Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.113 0.00035
-
 5'-CAGTTTAGGATCCATTTCAC-3'/3'-GTCAAATCCTAGGTAAAAGAG-5'
-
 Bacillus amyloliquefaciens
2.1.1.113 0.0016
-
 S-adenosyl-L-methionine
-
 Bacillus amyloliquefaciens

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.113 S-adenosyl-L-methionine + 5'-CAGTTTAGGATCCATTTCAC-3'/3'-GTCAAATCCTAGGTAAAAGAG-5
-
 Bacillus amyloliquefaciens ?
-
 ?
2.1.1.113 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

EC Number Subunits Comment Organism
2.1.1.113 additional information 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]

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