Literature summary for 3.1.13.1 extracted from

Hsu, C.H.; Chang, C.F.; Liao, Y.D.; Wu, S.H.; Chen, C.
Solution structure and base specificity of cytotoxic RC-RNase 2 from Rana catesbeiana (2015), Arch. Biochem. Biophys., 584, 70-78 .

Cloned(Commentary)

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/ Products (Substrates)

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

Organism	UniProt	Comment	Textmining
Lithobates catesbeianus	A0A2G9RV63	i.e. Rana catesbeiana	-

Purification (Commentary)

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 (Commentary)

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

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

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 and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the base preference for RNase 2 is UpG	Lithobates catesbeianus	?	-	?

Subunits

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

Synonyms	Comment	Organism
AB205_0003320	-	Lithobates catesbeianus
RC-RNase 2	-	Lithobates catesbeianus
RNase 2	-	Lithobates catesbeianus

General Information

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