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Literature summary for 2.1.1.113 extracted from

  • Malygin, E.G.; Ovechkina, L.G.; Zinoviev, V.V.; Lindstrem, U.M.; Reich, N.O.
    DNA-(N4-cytosine)-methyltransferase from Bacillus amyloliquefaciens: kinetic and substrate-binding properties (2001), Mol. Biol. (Mosk.), 35, 35-44.
No PubMed abstract available
Search for more literature for 2.1.1.113

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00035
-
 5'-CAGTTTAGGATCCATTTCAC-3'/3'-GTCAAATCCTAGGTAAAAGAG-5'
-
 Bacillus amyloliquefaciens
0.0016
-
 S-adenosyl-L-methionine
-
 Bacillus amyloliquefaciens

Organism

Organism UniProt Comment Textmining
Bacillus amyloliquefaciens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + 5'-CAGTTTAGGATCCATTTCAC-3'/3'-GTCAAATCCTAGGTAAAAGAG-5
-
 Bacillus amyloliquefaciens ?
-
 ?
S-adenosyl-L-methionine + [DNA]-cytosine 20-mer duplex 5'-CAGTTTAGGATCCATTTCAC-3'/3'-GTCAAATCCTAGGTAAAAGAG-5' containing a palindromic recognition site GGATCC Bacillus amyloliquefaciens S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
 ?

Subunits

Subunits Comment Organism
More enzyme in a free state exists as a dimer. Introduction of substoichiometric amounts of DNA into the reaction mixture results in pronounced multimerization of the enzyme. However, addition of SAM in saturating concentration at an excess of the oligonucleotide duplex over BamHI Mtase converts most of the enzyme into a monomeric state Bacillus amyloliquefaciens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Bacillus amyloliquefaciens