Ribonuclease T2

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Ribonuclease T2
Ribonuclease T2
Identifiers
EC no.	3.1.27.1
CAS no.	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
PMC
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PMC	articles
PubMed	articles
NCBI	proteins

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

References

^ Garcia-Segura, J.M.; Orozco, M.M.; Fominaya, J.M.; Gavilanes, J.G. (1986). "Purification, molecular and enzymic characterization of an acid RNase from the insect Ceratitis capitata". Eur. J. Biochem. 158 (2): 367–372. doi:10.1111/j.1432-1033.1986.tb09760.x. PMID 3732273.
^ Heppel, L.A.; Davies, D.R. (1966). "Pig liver nuclei ribonuclease". In Cantoni, G.L. (ed.). Procedures in Nucleic Acid Research. New York: Procedures in Nucleic Acid Research. pp. 31–36.
^ Reddi, K.K.; Mauser, L.J. (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". Proc. Natl. Acad. Sci. USA. 53 (3): 607–613. doi:10.1073/pnas.53.3.607. PMC 336984. PMID 14338240.
^ Uchida, I.; Egami, F. (1967). "The specificity of ribonuclease T₂". J. Biochem. (Tokyo). 61 (1): 44–53. PMID 6048969.

External links

Ribonuclease+T2 at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

[1] Garcia-Segura, J.M.; Orozco, M.M.; Fominaya, J.M.; Gavilanes, J.G. (1986). "Purification, molecular and enzymic characterization of an acid RNase from the insect Ceratitis capitata". Eur. J. Biochem. 158 (2): 367–372. doi:10.1111/j.1432-1033.1986.tb09760.x. PMID 3732273.

[2] Heppel, L.A.; Davies, D.R. (1966). "Pig liver nuclei ribonuclease". In Cantoni, G.L. (ed.). Procedures in Nucleic Acid Research. New York: Procedures in Nucleic Acid Research. pp. 31–36.

[3] Reddi, K.K.; Mauser, L.J. (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". Proc. Natl. Acad. Sci. USA. 53 (3): 607–613. doi:10.1073/pnas.53.3.607. PMC 336984. PMID 14338240.

[4] Uchida, I.; Egami, F. (1967). "The specificity of ribonuclease T₂". J. Biochem. (Tokyo). 61 (1): 44–53. PMID 6048969.

[1]

[2]

[3]

[4]

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

See also

References

External links