Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.6.1.18 extracted from

  • Klink, T.A.; Raines, R.T.
    Conformational stability is a determinant of ribonuclease A cytotoxicity (2000), J. Biol. Chem., 275, 17463-17467.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Bos taurus

Protein Variants

Protein Variants Comment Organism
G88R mutant with similar thermal stability to wild type enzyme Bos taurus
additional information A4C/G88R/V118C mutant, with a new disulfide bond that links the N and C termini, is more stable to thermal denaturation than wild type and G88R enzymes. The conformational stability of the C40A/G88R/C95A and C65A/C72A/G88R mutants is less than that of G88R. A4C/C65A/C72A/G88R/V118C mutant, with a new disulfide bond is more stable than C65A/C72A/G88R mutant Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
ribonuclease inhibitor
-
Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus P61823
-
-

Source Tissue

Source Tissue Comment Organism Textmining
pancreas
-
Bos taurus
-

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00024
-
ribonuclease inhibitor G88R mutant, pH 6.0, 25ºC Bos taurus
0.00035
-
ribonuclease inhibitor C40A/G88R/C95A mutant, pH 6.0, 25ºC Bos taurus
0.00065
-
ribonuclease inhibitor A4C/G88R/V118C mutant, pH 6.0, 25ºC Bos taurus
0.00078
-
ribonuclease inhibitor C65A/C72A/G88R mutant, pH 6.0, 25ºC Bos taurus
0.0039
-
ribonuclease inhibitor A4C/C65A/C72A/G88R/V118C mutant, pH 6.0, 25ºC Bos taurus