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Literature summary extracted from

  • Arnold, U.; Leich, F.; Neumann, P.; Lilie, H.; Ulbrich-Hofmann, R.
    Crystal structure of RNase A tandem enzymes and their interaction with the cytosolic ribonuclease inhibitor (2011), FEBS J., 278, 331-340.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.6.1.18 RNase A tandem enzymes, hanging drop vapor diffusion method, mixing of 0.002 ml of 10 mg/ml protein in 10 mm Tris-HCl, pH 7.0, with 0.002 ml of reservoir solution containing 30% w/v PEG 8000 and 200 mm (NH4)2SO4, 6 days, 13°C, X-ray diffraction structure determination and analysis at 1.68 A resolution Bos taurus

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.6.1.18 cytosolic ribonuclease inhibitor RI, from Sus scrofa, binding of the RI molecule to the N-terminal RNase A entity, analysis of crystal structures of the RI–RNase A complex and the SGRSGRSG-RNase A tandem enzyme, PDB-ID 1DFJ, overview Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
4.6.1.18 Bos taurus P61823
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.6.1.18 additional information 6-carboxyfluorescein-dArU(dA)2-6-carboxytetramethylrhodamine as artificial substrate Bos taurus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.6.1.18 RNase A
-
 Bos taurus

General Information

EC Number General Information Comment Organism
4.6.1.18 malfunction RNase A tandem enzymes, in which two RNase A molecules are artificially connected by a peptide linker, and thus have a pseudodimeric structure, exhibit remarkable cytotoxic activity, but can be inhibited by the cytosolic ribonuclease inhibitor in vitro. Structure modeling, overview Bos taurus