1.11.1.5: cytochrome-c peroxidase
This is an abbreviated version!
For detailed information about cytochrome-c peroxidase, go to the full flat file.
Word Map on EC 1.11.1.5
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1.11.1.5
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peroxidases
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horseradish
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horse
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high-spin
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paramagnetic
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low-spin
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ferrous
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porphyrin
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ferryl
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peroxidatic
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paracoccus
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iso-1-cytochrome
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soret
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electron-transfer
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ferricytochrome
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kraut
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denitrificans
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ccp1
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hexacoordinate
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oxyferryl
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katgs
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catalase-peroxidase
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poulos
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pentacoordinate
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chrysosporium
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interprotein
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intracomplex
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five-coordinate
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high-potential
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ferrocyanide
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phanerochaete
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low-potential
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six-coordinate
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azurin
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pi-cation
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chloroperoxidase
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protoheme
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5-coordinate
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half-reduced
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pantotrophus
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nitrosomonas
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hyperfine-shifted
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metmyoglobins
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biotechnology
- 1.11.1.5
- peroxidases
- horseradish
- horse
-
high-spin
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paramagnetic
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low-spin
-
ferrous
- porphyrin
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ferryl
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peroxidatic
- paracoccus
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iso-1-cytochrome
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soret
-
electron-transfer
- ferricytochrome
-
kraut
- denitrificans
- ccp1
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hexacoordinate
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oxyferryl
-
katgs
- catalase-peroxidase
-
poulos
-
pentacoordinate
- chrysosporium
-
interprotein
-
intracomplex
-
five-coordinate
-
high-potential
- ferrocyanide
-
phanerochaete
-
low-potential
-
six-coordinate
- azurin
-
pi-cation
- chloroperoxidase
- protoheme
-
5-coordinate
-
half-reduced
- pantotrophus
- nitrosomonas
-
hyperfine-shifted
- metmyoglobins
- biotechnology
Reaction
2 ferrocytochrome c
+
Synonyms
apocytochrome c peroxidase, BCcP, CCP, CCP1, CcpA, Cjj0382, CytC, cytochrome c iso-1, cytochrome c peroxidase, cytochrome c-551 peroxidase, cytochrome c-H2O oxidoreductase, cytochrome peroxidase, di-heme cytochrome c peroxidase, diheme cytochrome c peroxidase, diheme cytochrome c5 peroxidase CcpA, DocA, LmP, MacA, mesocytochrome c peroxidase azide, mesocytochrome c peroxidase cyanate, mesocytochrome c peroxidase cyanide, peroxidase, cytochrome c, Psa CcP
ECTree
1.11.1.5 cytochrome-c peroxidaseAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 1.11.1.5 - cytochrome-c peroxidase
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
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-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
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-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
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-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
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-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
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-
-
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?
additional information
?
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Leishmania major peroxidase (LmP) exhibits both ascorbate and cytochrome c peroxidase activities, but cytochrome c is the natural substrate
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-
?
additional information
?
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investigation of the binding hot-spot residue Y39 in the weak protein complex of physiological redox partners yeast iso-1-cytochrome c and cytochrome c peroxidase, cytochrome c and cytochrome c peroxidase binding parameters
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?
additional information
?
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investigation of the binding hot-spot residue Y39 in the weak protein complex of physiological redox partners yeast iso-1-cytochrome c and cytochrome c peroxidase, cytochrome c and cytochrome c peroxidase binding parameters
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?
additional information
?
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menaquinol pool-based origin of electrons that are transferred to CcpA
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-
?
