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Literature summary for 2.1.1.72 extracted from

  • Evdokimov, A.A.; Zinoviev, V.V.; Malygin, E.G.; Schlagman, S.L.; Hattman, S.
    Bacteriophage T4 Dam DNA-[N6-adenine]methyltransferase. Kinetic evidence for a catalytically essential conformational change in the ternary complex (2002), J. Biol. Chem., 277, 279-286.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
S-adenosyl-L-methionine stimulates at increasing concentrations Tequatrovirus T4

Inhibitors

Inhibitors Comment Organism Structure
additional information reduction of methylation rate at high concentrations of the substrate 20-mer DNA duplex Tequatrovirus T4
S-adenosyl-L-homocysteine product inhibition Tequatrovirus T4
sinefungin
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Tequatrovirus T4

Organism

Organism UniProt Comment Textmining
Tequatrovirus T4
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Reaction

Reaction Comment Organism Reaction ID
S-adenosyl-L-methionine + adenine in DNA = S-adenosyl-L-homocysteine + N6-methyladenine in DNA steady-state-ordered bi-bi mechanism in which the order of substrate binding and product release is S-adenosyl-L-methionine, DNA, DNAMe, S-adenosyl-L-homocysteine Tequatrovirus T4

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + DNA adenine 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 Tequatrovirus T4 S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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