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
-
1.11.1.5
-
peroxidases
-
horseradish
-
horse
-
high-spin
-
paramagnetic
-
low-spin
-
ferrous
-
porphyrin
-
ferryl
-
peroxidatic
-
paracoccus
-
iso-1-cytochrome
-
soret
-
electron-transfer
-
ferricytochrome
-
kraut
-
denitrificans
-
ccp1
-
hexacoordinate
-
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
- 1.11.1.5
- peroxidases
- horseradish
- horse
-
high-spin
-
paramagnetic
-
low-spin
-
ferrous
- porphyrin
-
ferryl
-
peroxidatic
- paracoccus
-
iso-1-cytochrome
-
soret
-
electron-transfer
- ferricytochrome
-
kraut
- denitrificans
- ccp1
-
hexacoordinate
-
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
results (
results (Substrates Products
Substrates Products on EC 1.11.1.5 - cytochrome-c peroxidase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
SUBSTRATE 
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
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
?
-
-
-
?
ferrocytochrome c + CN-
?
-
dominant binding pathway for H52L mutant, biphasic reaction
-
-
?
ferrocytochrome c + HCN
?
-
dominant binding pathway for wild-type enzyme
-
-
?
ferrocytochrome c + menadione
ferricytochrome + oxidized menadione
-
menadione can be substituted by 1,4-naphthoquinone
-
-
?
ferrocytochrome c4 + H2O2
ferricytochrome c4 + OH-
-
-
-
?
iso-1 ferrocytochrome c mutant C102T + H2O2
iso-1 ferricytochrome c mutant C102T + 2 H2O
-
-
-
-
?
reduced cytochrome c551 + H2O2
oxidized cytochrome c551 + H2O
-
-
-
-
?
Rhodobacter capsulatus ferrocytochrome c + H2O2
Rhodobacter capsulatus ferricytochrome c + H2O
Rhodobacter capsulatus ferrocytochrome c2 + H2O2
Rhodobacter capsulatus ferricytochrome c2 + H2O
yeast ferrocytochrome c + H2O2
yeast ferricytochrome c + H2O
-
-
-
-
r
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
-
activity with wild-type cytochrome c from Leishmania major and reduced activity with mutant cytochrome c R24A and K98A, no activity with cyt c mutant R24A/K98A
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
-
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
-
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
-
via intermediate compound I formation. The rate-limiting step in CcP compound I formation is the binding of hydrogen peroxide to the heme iron rather than the redox chemistry involved in compound I formation
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
-
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
-
horse cytochrome c
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
-
Pseudomonas aeruginosa cytochrome c-551
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
-
Pseudomonas aeruginosa cytochrome c-551
-
-
?
2,2'-azino-bis(3-ethylenbenzthiazoline-6-sulfonic acid) + H2O2
?
-
-
-
?
2,2'-azino-bis(3-ethylenbenzthiazoline-6-sulfonic acid) + H2O2
?
-
-
-
?
azurin + H2O2
oxidized azurin + ?
-
blue copper protein
-
?
cytochrome c + H2O2
?
-
the reaction with hydrogen peroxide of the W51H/H52L mutant is much slower compared to those of the mutant W51H and W51H/H52W
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
horse heart
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
antioxidant defense
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
antioxidant defense
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
horse heart
-
-
ir
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
horse heart
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
investigation of the catalytic mechanism
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
H2O2 can be substituted by ethyl peroxide
-
-
ir
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
horse heart
-
-
ir
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
H2O2 can be substituted by ethyl peroxide
-
-
ir
ferrocytochrome c + H2O2
ferricytochrome c + H2O
-
horse heart
-
-
ir
ferrocytochrome c551 + H2O2
ferricytochrome c551 + OH-
-
-
-
?
guaiacol + H2O2
2-methoxy-cyclohexa-2,5-dienone + H2O
-
-
-
-
?
guaiacol + H2O2
2-methoxy-cyclohexa-2,5-dienone + H2O
-
-
-
?
