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 proteins type I Cu(II) | Saccharomyces cerevisiae |
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 |
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 |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.16.3.1 | Saccharomyces cerevisiae | - |
- |
- |
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 proteins type I Cu(II) | Saccharomyces cerevisiae |
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 | - |
? |
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 |