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• W2040495869 abstract "Analyzing the pattern of oligonucleotide formation induced by HP-RNase cleavage shows that the enzyme does not act randomly and follows a more endonucleolytic pattern when compared to RNase A. The enzyme prefers the binding and cleavage of longer substrate molecules, especially when the phosphodiester bond that is broken is 8-11 nucleotides away from at least one of the ends of the substrate molecule. This more endonucleolytic pattern is more appropriate for an enzyme with a regulatory role. Deleting two positive charges on the N-terminus (Arg4 and Lys6) modifies this pattern of external/internal phosphodiester bond cleavage preference, and produces a more exonucleolytic enzyme. These residues may reinforce the strength of a non-catalytic secondary phosphate binding (p2) or, alternatively, constitute a new non-catalytic phosphate binding subsite (p3)." @default.
• W2040495869 created "2016-06-24" @default.
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• W2040495869 date "2008-03-01" @default.
• W2040495869 modified "2023-09-24" @default.
• W2040495869 title "Human pancreatic ribonuclease presents higher endonucleolytic activity than ribonuclease A" @default.
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• W2040495869 doi "https://doi.org/10.1016/j.abb.2007.12.016" @default.
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