Literature summary extracted from

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

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
4.6.1.18	expression in Escherichia coli	Bos taurus

Protein Variants

EC Number	Protein Variants	Comment	Organism
4.6.1.18	G88R	mutant with similar thermal stability to wild type enzyme	Bos taurus
4.6.1.18	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

EC Number	Inhibitors	Comment	Organism	Structure
4.6.1.18	ribonuclease inhibitor	-	Bos taurus

Organism

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

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
4.6.1.18	pancreas	-	Bos taurus	-

Ki Value [mM]

EC Number	Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
4.6.1.18	0.00024	-	ribonuclease inhibitor	G88R mutant, pH 6.0, 25ºC	Bos taurus
4.6.1.18	0.00035	-	ribonuclease inhibitor	C40A/G88R/C95A mutant, pH 6.0, 25ºC	Bos taurus
4.6.1.18	0.00065	-	ribonuclease inhibitor	A4C/G88R/V118C mutant, pH 6.0, 25ºC	Bos taurus
4.6.1.18	0.00078	-	ribonuclease inhibitor	C65A/C72A/G88R mutant, pH 6.0, 25ºC	Bos taurus
4.6.1.18	0.0039	-	ribonuclease inhibitor	A4C/C65A/C72A/G88R/V118C mutant, pH 6.0, 25ºC	Bos taurus

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Release 2023.1 (January 2023)