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Literature summary for 3.1.21.5 extracted from

  • Raghavendra, N.K.; Rao, D.N.
    Unidirectional translocation from recognition site and a necessary interaction with DNA end for cleavage by Type III restriction enzyme (2004), Nucleic Acids Res., 32, 5703-5711.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
HU protein binding of HU protein interfers with R.EcoP15I cleavage activity Escherichia coli
Lac repressor cleavage can be abolished by the binding of Lac repressor downstream (3' side) but not upstream (5' side) of the recognition site Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Purification (Commentary)

Purification (Comment) Organism
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Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DNA + H2O cleavage site does not depend on the sequence context of the recognition sie. The enzyme can cleave linear DNA having either recognition sites in the same orientation or a single recognition site. Cleavage occurs predominantly at a site proximal to the DNA end in the case of multiple site substrates. The mechanism requires two enzyme molecules cooperating to elicit double-stranded break on DNA. The enzyme translocates on DNA in a 5' to 3' direction from its recognition site, switch in the direction of enzyme motion at the FNA ends Escherichia coli specific double-stranded DNA fragments with terminal 5'-phosphate
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Synonyms

Synonyms Comment Organism
R.EcoP15I
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Escherichia coli