Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Sliwkowski, M.X.; Swaisgood, H.E.; Clare, D.A.; Horton, H.R.
    Kinetic mechanism and specificity of bovine milk sulphydryl oxidase (1984), Biochem. J., 220, 51-55.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.3.2 0.77
-
 O2
-
 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
1.8.3.2 3.16
-
 GSH
-
 Bos taurus

Organism

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

Reaction

EC Number Reaction Comment Organism Reaction ID
1.8.3.2 2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 ter bi substituted mechanism, O2 binds first Bos taurus
a

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
-
 ?