA, linear diffusion along the DNA, overview
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additional information
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the enzyme does not produce any detectable N4-cytosine methylation
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