horse ferrocytochrome c + H2O2
horse ferricytochrome c + H2O
-
-
-
-
r
horse ferrocytochrome c + H2O2
horse ferricytochrome c + H2O
-
-
-
-
r
horse heart ferrocytochrome c + H2O2
horse heart ferricytochrome c + H2O
-
-
-
-
?
horse heart ferrocytochrome c + H2O2
horse heart ferricytochrome c + H2O
Paracoccidioides brasiliensis Pb01 / ATCC MYA 826
-
-
-
-
?
horse heart ferrocytochrome c + H2O2
horse heart ferricytochrome c + H2O
-
-
-
-
?
horse heart ferrocytochrome c + H2O2
horse heart ferricytochrome c + H2O
-
-
-
-
r
reduced cytochrome c2 + H2O2
oxidized cytochrome c2 + H2O
-
-
-
-
?
reduced horse cytochrome c + H2O2
oxidized horse cytochrome c + H2O
-
-
-
-
?
reduced horse cytochrome c + H2O2
oxidized horse cytochrome c + H2O
-
-
-
-
?
Rhodobacter capsulatus ferrocytochrome c + H2O2
Rhodobacter capsulatus ferricytochrome c + H2O
-
-
-
-
r
Rhodobacter capsulatus ferrocytochrome c + H2O2
Rhodobacter capsulatus ferricytochrome c + H2O
-
-
-
-
r
Rhodobacter capsulatus ferrocytochrome c2 + H2O2
Rhodobacter capsulatus ferricytochrome c2 + H2O
-
-
-
-
r
Rhodobacter capsulatus ferrocytochrome c2 + H2O2
Rhodobacter capsulatus ferricytochrome c2 + H2O
-
-
-
-
r
additional information
?
-
-
Leishmania major peroxidase (LmP) exhibits both ascorbate and cytochrome c peroxidase activities, but cytochrome c is the natural substrate
-
-
?
additional information
?
-
-
Leishmania major cytochrome c has an electropositive surface surrounding the exposed heme edge that serves as the docking site with redox partners. Kinetic assays performed with Leishmania major cytochrome c and the enzyme show that it is a much better substrate for LmP than horse heart cytochrome c
-
-
?
additional information
?
-
-
no oxidation of ferrocytochrome c of bacteria, no mammalian ferrocytochrome b, b5, c1
-
-
?
additional information
?
-
-
Ccp1 functions as a terminal electron acceptor for sulfhydryl oxidase Erv1
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
formation of a covalent link from Trp51 to the heme on reaction with H2O2
-
-
?
additional information
?
-
investigation of an engineered channel mutant with the surrogate peptide (N-benzimidazole-propionic acid)-Gly-Ala-Ala (BzGAA), complete loss of functional activity in the BzGAA/ET channel mutant strongly supports proposals that the Trp-191 radical intermediate is required for efficient turnover of cyt c via the proposed ET pathway
-
-
?
additional information
?
-
-
residues Tyr71 and Tyr236 contribute primarily to the EPR spectrum of the tyrosyl radical. The heme distal-side Trp51 is involved in the intramolecular electron transfer between Tyr71 and the heme and formation of Tyr71 and Tyr236 radicals is independent of the [Fe(IV)=O Trp191+] radical intermediate. Tyr71 radical is the reactive species with the guaiacol substrate. Surface-exposed residue Tyr236 is the other radical site
-
-
?
additional information
?
-
-
no oxidation of ferrocytochrome c of bacteria, no mammalian ferrocytochrome b, b5, c1
-
-
?
additional information
?
-
-
menaquinol pool-based origin of electrons that are transferred to CcpA
-
-
?
additional information
?
-
the rate-limiting step involves a proton-coupled single electron reduction of a high valent iron species centered on the low-potential heme. Reduction shifts the pKa's of at least two amino acids. Loop 1 shifts during the rate-limiting step, changing the environment of residue His81
-
-
?
additional information
?
-
-
the rate-limiting step involves a proton-coupled single electron reduction of a high valent iron species centered on the low-potential heme. Reduction shifts the pKa's of at least two amino acids. Loop 1 shifts during the rate-limiting step, changing the environment of residue His81
-
-
?
