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Literature summary for 4.6.1.18 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
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
 Bos taurus
-
pancreas
-
 Bos taurus
-

Synonyms

Synonyms Comment Organism
pancreatic ribonuclease A
-
 Bos taurus
RNase A
-
 Bos taurus

General Information

General Information Comment Organism
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