Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P12364 | - |
- |
Punavirus P1 | P08764 | Bacteriophage P1 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
DNA + H2O | 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 | Punavirus P1 | specific double-stranded DNA fragments with terminal 5'-phosphate | - |
? | |
DNA + H2O | the kinetics of ATP hydrolysis by EcoP15I is influenced by the proximity of DNA ends to the site. 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 | Escherichia coli | specific double-stranded DNA fragments with terminal 5'-phosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
EcoP15I | - |
Escherichia coli |
EcoPI | - |
Punavirus P1 |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
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 | Punavirus P1 | |
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 | Escherichia coli |