Literature summary for 3.1.21.5 extracted from

Toth, J.; Bollins, J.; Szczelkun, M.D.
Re-evaluating the kinetics of ATP hydrolysis during initiation of DNA sliding by Type III restriction enzymes (2015), Nucleic Acids Res., 43, 10870-10881 .

Search for more literature for 3.1.21.5

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P12364	-	-
Punavirus P1	P08764	Bacteriophage P1	-

Substrates and Products (Substrate)

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

Synonyms	Comment	Organism
EcoP15I	-	Escherichia coli
EcoPI	-	Punavirus P1

Cofactor

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

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Release 2023.1 (January 2023)