EC Number   |
Subunits |
Reference |
|---|
   3.1.21.5 | ? |
x * 106000, subunit Res, + x * 75000, subunit Mod, deduced from gene sequence |
653387 |
| 3.1.21.5 | heterotrimer |
1 * 108264 + 2 * 63715, calculated from amino acid sequence |
730513 |
| 3.1.21.5 | heterotrimer |
1 * 110957 + 2 * 74094, EcoP15I, calculated from amino acid sequence |
730513 |
| 3.1.21.5 | heterotrimer |
1 * 111459 + 2 * 73486, EcoPI, calculated from amino acid sequence |
730513 |
| 3.1.21.5 | More |
functional interaction of enzymes EcoP1I and EcoP15I |
653387 |
| 3.1.21.5 | More |
in the presence of specific DNA, the entire modification subunit of the enzyme is protected from trypsin digestion, whereas in the absence of DNA stable protein domains of the modification subunit are not detected. In contrast, the restriction subunit is comprised of two trypsin-resistant domains of about 77000-79000 Da and 27000-29000 Da, respectively. Both structural restriction domains are connected by a flexible linker region that spans 23 amino acid residues |
683774 |
| 3.1.21.5 | More |
separation of Res and Mod subunits by gel filtration in presence of 2 M NaCl |
652861 |
| 3.1.21.5 | More |
the type III R/M enzymes comprise two modification subunits, each containing a target recognition domain to bind to the target sequence and a methyltransferase catalytic domain to monitor the methylation status of an adenine in the target, and two restriction subunits each containing a DNA helicase and ATP-hydrolysing domain and an endonuclease DNA cleavage domain |
716751 |
| 3.1.21.5 | tetramer |
2 * 105000 + 2 * 74000, deduced from gene sequence |
652848 |
| 3.1.21.5 | tetramer |
the intact Res2Mod2 tetramer is a fast endonuclease and slow methyltransferase, thereby favouring DNA cleavage, subassemblies of PstII in which the Res subunits have dissociated are more efficient methyltransferases. DNA cleavage by these lower molecular weight species may only occur if sufficient hsdR associates to form a Res2Mod2 tetramer before methylation occurs. This dynamic association of Res and Mod might play a key role in the control of PstII activity in vivo |
-, 666499 |
