EC Number   |
Cofactor |
Reference |
|---|
   3.1.21.5 | ATP |
- |
651365, 652943, 653387, 693685, 694914 |
| 3.1.21.5 | ATP |
ATP-dependent type III restriction endonuclease |
716751 |
| 3.1.21.5 | ATP |
DNA cleavage by the Type III restriction enzymes requires long-range protein communication between recognition sites facilitated by thermally-driven 1D diffusion. This DNA sliding is initiated by hydrolysis of multiple ATPs catalysed by a helicase-like domain. Two distinct ATPase phases are observed using short oligoduplex substrates; the rapid consumption of about 10 ATPs coupled to a protein conformation switch followed by a slower phase, the duration of which is dictated by the rate of dissociation from the recognition site. The second ATPase phase is both variable and only observable when DNA ends are proximal to the recognition site. On DNA with sites more distant from the ends, a single ATPase phase coupled to the conformation switch is observed and subsequent site dissociation requires little or no further ATP hydrolysis. The overall DNA dissociation kinetics (encompassing site release, DNA sliding and escape via a DNA end) are not influenced by the second phase |
751721 |
| 3.1.21.5 | ATP |
essential for the endonuclease activity |
730532 |
| 3.1.21.5 | ATP |
required |
134272 |
| 3.1.21.5 | ATP |
type III R-M enzymes possess a sequence-specific ATPase activity for DNA cleavage. ATP hydrolysis is required for the long-distance communication between the sites before cleavage |
730511 |
| 3.1.21.5 | CTP |
- |
730511 |
| 3.1.21.5 | GTP |
- |
730511 |
| 3.1.21.5 | S-adenosyl-L-methionine |
- |
694914, 730511 |
| 3.1.21.5 | S-adenosyl-L-methionine |
allosteric activator and specificity factor that ensures that cleavage only occurs when two endonucleases bind two recognition sites in a designated orientation |
652926 |
