Ribonuclease T2

Ribonuclease T2
Identifiers
EC number 3.1.27.1
CAS number 37278-25-4
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Ribonuclease T2 (EC 3.1.27.1, ribonuclease II, base-non-specific ribonuclease, nonbase-specific RNase, RNase (non-base specific), non-base specific ribonuclease, nonspecific RNase, RNase Ms, RNase M, RNase II, Escherichia coli ribonuclease II, ribonucleate nucleotido-2'-transferase (cyclizing), acid ribonuclease, RNAase CL, Escherichia coli ribonuclease I' ribonuclease PP2, ribonuclease N2, ribonuclease M, acid RNase, ribonnuclease (non-base specific), ribonuclease (non-base specific), RNase T2, ribonuclease PP3, ribonucleate 3'-oligonucleotide hydrolase, ribonuclease U4) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction

Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates

See also

References

  1. ↑ García-Segura JM, Orozco MM, Fominaya JM, Gavilanes JG (July 1986). "Purification, molecular and enzymic characterization of an acid RNase from the insect Ceratitis capitata". European Journal of Biochemistry. 158 (2): 367–72. doi:10.1111/j.1432-1033.1986.tb09760.x. PMID 3732273.
  2. ↑ Heppel LA, Davies DR (1966). "Pig liver nuclei ribonuclease". In Cantoni GL. Procedures in Nucleic Acid Research. New York: Procedures in Nucleic Acid Research. pp. 31–36.
  3. ↑ Reddi KK, Mauser LJ (March 1965). "Studies on the formation of tobacco mosaic virus ribonucleic acid. VI. Mode of degradation of host ribonucleic acid to ribonucleosides and their conversion to ribonucleoside 5′-phosphates". Proceedings of the National Academy of Sciences of the United States of America. 53 (3): 607–13. doi:10.1073/pnas.53.3.607. PMC 336984. PMID 14338240.
  4. ↑ Uchida T, Egami F (January 1967). "The specificity of ribonuclease T2". Journal of Biochemistry. 61 (1): 44–53. PMID 6048969.
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