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Literature summary 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., 278, 15713-15719.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.1.72 20mer fully methylated DNA duplex product inhibition, noncompetitive against both S-adenosyl-L-methionine and 20mer unmethylated DNA duplex Bacillus amyloliquefaciens
2.1.1.72 additional information no substrate inhibition even at high concentrations, no formation of dead-end complexes Bacillus amyloliquefaciens
2.1.1.72 S-adenosyl-L-homocysteine product inhibition, competitive against S-adenosyl-L-methionine, noncompetitive to 20mer unmethylated DNA duplex Bacillus amyloliquefaciens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.72 additional information
-
 additional information detailed kinetics, enzyme shows a simple kinetic behaviour towards a 20mer duplex DNA, random bi bi mechanism Bacillus amyloliquefaciens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.72 S-adenosyl-L-methionine + DNA adenine Bacillus amyloliquefaciens
-
 S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.72 Bacillus amyloliquefaciens
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.1.1.72 S-adenosyl-L-methionine + adenine in DNA = S-adenosyl-L-homocysteine + N6-methyladenine in DNA reaction scheme and random bi bi kinetic mechanism Bacillus amyloliquefaciens
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.72 additional information 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 Bacillus amyloliquefaciens ?
-
 ?
2.1.1.72 S-adenosyl-L-methionine + DNA adenine
-
 Bacillus amyloliquefaciens S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.72 BamHI MTase
-
 Bacillus amyloliquefaciens
2.1.1.72 DNA-(adenine-N6-)-methyltransferase
-
 Bacillus amyloliquefaciens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.1.72 37
-
 assay at Bacillus amyloliquefaciens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.1.72 8
-
 assay at Bacillus amyloliquefaciens

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.1.1.72 additional information
-
 additional information detailed inhibition kinetics Bacillus amyloliquefaciens