Cloned (Comment) | Organism |
---|---|
recombinant expression of RC-RNase 2 with an extra Met at its N-terminus in Escherichia coli strain BL21(DE3) in inclusion bodies | Lithobates catesbeianus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Lithobates catesbeianus | the base preference for RNase 2 is UpG | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Lithobates catesbeianus | A0A2G9RV63 | i.e. Rana catesbeiana | - |
Purification (Comment) | Organism |
---|---|
recombinant RC-RNase 2 refolded from Escherichia coli strain BL21(DE3) inclusion bodies, further purification of the dialyzed enzyme by two different steps of cation exchange chromatography. The native enzyme is purified from oocytes by ultracentrifugation, extraction of the yolk granules from the pellet, followed by cation exchange chromatography | Lithobates catesbeianus |
Renatured (Comment) | Organism |
---|---|
recombinant RC-RNase 2 from Escherichia coli strain BL21(DE3) inclusion bodies by solution in 6 M GdnHCl, followed by rapid dilution to a final concentration of 0.07 mg/ml and incubated at 10°C for 24 h with refolding buffer containing Tris-acetate pH 8.5, 0.5 M L-arginine, 3 mM reduced glutathione, and 0.6 mM oxidized glutathione. The refolding solution is concentrated and dialyzed against sodium acetate (pH 5.0) | Lithobates catesbeianus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
embryo | cytotoxic ribonucleases with antitumor activity are found in the oocytes and early embryos of frogs | Lithobates catesbeianus | - |
oocyte | cytotoxic ribonucleases with antitumor activity are found in the oocytes and early embryos of frogs | Lithobates catesbeianus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the base preference for RNase 2 is UpG | Lithobates catesbeianus | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | NMR solution structure of recombinant rRC-RNase 2, the rRC-RNase 2 comprises three alpha-helices and two sets of antiparallel beta-sheets, RNAse 2 structure comparisons, overview. Enzyme analysis by NMR spectroscopy and tertiary structure calculations | Lithobates catesbeianus |
Synonyms | Comment | Organism |
---|---|---|
AB205_0003320 | - |
Lithobates catesbeianus |
RC-RNase 2 | - |
Lithobates catesbeianus |
RNase 2 | - |
Lithobates catesbeianus |
General Information | Comment | Organism |
---|---|---|
evolution | RC-RNase 2, a cytotoxic ribonuclease isolated from oocytes of bullfrog Rana catesbeiana, consists of 105 residues linked with 4 disulfide bridges and belongs to the bovine pancreatic ribonuclease (RNase A) superfamily. Among the RC-RNases, the base preference for RNase 2 is UpG but CpG for RCRNase 4, while RC-RNase possesses the base specificity of both UpG and CpG. RC-RNase 2 or 4 has much lower catalytic activity but only 3fold less cytotoxicity than RC-RNase. The differences of side-chain conformations of subsite residues among RNase A, RC-RNase, RC-RNase 4 and rRNase 2 are related to their distinct catalytic activities and base preferences. Chemical shift perturbations of three RC-RNases with various substrate analogues, overview | Lithobates catesbeianus |
additional information | solution structure of recombinant RC-RNase 2 by heteronuclear NMR technique, overview. The substrate-related residues in the base specificity among native RC-RNases are derived using the chemical shift perturbation on ligand binding | Lithobates catesbeianus |
physiological function | cytotoxic ribonucleases with antitumor activity are found in the oocytes and early embryos of frogs | Lithobates catesbeianus |