A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.
ENZYME entry: EC 184.108.40.206
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|RH + Cl(-) + H(2)O(2) <=> RCl + 2 H(2)O|
- 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
- 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 H(2)O(2) to chloride.
- At a separate site it catalyzes the chlorination of activated
aliphatic and aromatic substrates, via HClO and derived chlorine
- In the absence of halides, it shows peroxidase (e.g. phenol
oxidation) and peroxygenase activities.
- The latter inserts oxygen from H(2)O(2) into, for example, styrene
(side chain epoxidation) and toluene (benzylic hydroxylation),
however, these activities are less pronounced than its activity with
- 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 220.127.116.11).
- It contains vanadate and oxidizes chloride, bromide and iodide into
- In the absence of halides, it peroxygenates organic sulfides and
oxidizes ABTS (2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid))
but no phenols.
|PRIAM enzyme-specific profiles||18.104.22.168|
|KEGG Ligand Database for Enzyme Nomenclature||22.214.171.124|
|IUBMB Enzyme Nomenclature||126.96.36.199|
|MEDLINE||Find literature relating to 188.8.131.52|
entries corresponding to 1.11.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.11.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-