Peroxidase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
Symbol | peroxidase | ||||||||
Pfam | PF00141 | ||||||||
InterPro | IPR002016 | ||||||||
PROSITE | PDOC00394 | ||||||||
SCOP2 | 1hsr / SCOPe / SUPFAM | ||||||||
CDD | cd00314 | ||||||||
|
Fungal peroxidase extension region | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
Symbol | Peroxidase_ext | ||||||||
Pfam | PF11895 | ||||||||
InterPro | IPR024589 | ||||||||
|
Haem peroxidases (or heme peroxidases) are haem-containing enzymes that use hydrogen peroxide as the electron acceptor to catalyse a number of oxidative reactions. Most haem peroxidases follow the reaction scheme:
In this mechanism, the enzyme reacts with one equivalent of H2O2 to give [Fe4+=O]R' (compound I). This is a two-electron oxidation/reduction reaction in which H2O2 is reduced to water, and the enzyme is oxidized. One oxidizing equivalent resides on iron, giving the oxyferryl [1] intermediate, and in many peroxidases the porphyrin (R) is oxidized to the porphyrin pi-cation radical (R'). Compound I then oxidizes an organic substrate to give a substrate radical [2] and Compound II, which can then oxidize a second substrate molecule.
Haem peroxidases include two superfamilies: one found in bacteria, fungi, and plants, and the second found in animals. The first one can be viewed as consisting of 3 major classes: [3]
The crystal structures of a number of these proteins show that they share the same architecture - two all-alpha domains between which the haem group is embedded.
Another family of haem peroxidases is the DyP-type peroxidase family. [8]
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Peroxidase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
Symbol | peroxidase | ||||||||
Pfam | PF00141 | ||||||||
InterPro | IPR002016 | ||||||||
PROSITE | PDOC00394 | ||||||||
SCOP2 | 1hsr / SCOPe / SUPFAM | ||||||||
CDD | cd00314 | ||||||||
|
Fungal peroxidase extension region | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
Symbol | Peroxidase_ext | ||||||||
Pfam | PF11895 | ||||||||
InterPro | IPR024589 | ||||||||
|
Haem peroxidases (or heme peroxidases) are haem-containing enzymes that use hydrogen peroxide as the electron acceptor to catalyse a number of oxidative reactions. Most haem peroxidases follow the reaction scheme:
In this mechanism, the enzyme reacts with one equivalent of H2O2 to give [Fe4+=O]R' (compound I). This is a two-electron oxidation/reduction reaction in which H2O2 is reduced to water, and the enzyme is oxidized. One oxidizing equivalent resides on iron, giving the oxyferryl [1] intermediate, and in many peroxidases the porphyrin (R) is oxidized to the porphyrin pi-cation radical (R'). Compound I then oxidizes an organic substrate to give a substrate radical [2] and Compound II, which can then oxidize a second substrate molecule.
Haem peroxidases include two superfamilies: one found in bacteria, fungi, and plants, and the second found in animals. The first one can be viewed as consisting of 3 major classes: [3]
The crystal structures of a number of these proteins show that they share the same architecture - two all-alpha domains between which the haem group is embedded.
Another family of haem peroxidases is the DyP-type peroxidase family. [8]
{{
cite journal}}
: Cite journal requires |journal=
(
help)
{{
cite journal}}
: Cite journal requires |journal=
(
help)