Exoribonuclease II (EC 3.1.13.1, ribonuclease II, ribonuclease Q, BN ribonuclease, Escherichia coli exo-RNase II, RNase II, exoribonuclease (misleading), 5'-exoribonuclease) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction
Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates
This enzyme has preference for single-stranded RNA.
^Nossal NG, Singer MF (March 1968). "The processive degradation of individual polyribonucleotide chains. I. Escherichia coli ribonuclease II". The Journal of Biological Chemistry. 243 (5): 913–22. PMID 4867942.
^Schmidt FJ, McClain WH (November 1978). "An Escherichia coli ribonuclease which removes an extra nucleotide from a biosynthetic intermediate of bacteriophage T4 proline transfer RNA". Nucleic Acids Research. 5 (11): 4129–39. doi:10.1093/nar/5.11.4129. PMC 342738. PMID 364422.
^Shimura Y, Sakano H, Nagawa F (May 1978). "Specific ribonucleases involved in processing of tRNA precursors of Escherichia coli. Partial purification and some properties". European Journal of Biochemistry. 86 (1): 267–81. doi:10.1111/j.1432-1033.1978.tb12308.x. PMID 350582.
^Sporn MB, Lazarus HM, Smith JM, Henderson WR (April 1969). "Studies on nuclear exoribonucleases. 3. Isolation and properties of the enzyme from normal and malignant tissues of the mouse". Biochemistry. 8 (4): 1698–706. doi:10.1021/bi00832a053. PMID 5805304.
and 21 Related for: Exoribonuclease II information
ExoribonucleaseII (EC 3.1.13.1, ribonuclease II, ribonuclease Q, BN ribonuclease, Escherichia coli exo-RNase II, RNase II, exoribonuclease (misleading)...
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RNase R, or Ribonuclease R, is a 3'-->5' exoribonuclease, which belongs to the RNase II superfamily, a group of enzymes that hydrolyze RNA in the 3' -...
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all belong to the RNase PH family of RNases and are phosphorolytic exoribonucleases, meaning that they use inorganic phosphate to remove nucleotides from...
is that some members of the order Nidovirales encode proofreading exoribonuclease activity as part of a protein that is distinct from RdRp. Excluding...
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