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Literature summary for 1.16.3.1 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
Search for more literature for 1.16.3.1

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Protein Variants Comment Organism
D283A wild-type reduction potential Saccharomyces cerevisiae
D409A increase in reduction potential by 120 mV Saccharomyces cerevisiae
E185A wild-type reduction potential Saccharomyces cerevisiae
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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0049
-
 Fe(II) wild-type, pH 6.0 Saccharomyces cerevisiae
0.0188
-
 Fe(II) mutant D409A, pH 6.0 Saccharomyces cerevisiae
0.0193
-
 Fe(II) mutant D283A, pH 6.0 Saccharomyces cerevisiae
0.0356
-
 Fe(II) mutant E185A, pH 6.0 Saccharomyces cerevisiae
3.994
-
 Fe(II) mutant E185A/D409A, pH 6.0 Saccharomyces cerevisiae
18.2
-
 hydroquinone mutant E185A, pH 6.0 Saccharomyces cerevisiae
19.3
-
 hydroquinone mutant D283A, pH 6.0 Saccharomyces cerevisiae
25.5
-
 hydroquinone wild-type, pH 6.0 Saccharomyces cerevisiae
30.3
-
 hydroquinone mutant D409A, pH 6.0 Saccharomyces cerevisiae
30.5
-
 hydroquinone mutant E185A/D409A, pH 6.0 Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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
a

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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