3.1.21.5: type III site-specific deoxyribonuclease
This is an abbreviated version!
For detailed information about type III site-specific deoxyribonuclease, go to the full flat file.
Word Map on EC 3.1.21.5
Reaction
endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates
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Synonyms
ATP-dependent type III restriction endonuclease, BceSI, BsaHI, cj0031, EC 3.1.23, EC 3.1.24, EcoP1, EcoP15, EcoP15I, EcoPI, HinFIII, LlaFI, MmyCI, More, NgoAXP, PhaBI, PspGI, PstII, R.EcoP15I, R.MmyCI, REase, restriction endonuclease PstII, restriction-modification system, StyLTI, type III DNA restriction/modification enzyme, type III R-M enzyme, type III R/M enzyme, type III RE, type III restriction endonuclease, type III restriction enzyme, type III restriction-modification enzyme, type III restriction-modification system, type III RM system, type III testriction-modification enzyme, type III-like restriction endonuclease
ECTree
Cofactor
Cofactor on EC 3.1.21.5 - type III site-specific deoxyribonuclease
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ATP
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ATP
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ATP-dependent type III restriction endonuclease
ATP
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essential for the endonuclease activity
ATP
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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
ATP
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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
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
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
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
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
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
ATP
Punavirus P1
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
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
S-adenosyl-L-methionine
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S-adenosyl-L-methionine
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S-adenosyl-L-methionine
prophage P1
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allosteric activator and specificity factor that ensures that cleavage only occurs when two endonucleases bind two recognition sites in a designated orientation
S-adenosyl-L-methionine
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endogenously bound, absolutely required
S-adenosyl-L-methionine
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S-adenosyl-L-methionine is not necessary for DNA cleavage, the presence of S-adenosyl-L-methionine dramatically impaires DNA cleavage due to competing DNA methylation