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S-adenosyl-L-methionine + 5'-CAGTTTAGGATCCATTTCAC-3'/3'-GTCAAATCCTAGGTAAAAGAG-5
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S-adenosyl-L-methionine + 5'-GTGAAAT*GGATCC*TAAACTG-3'/3'-CACTTTA*CCTAGG*ATTTGAC-5'
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S-adenosyl-L-methionine + DNA cytosine
S-adenosyl-L-homocysteine + DNA N4-methylcytosine
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
additional information
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S-adenosyl-L-methionine + DNA cytosine
S-adenosyl-L-homocysteine + DNA N4-methylcytosine
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S-adenosyl-L-methionine + DNA cytosine
S-adenosyl-L-homocysteine + DNA N4-methylcytosine
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S-adenosyl-L-methionine + DNA cytosine
S-adenosyl-L-homocysteine + DNA N4-methylcytosine
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S-adenosyl-L-methionine + DNA cytosine
S-adenosyl-L-homocysteine + DNA N4-methylcytosine
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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20-mer oligodeoxynucleotide duplex containing the palindromic recognition site GGATCC. The enzyme catalyzes methyl group transfer to the internal cytosine residue in the palindromic recognition site GGATCC. The enzyme transfers the methyl group to the exocyclic NH2-group without formation of a transient covalent bond
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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5'-GTGAAAT*GGATCC*TAAACTG-3'/3'-CACTTTA*CCTAGG*ATTTGAC-5'. The target base is the internal cytosine in the recognition sequence
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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20-mer duplex 5'-CAGTTTAGGATCCATTTCAC-3'/3'-GTCAAATCCTAGGTAAAAGAG-5' containing a palindromic recognition site GGATCC
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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M.BcnIA and M.BcnIB act on 5'-CC(C/G)GG-3' sites in double-stranded DNA. M.BcnIA can also, with a comparable efficiency, modify the specific targets in single-stranded DNA
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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substrate is pNH20 plasmid DNA. M2.MboII modifies the internal cytosine in the recognition sequence 39-CTTCT-59, yielding N4-methylcytosine, and moreover is able to methylate double- and single-stranded DNA, single-stranded DNA is preferred. Determination and analysis of the methylation pattern of M2.MboII, overview
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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substrate is pNH20 plasmid DNA. M2.NcuI modifies the internal cytosine in the recognition sequence yielding N4-methylcytosine, and moreover is able to methylate double- and single-stranded DNA, single-stranded DNA is preferred. Determination of the methylation position, overview
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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the enzyme generates N4-methylcytosine in duplex 5'-CAGCTG-3' DNA. PvuII methyltransferase is catalytically competent with one and with two bound molecules of S-adenosyl-L-methionine
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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the enzyme catalyzes the transfer of the methyl group from S-adenosyl-L-methionine to the exocyclic aminoN4 nitrogen of the central cytosine in its recognition sequence 5'-CAGCTG-3'
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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the enzyme modifies the second cytosine in CAGCTG sequences, also methylates adenine residues in CAGATG/CAGCTG substrates in which the target cytosine is replaced by adenine in one strand of the recognition sequence
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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substrate is methylated plasmid DNA. M.PspGI is a type IIP methyltransferase and enhances fluorescence of 2-aminopurine in DNA if it replaces the second C in the sequence
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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the SuaI restriction-modification system uses N4 methylation of the inner C of the recognition sequence GGCC in genomic DNA of Sulfolobus acidocaldarius to protect the recognition sequence from cleavage. SuaI is the only restriction-modification system detected in SUlfolobus acidocaldarius and the N4 methylation of the inner C in the recognition site is necessary and sufficient to protect against it
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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the SuaI restriction-modification system uses N4 methylation of the inner C of the recognition sequence GGCC in genomic DNA of Sulfolobus acidocaldarius to protect the recognition sequence from cleavage
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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the SuaI restriction-modification system uses N4 methylation of the inner C of the recognition sequence GGCC in genomic DNA of Sulfolobus acidocaldarius to protect the recognition sequence from cleavage. SuaI is the only restriction-modification system detected in SUlfolobus acidocaldarius and the N4 methylation of the inner C in the recognition site is necessary and sufficient to protect against it
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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the SuaI restriction-modification system uses N4 methylation of the inner C of the recognition sequence GGCC in genomic DNA of Sulfolobus acidocaldarius to protect the recognition sequence from cleavage
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
methylation of second cytosine of 5'-CCCGGG-3' recognition sequence
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
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S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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target sequences
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additional information
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integrity of ATCC sequence is critical
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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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