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Literature summary extracted from

  • Stoj, C.S.; Augustine, A.J.; Zeigler, L.; Solomon, E.I.; Kosman, D.J.
    Structural basis of the ferrous iron specificity of the yeast ferroxidase, Fet3p (2006), Biochemistry, 45, 12741-12749.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.16.3.1 residues D283, E185, D409 provide a Fe(II) binding site that favors ferric ion thus reducing the reduction potential of the bound Fe(II). Residues E185 and D409 form part of the electron-transfer pathway from the bound Fe(II) to the protein’s type I Cu(II) Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
1.16.3.1 D283A wild-type reduction potential Saccharomyces cerevisiae
1.16.3.1 D409A increase in reduction potential by 120 mV Saccharomyces cerevisiae
1.16.3.1 E185A wild-type reduction potential Saccharomyces cerevisiae
1.16.3.1 E185A/D409A increase in reduction potential by 120 mV, complete loss of specificity for Fe(II), functions kinetically as an inefficient laccase Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.16.3.1 0.0049
-
 Fe(II) wild-type, pH 6.0 Saccharomyces cerevisiae
1.16.3.1 0.0188
-
 Fe(II) mutant D409A, pH 6.0 Saccharomyces cerevisiae
1.16.3.1 0.0193
-
 Fe(II) mutant D283A, pH 6.0 Saccharomyces cerevisiae
1.16.3.1 0.0356
-
 Fe(II) mutant E185A, pH 6.0 Saccharomyces cerevisiae
1.16.3.1 3.994
-
 Fe(II) mutant E185A/D409A, pH 6.0 Saccharomyces cerevisiae
1.16.3.1 18.2
-
 hydroquinone mutant E185A, pH 6.0 Saccharomyces cerevisiae
1.16.3.1 19.3
-
 hydroquinone mutant D283A, pH 6.0 Saccharomyces cerevisiae
1.16.3.1 25.5
-
 hydroquinone wild-type, pH 6.0 Saccharomyces cerevisiae
1.16.3.1 30.3
-
 hydroquinone mutant D409A, pH 6.0 Saccharomyces cerevisiae
1.16.3.1 30.5
-
 hydroquinone mutant E185A/D409A, pH 6.0 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 residues D283, E185, D409 provide a Fe(II) binding site that favors ferric ion thus reducing the reduction potential of the bound Fe(II). Residues E185 and D409 form part of the electron-transfer pathway from the bound Fe(II) to the protein’s type I Cu(II) Saccharomyces cerevisiae
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.16.3.1 Fe(II) + H+ + O2
-
 Saccharomyces cerevisiae Fe(III) + H2O
-
 ?
1.16.3.1 Fe(II) + hydroquinone + O2
-
 Saccharomyces cerevisiae Fe(III) + ? + H2O
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.16.3.1 0.232
-
 Fe(II) mutant E185A/D409A, pH 6.0 Saccharomyces cerevisiae
1.16.3.1 0.405
-
 Fe(II) mutant E185A, pH 6.0 Saccharomyces cerevisiae
1.16.3.1 0.66
-
 Fe(II) wild-type, pH 6.0 Saccharomyces cerevisiae
1.16.3.1 0.805
-
 Fe(II) mutant D409A, pH 6.0 Saccharomyces cerevisiae
1.16.3.1 1.26
-
 Fe(II) mutant D283A, pH 6.0 Saccharomyces cerevisiae
1.16.3.1 1.53
-
 hydroquinone mutant E185A, pH 6.0 Saccharomyces cerevisiae
1.16.3.1 2.2
-
 hydroquinone wild-type, pH 6.0 Saccharomyces cerevisiae
1.16.3.1 2.3
-
 hydroquinone mutant E185A/D409A, pH 6.0 Saccharomyces cerevisiae
1.16.3.1 2.33
-
 hydroquinone mutant D409A, pH 6.0 Saccharomyces cerevisiae
1.16.3.1 2.81
-
 hydroquinone mutant D283A, pH 6.0 Saccharomyces cerevisiae
1.16.3.1 6.08
-
 Fe(II) mutant D409A, pH 6.0 Saccharomyces cerevisiae