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Literature summary extracted from

  • Pecher, P.; Arnold, U.
    The effect of additional disulfide bonds on the stability and folding of ribonuclease A (2009), Biophys. Chem., 141, 21-28.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
4.6.1.18 A4C/V118C site-directed mutagenesis Bos taurus
4.6.1.18 H105C/V124C site-directed mutagenesis Bos taurus
4.6.1.18 I107C/A122C site-directed mutagenesis Bos taurus
4.6.1.18 M30C/N44C site-directed mutagenesis Bos taurus
4.6.1.18 R10C/R33C site-directed mutagenesis Bos taurus
4.6.1.18 V43C/R85C site-directed mutagenesis Bos taurus

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
4.6.1.18
-
 Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.6.1.18 commercial preparation
-
 Bos taurus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.6.1.18 6-carboxyfluorescein-dArUdAdA-6-carboxytetramethylrhodamine + H2O
-
 Bos taurus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.6.1.18 ribonuclease A
-
 Bos taurus
4.6.1.18 RNase A
-
 Bos taurus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.6.1.18 additional information
-
 The thermal stability of ribonuclease A and its variants is investigated by circular dichroism spectroscopy measurements. Thermal unfolding proves to be reversible and follows a two-state transition model as judged from the fit of the data. While H105C/V124C-ribonuclease A, the variant with the disulfide bond homolog to onconase is as stable as ribonuclease A and A4C/V118C- and V43C/R85C-ribonuclease A are more stable than ribonuclease A, R10C/R33C-, I107C/A122C-, and particularly M30C/N44C-ribonuclease A are destabilized in comparison to ribonuclease A Bos taurus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.6.1.18 12
-
 6-carboxyfluorescein-dArUdAdA-6-carboxytetramethylrhodamine mutant enzyme M30C/N44C Bos taurus
4.6.1.18 1044
-
 6-carboxyfluorescein-dArUdAdA-6-carboxytetramethylrhodamine mutant enzyme I107C/A122C Bos taurus
4.6.1.18 1566
-
 6-carboxyfluorescein-dArUdAdA-6-carboxytetramethylrhodamine mutant enzyme H105C/V124C Bos taurus
4.6.1.18 3132
-
 6-carboxyfluorescein-dArUdAdA-6-carboxytetramethylrhodamine mutant enzyme A4C/V118C Bos taurus
4.6.1.18 3480
-
 6-carboxyfluorescein-dArUdAdA-6-carboxytetramethylrhodamine mutant enzyme V43C/R85C Bos taurus
4.6.1.18 4002
-
 6-carboxyfluorescein-dArUdAdA-6-carboxytetramethylrhodamine mutant enzyme R10C/R33C Bos taurus
4.6.1.18 17400
-
 6-carboxyfluorescein-dArUdAdA-6-carboxytetramethylrhodamine wild-type enzyme Bos taurus