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