| 词条 | DNA/RNA non-specific endonuclease |
| 释义 |
| Symbol = Endonuclease_NS | Name = Endonuclease_NS | image = PDB 1smn EBI.jpg | width = | caption = identification of the serratia endonuclease dimer: structural basis and implications for catalysis | Pfam = PF01223 | Pfam_clan = CL0263 | InterPro = IPR001604 | SMART = | PROSITE = PDOC00821 | MEROPS = | SCOP = 1smn | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = cd00091 }} In molecular biology, enzymes in the DNA/RNA non-specific endonuclease family of bacterial and eukaryotic endonucleases {{EC number|3.1.30.-}} share the following characteristics: they act on both DNA and RNA, cleave double-stranded and single-stranded nucleic acids and require a divalent ion such as magnesium for their activity. A histidine has been shown to be essential for the activity of the Serratia marcescens nuclease. This residue is located in a conserved region which also contains an aspartic acid residue that could be implicated in the binding of the divalent ion.[1] References1. ^{{cite journal |vauthors=Friedhoff P, Gimadutdinow O, Pingoud A | title = Identification of catalytically relevant amino acids of the extracellular Serratia marcescens endonuclease by alignment-guided mutagenesis | journal = Nucleic Acids Res. | volume = 22 | issue = 16 | pages = 3280–7 |date=August 1994 | pmid = 8078761 | pmc = 523719 | doi = 10.1093/nar/22.16.3280| url = }} {{InterPro content|IPR001604}}{{DEFAULTSORT:DNA RNA non-specific endonuclease}} 1 : Protein domains |
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