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Literature summary for 1.8.3.2 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
Search for more literature for 1.8.3.2

Inhibitors

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

KM Value [mM]

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

Localization

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

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
milk
-
 Bos taurus
-

Substrates and Products (Substrate)

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