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Literature summary for 2.1.1.113 extracted from

  • Malygin, E.G.; Zinoviev, V.V.; Evdokimov, A.A.; Lindstrom, W.M., Jr.; Reich, N.O.; Hattman, S.
    DNA-(cytosine-N4)- and (adenine-N6)-methyltransferases have different kinetic mechanisms but the same reaction route: a comparison of M.BamHI and T4 Dam (2003), J. Biol. Chem., 20, 1-31.
No PubMed abstract available
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Inhibitors

Inhibitors Comment Organism Structure
additional information no apparent substrate inhibition at concentrations 100fold higher than the Km for DNA and 20fold higher than Km for S-adenosyl-L-methionine Bacillus amyloliquefaciens
S-adenosyl-L-homocysteine competitive with regard to S-adenosylmethionine and non-competitive with respect to unmethylated 20-mer duplex Bacillus amyloliquefaciens

Organism

Organism UniProt Comment Textmining
Bacillus amyloliquefaciens
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Reaction

Reaction Comment Organism Reaction ID
S-adenosyl-L-methionine + DNA cytosine = S-adenosyl-L-homocysteine + DNA N4-methylcytosine the product inhibition pattern consistent with a steady-state random bi-bi mechanism in which the dominant order of substrate binding and product release: S-adenosyl-L-methionine, methylated DNA, DNAMe, S-adenosyl-L-homocysteine Bacillus amyloliquefaciens
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + [DNA]-cytosine 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 Bacillus amyloliquefaciens S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
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 ?

Synonyms

Synonyms Comment Organism
BamHI [cytosine-N4] MTase
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 Bacillus amyloliquefaciens