Accepted Name |
chloride peroxidase
|
Alternative Name(s) |
chloroperoxidase |
CPO |
vanadium haloperoxidase |
Reaction catalysed |
RH + Cl(-) + H2O2 = RCl + 2 H2O |
Comment(s) |
- Brings about the chlorination of a range of organic molecules,
forming stable C-Cl bonds.
- Also oxidizes bromide and iodide.
- Enzymes of this type are either heme-thiolate proteins, or contain
vanadate.
- A secreted enzyme produced by the ascomycetous fungus Caldariomyces
fumago (Leptoxyphium fumago) is an example of the heme-thiolate type.
- It catalyzes the production of hypochlorous acid by transferring one
oxygen atom from H2O2 to chloride.
- At a separate site it catalyzes the chlorination of activated
aliphatic and aromatic substrates, via HClO and derived chlorine
species.
- In the absence of halides, it shows peroxidase (e.g. phenol
oxidation) and peroxygenase activities.
- The latter inserts oxygen from H2O2 into, for example, styrene (side
chain epoxidation) and toluene (benzylic hydroxylation), however,
these activities are less pronounced than its activity with halides.
- Has little activity with non-activated substrates such as aromatic
rings, ethers or saturated alkanes.
- The chlorinating peroxidase produced by ascomycetous fungi (e.g.
Curvularia inaequalis) is an example of a vanadium chloroperoxidase,
and is related to bromide peroxidase (EC 1.11.1.18).
- It contains vanadate and oxidizes chloride, bromide and iodide into
hypohalous acids.
- In the absence of halides, it peroxygenates organic sulfides and
oxidizes ABTS [2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)]
but no phenols.
|
Cross-references |
BRENDA | 1.11.1.10 |
EC2PDB | 1.11.1.10 |
ExplorEnz | 1.11.1.10 |
PRIAM enzyme-specific profiles | 1.11.1.10 |
KEGG Ligand Database for Enzyme Nomenclature | 1.11.1.10 |
IUBMB Enzyme Nomenclature | 1.11.1.10 |
IntEnz | 1.11.1.10 |
MEDLINE | Find literature relating to 1.11.1.10 |
MetaCyc | 1.11.1.10 |
Rhea expert-curated reactions | 1.11.1.10 |
UniProtKB/Swiss-Prot |
|
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