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Literature summary for 3.1.21.5 extracted from

  • Crampton, N.; Yokokawa, M.; Dryden, D.T.; Edwardson, J.M.; Rao, D.N.; Takeyasu, K.; Yoshimura, S.H.; Henderson, R.M.
    Fast-scan atomic force microscopy reveals that the type III restriction enzyme EcoP15I is capable of DNA translocation and looping (2007), Proc. Natl. Acad. Sci. USA, 104, 12755-12760.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
real-time imaging of enzyme at scan rates of 1-3 frames per s. EcoP15I translocates DNA in an ATP-dependent manner, at a rate of 79 bp/s, resulting in the accumulation of supercoiling. EcoP15I bound to its recognition site also makes nonspecific contacts with other DNA sites, thus forming DNA loops and reducing the distance between the two recognition sites Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli the enzyme uses both diffuse DNA loop formation and ATPase driven translocation of the intervening DNA contour to communicate between two recognition sites ?
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Organism

Organism UniProt Comment Textmining
Escherichia coli
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isoform EcoP15I
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme uses both diffuse DNA loop formation and ATPase driven translocation of the intervening DNA contour to communicate between two recognition sites Escherichia coli ?
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?