Jump to content

Exoribonuclease II

From Wikipedia, the free encyclopedia

This is the current revision of this page, as edited by PrimeBOT (talk | contribs) at 14:00, 26 August 2023 (top: Task 30: infobox bad param removal). The present address (URL) is a permanent link to this version.

(diff) ← Previous revision | Latest revision (diff) | Newer revision → (diff)
Exoribonuclease II
Identifiers
EC no.3.1.13.1
CAS no.37288-24-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

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.

See also

[edit]

References

[edit]
  1. ^ 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.
  2. ^ 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.
  3. ^ 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.
  4. ^ 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.
[edit]