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Literature summary extracted from

  • Janolino, V.G.; Swaisgood, H.E.
    Sulfhydryl oxidase-catalyzed formation of disulfide bonds in reduced ribonuclease (1987), Arch. Biochem. Biophys., 258, 265-271.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.8.3.2 ribonuclease substrate inhibition above 0.04 mM Bos taurus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.3.2 0.0174
-
 Reduced ribonuclease corresponds to a sulfhydryl concentration of 0.14 mM Bos taurus
1.8.3.2 0.805
-
 L-Cys
-
 Bos taurus
1.8.3.2 0.966
-
 L-Cys
-
 Bos taurus
1.8.3.2 1.13
-
 N-acetyl-L-Cys
-
 Bos taurus
1.8.3.2 1.25
-
 cysteamine
-
 Bos taurus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.8.3.2 vesicular fraction
-
 Bos taurus
-
-

Organism

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.8.3.2 milk
-
 Bos taurus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.3.2 cysteamine + O2
-
 Bos taurus ? + H2O
-
 ?
1.8.3.2 D-Cys + O2
-
 Bos taurus ? + H2O
-
 ?
1.8.3.2 GSH + O2 + O2
-
 Bos taurus GSSG + H2O
-
 ?
1.8.3.2 L-Cys + O2
-
 Bos taurus ? + H2O
-
 ?
1.8.3.2 N-acetylcysteine + O2
-
 Bos taurus ? + H2O
-
 ?
1.8.3.2 reduced ribonuclease + O2
-
 Bos taurus ribonuclease + H2O
-
 r
1.8.3.2 reductively denatured ribonuclease A + O2
-
 Bos taurus renatured ribonuclease + H2O
-
 ?