1.11.1.10: chloride peroxidase
This is an abbreviated version!
For detailed information about chloride peroxidase, go to the full flat file.
Word Map on EC 1.11.1.10
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1.11.1.10
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fumago
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caldariomyces
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horseradish
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chlorination
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peroxidases
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halogen
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halide
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haloperoxidase
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bromination
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lactoperoxidase
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inaequalis
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ferryl
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curvularia
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soret
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bromoperoxidase
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monochlorodimedone
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low-spin
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p450cam
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vanadium-dependent
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thioanisole
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peroxidase-catalyzed
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thiolate-ligated
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pyrrocinia
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oxoferryl
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n,n-dimethylaniline
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peroxygenases
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agrocybe
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vanadium-containing
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hypohalous
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aegerita
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degradation
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synthesis
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environmental protection
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biotechnology
- 1.11.1.10
- fumago
-
caldariomyces
- horseradish
-
chlorination
- peroxidases
-
halogen
- halide
- haloperoxidase
-
bromination
- lactoperoxidase
- inaequalis
-
ferryl
-
curvularia
-
soret
-
bromoperoxidase
- monochlorodimedone
-
low-spin
-
p450cam
-
vanadium-dependent
- thioanisole
-
peroxidase-catalyzed
-
thiolate-ligated
- pyrrocinia
-
oxoferryl
- n,n-dimethylaniline
-
peroxygenases
-
agrocybe
-
vanadium-containing
-
hypohalous
- aegerita
- degradation
- synthesis
- environmental protection
- biotechnology
Reaction
Synonyms
CCPO, Chloride peroxidase, chloroperoxidase, chloroproxidase, CPO, CPO-I, CPO2, haeme-thiolate peroxidase, heme-containing CPO, heme-thiolate chloroperoxidase, More, peroxidase, chloride, Vanadium chloride peroxidase, vCPO
ECTree
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Cofactor
Cofactor on EC 1.11.1.10 - chloride peroxidase
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heme
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heme
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binding of the para-substituted phenolic compounds close to the heme
heme
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the enzyme functions without reduction to the ferrous state. Instead, peroxide addition of the ferric enzyme produces an iron-oxo species that reacts with chloride to effect chlorination. Evidence for a sulfur donor axial ligand trans to dioxygen, iron-sulfur bond distance of 2.37 A
heme
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formation and decay of hydroperoxo-ferric intermediate in CPO via an oxygenase/oxidase pathway is documented
heme
the heme group of CPO is nonplanar and saddle, with the iron positioned under the main plane of the porphyrin toward the Cys29 ligand. The distal pocket of the heme group in CPO is polar. In the peroxidases, the edge of the heme group is open for the reaction with the substrate, while the direct access to its Fe4+ =O center is limited
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the enzyme does not require any cofactor for its activity
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additional information
the CPO prosthetic group is Fe (IV) protoporphyrin
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additional information
the enzyme involves the protoporphyrin prosthetic group with the pI range of 3.2-4.0
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