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Literature summary for 1.8.3.2 extracted from

  • Hoober, K.L.; Thorpe, C.
    Flavin-dependent sulfhydryl oxidases in protein disulfide bond formation (2002), Methods Enzymol., 348, 30-34.
    View publication on PubMed
Search for more literature for 1.8.3.2

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.014
-
 RNAse A pH 8.1, 25°C Gallus gallus
0.2
-
 DTT 7.5, 25°C Gallus gallus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular secretion of enzyme Homo sapiens
-
-
extracellular secretion of enzyme Aspergillus niger
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
additional information metalloenzyme Gallus gallus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
R-SH + O2 Gallus gallus
-
 R-S-S-R + H2O2
-
 ir
R-SH + O2 Aspergillus niger
-
 R-S-S-R + H2O2
-
 ir
R-SH + O2 Homo sapiens enzyme might counterbalance the plasmin reductase in extracellular reductive processes R-S-S-R + H2O2
-
 ir

Organism

Organism UniProt Comment Textmining
Aspergillus niger
-
-
-
Gallus gallus
-
-
-
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
from egg white form a riboflavin-binding, protein-deficient strain, several steps Gallus gallus

Reaction

Reaction Comment Organism Reaction ID
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 enzyme contains a functionally involved redox-active motif CXXC Gallus gallus
a

Source Tissue

Source Tissue Comment Organism Textmining
egg white
-
 Gallus gallus
-
fibroblast
-
 Homo sapiens
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 several assay methods are used dependent on the substrate, overview Gallus gallus

Storage Stability

Storage Stability Organism
-20°C, purified enzyme from egg white, in 20 mM Tris buffer, stable for months Gallus gallus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dithiothreitol + O2
-
 Gallus gallus dithiothreitol disulfide + H2O2
-
 ir
additional information preferred substrates are protein or peptide sulfhydryl groups, but not low molecular weight thiols, such as cysteine or glutathione Gallus gallus ?
-
 ?
protein disulfide isomerase + O2 i.e. PDI Gallus gallus protein disulfide isomerase disulfide + H2O2
-
 ir
R-SH + O2
-
 Gallus gallus R-S-S-R + H2O2
-
 ir
R-SH + O2
-
 Aspergillus niger R-S-S-R + H2O2
-
 ir
R-SH + O2 enzyme might counterbalance the plasmin reductase in extracellular reductive processes Homo sapiens R-S-S-R + H2O2
-
 ir
R-SH + O2 oxidation of thiols to disulfides with a concomitant reduction of molecular oxygen to peroxide Gallus gallus R-S-S-R + H2O2
-
 ir
R-SH + O2 oxidation of thiols to disulfides with a concomitant reduction of molecular oxygen to peroxide Homo sapiens R-S-S-R + H2O2
-
 ir
R-SH + O2 oxidation of thiols to disulfides with a concomitant reduction of molecular oxygen to peroxide Aspergillus niger R-S-S-R + H2O2
-
 ir
RNase A + O2
-
 Gallus gallus RNase A disulfide + H2O2
-
 ir
thioredoxin + O2 substrate from Escherichia coli Gallus gallus thioredoxin disulfide + H2O2
-
 ir

Subunits

Subunits Comment Organism
More enzyme contains an N-terminal thioredoxin domain, an intervening domain, and a C-terminal ALR/ERV domain, redox-active motif CXXC Gallus gallus

Synonyms

Synonyms Comment Organism
egg white oxidase
-
 Gallus gallus
More enzyme belongs to the sulfhydryl oxidase/Quiescin Q6 family Gallus gallus
More enzyme belongs to the sulfhydryl oxidase/Quiescin Q6 family Homo sapiens
Quiescin Q6
-
 Homo sapiens
sulfhydryl oxidase
-
 Gallus gallus
sulfhydryl oxidase
-
 Homo sapiens
sulfhydryl oxidase
-
 Aspergillus niger

Cofactor

Cofactor Comment Organism Structure
FAD dependent on Gallus gallus
FAD bound to the enzyme Homo sapiens
FAD bound to the enzyme Aspergillus niger
additional information enzyme contains a redox-active cysteine-bridge Gallus gallus
additional information enzyme contains a redox-active cysteine-bridge Homo sapiens
additional information enzyme contains a redox-active cysteine-bridge Aspergillus niger