EC |
3.1.13.1 |
Accepted name: |
exoribonuclease II |
Reaction: |
Exonucleolytic cleavage in the 3′- to 5′-direction to yield nucleoside 5′-phosphates |
Other name(s): |
ribonuclease II; ribonuclease Q; BN ribonuclease; Escherichia coli exo-RNase II; RNase II; exoribonuclease (misleading); 5′-exoribonuclease (misleading) |
Comments: |
Preference for single-stranded RNA. The enzyme processes 3′-terminal extra-nucleotides of monomeric tRNA precursors, following the action of EC 3.1.26.5 ribonuclease P. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 37288-24-7 |
References: |
1. |
Nossal, N.G. and Singer, M. The processive degradation of individual polyribonucleotide chains. I. Escherichia coli ribonuclease II. J. Biol. Chem. 243 (1968) 913–922. [PMID: 4867942] |
2. |
Schmidt, F.J. and McClain, W.H. An Escherichia coli ribonuclease which removes an extra nucleotide from a biosynthetic intermediate of bacteriophage T4 proline transfer RNA. Nucleic Acids Res. 5 (1978) 4129–4139. [DOI] [PMID: 364422] |
3. |
Shimura, Y., Sakano, H. and Nagawa, F. Specific ribonucleases involved in processing of tRNA precursors of Escherichia coli. Partial purification and some properties. Eur. J. Biochem. 86 (1978) 267–281. [DOI] [PMID: 350582] |
4. |
Sporn, M.B., Lazarus, H.M. Smith, J.M. and Henderson, W.R. Studies on nuclear exoribonucleases. 3. Isolation and properties of the enzyme from normal and malignant tissues of the mouse. Biochemistry 8 (1969) 1698–1706. [PMID: 5805304] |
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[EC 3.1.13.1 created 1972 as EC 3.1.4.20, transferred 1978 to EC 3.1.13.1] |
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