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Literature summary extracted from

  • Quintanar, L.; Gebhard, M.; Wang, T.P.; Kosman, D.J.; Solomon, E.I.
    Ferrous binding to the multicopper oxidases Saccharomyces cerevisiae Fet3p and human ceruloplasmin: Contributions to Ferroxidase Activity (2004), J. Am. Chem. Soc., 126, 6579-6589.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.16.3.1 E185A CD and MCD spectra similar to wild-type Saccharomyces cerevisiae
1.16.3.1 E185D 2.8 atoms of Cu per protein, CD and MCD spectra similar to wild-type Saccharomyces cerevisiae
1.16.3.1 Y354A 2.8 atoms of Cu per protein, CD and MCD spectra similar to wild-type Saccharomyces cerevisiae
1.16.3.1 Y354F CD and MCD spectra similar to wild-type Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.16.3.1 3
-
 hydroquinone wild-type, pH 6.5, 25°C Saccharomyces cerevisiae
1.16.3.1 3
-
 Fe2+ wild-type, pH 6.5, 4°C Saccharomyces cerevisiae
1.16.3.1 4.6
-
 hydroquinone mutant Y354A, pH 6.5, 25°C Saccharomyces cerevisiae
1.16.3.1 4.6
-
 Fe2+ mutant Y354A, pH 6.5, 4°C Saccharomyces cerevisiae
1.16.3.1 8.2
-
 hydroquinone mutant E185D, pH 6.5, 25°C Saccharomyces cerevisiae
1.16.3.1 8.2
-
 Fe2+ mutant E185D, pH 6.5, 4°C Saccharomyces cerevisiae
1.16.3.1 12.7
-
 hydroquinone mutant Y354F, pH 6.5, 25°C Saccharomyces cerevisiae
1.16.3.1 12.7
-
 Fe2+ mutant Y354F, pH 6.5, 4°C Saccharomyces cerevisiae
1.16.3.1 14.1
-
 hydroquinone mutant E185A, pH 6.5, 25°C Saccharomyces cerevisiae
1.16.3.1 14.1
-
 Fe2+ mutant E185A, pH 6.5, 4°C Saccharomyces cerevisiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.16.3.1 Cu 4 atoms per protein Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
1.16.3.1 Saccharomyces cerevisiae
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.16.3.1 4 Fe(II) + 4 H+ + O2 = 4 Fe(III) + 2 H2O iron binding site plays a major role in tuning the reduction potenzial of iron to provide a large driving force for the reaction, E185 residue provides the dominant electron transfer pathway to the T1 Cu site Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.16.3.1 hydroquinone + Fe2+ + O2
-
 Saccharomyces cerevisiae ?
-
 ?