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• W2007458839 abstract "The Eco57l restriction endonuclease and methylase were purified to homogeneity from the E.coli RR1 strain carrying the eco57IRM genes on a recombinant plasmid. The molecular weight of the denaturated methylase is 63 kDa. The restriction endonuclease exists in a monomeric form with an apparent molecular weight of 104–108 kDa. R. Eco57l also possesses methylase activity. The methylation activities of both enzymes modify the outer A residue in the target sequence 5′CTGAAG yielding N6-methyladenine. M. Eco57l modifies both strands of the substrate while R. Eco57l modifies only one. Only the methylase enzyme is stimulated by Ca 2++ . The restriction endonuclease shows an absolute requirement for Mg 2+ and is stimulated by AdoMet. ATP has no influence on either activity of the enzymes. The subunit structure and enzymatic properties of the Eco57l enzymes distinguish them from all other restriction-modification enzymes that have been described previously. Therefore, RM. Eco57l may be regarded as a representative of a novel class of restriction-modification systems, and we propose to classify it as type IV." @default.
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• W2007458839 date "1992-01-01" @default.
• W2007458839 modified "2023-10-18" @default.
• W2007458839 title "Purification and properties of the<i>Eco57l</i>restriction endonuclease and methylas—prototypes of a new class (type IV)" @default.
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• W2007458839 doi "https://doi.org/10.1093/nar/20.22.6043" @default.
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