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Literature summary for 3.1.21.5 extracted from

  • Van Aelst, K.; Toth, J.; Ramanathan, S.; Schwarz, F.; Seidel, R.; Szczelkun, M.
    Type III restriction enzymes cleave DNA by long-range interaction between sites in both head-to-head and tail-to-tail inverted repeat (2010), Proc. Natl. Acad. Sci. USA, 107, 9123-9128.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.21.5

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli on linear DNA in contrast, there is only one route and resolvase completely blocks communication and cleavage, while on circular DNA, there are two routes for communication. If one route is blocked by resolvase, the enzyme can use the alternative route. No stepwise motor mechanism for type III enzymes, the enzyme can bypass triplexes during sliding ?
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 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information on linear DNA in contrast, there is only one route and resolvase completely blocks communication and cleavage, while on circular DNA, there are two routes for communication. If one route is blocked by resolvase, the enzyme can use the alternative route. No stepwise motor mechanism for type III enzymes, the enzyme can bypass triplexes during sliding Escherichia coli ?
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 ?
additional information DNA end capping stimulates cleavage of tail-to-tail oriented pairs of sites, rates of cleavage of tail-to-tail repeats, ATP hydrolysis rates, and DNA cleavage kinetics, overview Escherichia coli ?
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Synonyms

Synonyms Comment Organism
EcoPI
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 Escherichia coli
type III restriction enzyme
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 Escherichia coli
type III testriction-modification enzyme
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 Escherichia coli