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Literature summary extracted from

  • Brohawn, S.G.; Miksa, I.R.; Thorpe, C.
    Avian sulfhydryl oxidase is not a metalloenzyme: adventitious binding of divalent metal ions to the enzyme (2003), Biochemistry, 42, 11074-11082.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.8.3.2 Cu2+ modeling of metal binding Gallus gallus
1.8.3.2 Zn2+ weak binding to the four-electron-reduced enzyme, rapid inhibition, modeling of metal binding Gallus gallus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.8.3.2 additional information no metalloenzyme Gallus gallus
1.8.3.2 Phosphorus 6.60 atoms per subunit/FAD, cofactor of the FAD Gallus gallus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.3.2 R-SH + O2 Gallus gallus
-
R-S-S-R + H2O2
-
ir

Organism

EC Number Organism UniProt Comment Textmining
1.8.3.2 Gallus gallus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.3.2 from egg white, preparation of apoprotein Gallus gallus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.8.3.2 egg white
-
Gallus gallus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.3.2 dithiothreitol + O2
-
Gallus gallus dithiothreitol disulfide + H2O2
-
ir
1.8.3.2 pancreatic RNase + O2
-
Gallus gallus pancreatic RNase disulfide + H2O2
-
ir
1.8.3.2 R-SH + O2
-
Gallus gallus R-S-S-R + H2O2
-
ir

Synonyms

EC Number Synonyms Comment Organism
1.8.3.2 More enzyme belongs to the sulfhydryl oxidase/Quiescin Q6 family Gallus gallus
1.8.3.2 QSOX
-
Gallus gallus
1.8.3.2 sulfhydryl oxidase
-
Gallus gallus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.8.3.2 25
-
assay at Gallus gallus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.3.2 7.5
-
assay at Gallus gallus

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.3.2 FAD flavoprotein, 1 FAD molecule per enzyme subunit with 1 phosphorus atom per FAD as cofactor of the cofactor Gallus gallus