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Literature summary extracted from

  • Arai, K.; Kumakura, F.; Iwaoka, M.
    Characterization of kinetic and thermodynamic phases in the prefolding process of bovine pancreatic ribonuclease A coupled with fast SS formation and SS reshuffling (2010), Biochemistry, 49, 10535-10542.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.6.1.18 additional information
-
 additional information second-order rate constants for disulfide bond formation in the oxidative folding of RNase A with DHSox as an oxidant at 25°C, overview Bos taurus

Organism

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

Source Tissue

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

Synonyms

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

General Information

EC Number General Information Comment Organism
4.6.1.18 additional information analysis of the disulfide bond formation phase in detail in the oxidative folding, as the first of two folding phases, of RNase A, overview. Comparision of folding intermediates of reduced RNase A obtained at 25°C and different pH values from pH 4.0, pH 7.0, to pH 10.0, shuffling and transformation of different intermediate types, overview. The preconformational folding phase coupled with disulfide bond formation can be divided into two distinct subphases, a kinetic (or stochastic) disulfide bond formation phase and a thermodynamic disulfide bond reshuffling phase. The transition from kinetically formed to thermodynamically stabilized disulfide bond intermediates are induced by hydrophobic nucleation as well as generation of the native interactions Bos taurus