EC Number   |
Reaction |
Reference |
|---|
   1.11.1.16 | 1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 4-hydroxy-3-methoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H2O |
(1) |
- |
| 1.11.1.16 | 1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 4-hydroxy-3-methoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H2O |
NMR study of enzyme both in resting state and cyanide-inhibited form. Analysis of interaction with Mn2+ |
665753 |
| 1.11.1.16 | 1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 4-hydroxy-3-methoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H2O |
study of reaction of H2O2 with the enzyme in the absence of substrate suggests an amino acid radical in moderate distance from ferryl heme. A tryptophan radical is formed during the catalytic mechanism |
664101 |
| 1.11.1.16 | 1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 4-hydroxy-3-methoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H2O |
the radical intermediate in the reaction of enzyme with H2O2 is a tryptophan neutral radical at W164 |
665749 |
| 1.11.1.16 | 2 manganese(II) + 2 H+ + H2O2 = 2 manganese(III) + 2 H2O |
(2) |
- |
| 1.11.1.16 | 2 manganese(II) + 2 H+ + H2O2 = 2 manganese(III) + 2 H2O |
at the ferric resting state, heme peroxidases are first activated by a single molecule of H2O2 to yield an oxidized catalytic intermediate called compound I (oxoferryl IV porphyrin p-cation radical), releasing one molecule of water as the only by-product. The enzyme then catalyzes two consecutive one-electron oxidations of two reducing substrates, regenerating the ground reduced state through a second catalytic intermediate called compound II (oxoferryl) and with the concomitant production of a second molecule of water. The main limiting step within this catalytic cycle is the low conversion rate from compound II to the ground state, which allows the former to accumulate and react with a new molecule of H2O2, either in the presence (with an excess of H2O2) or absence (at catalytic concentrations of H2O2) of the reducing substrate |
764058 |
| 1.11.1.16 | 2 manganese(II) + 2 H+ + H2O2 = 2 manganese(III) + 2 H2O |
the versatile peroxidase catalytic mechanism is similar to classic peroxidases, in which substrate oxidation is carried out by a two-electron multistep reaction at the expense of hydrogen peroxide. Versatile peroxidases oxidize Mn2+ (as MnP), degrade the lignin model dimer veratryl glycerol-guaiacylether to yield veratraldehyde, and oxidize veratryl alcohol and dimethoxybenzene to veratraldehyde and p-benzoquinone, respectively |
-, 765635 |
