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Literature summary for 2.1.1.113 extracted from

  • Zinoviev, V.V.; Evdokimov, A.A.; Malygin, E.G.
    DNA-(N4-Cytosine)-methyltransferase from Bacillus amyloliquefaciens: mechanism of action derived from steady-state kinetics (2003), Mol. Biol. (Mosk.), 37, 116-124.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
additional information no substrate inhibition even at concentrations many times higher than the Km-values 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

Substrates and Products (Substrate)

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

Synonyms

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