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

BRENDA support

Literature summary extracted from

  • Raje, S.; Thorpe, C.
    Inter-domain redox communication in flavoenzymes of the quiescin/sulfhydryl oxidase family: role of a thioredoxin domain in disulfide bond formation (2003), Biochemistry, 42, 4560-4568.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.3.2 0.14
-
 DTT native enzyme, pH 7.5 Gallus gallus
1.8.3.2 12.5
-
 DTT 60 kDa enzyme fragment, pH 7.5 Gallus gallus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.8.3.2 100000
-
 x * 100000, native enzyme, SDS-PAGE 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 oxidation of protein or peptide sulfhydryl groups to disulfides with a concomitant reduction of molecular oxygen to peroxide R-S-S-R + H2O2
-
 ir

Organism

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

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.8.3.2 glycoprotein heavy glycosylation of the 60-kDa-enzyme fragment Gallus gallus

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.3.2 intact enzyme and proteolytically cleaved enzyme in 30 kDa and 60 kDa fragments 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 intact enzyme and 60-kDa-enzyme fragment Gallus gallus dithiothreitol disulfide + H2O2
-
 ir
1.8.3.2 additional information a 30 kDa enzyme fragment shows no catalytic activity of its own Gallus gallus ?
-
 ?
1.8.3.2 R-SH + O2 oxidation of protein or peptide sulfhydryl groups to disulfides with a concomitant reduction of molecular oxygen to peroxide Gallus gallus R-S-S-R + H2O2
-
 ir
1.8.3.2 RNase A + O2 intact enzyme, but not 60-kDa-enzyme fragment Gallus gallus RNase A disulfide + H2O2
-
 ir

Subunits

EC Number Subunits Comment Organism
1.8.3.2 ? x * 100000, native enzyme, SDS-PAGE Gallus gallus
1.8.3.2 More 2 enzyme fragments by partial proteolysis: a 30 kDa nonglycosylated monomeric fragment containing a thioredoxin domain with a CXXC motif, and a 60 kDa glycosylated dimeric fragment with bound FAD and catalytic activity, the latter different from intact enzyme activity Gallus gallus

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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.8.3.2 1013
-
 DTT native enzyme, pH 7.5 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 required for activity, binding domain is located on the 60-kDa-enzyme fragment, electron-transfer mechanism in the native enzyme and the 60 kDA enzyme fragment Gallus gallus