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 (KM Value
KM Value 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
KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.0113
2,2-azinobis(3-ethylbenzthiazolinesulfonic acid)
-
pH 7.5, temperature not specified in the publication
0.71
ascorbate
wild-type cytochrome c peroxidase, pH 6.0, 25°C
93
cytochrome c
wild-type cytochrome c peroxidase, pH 6.0, 25°C
100
cytochrome c
mutant W191F, pH 6.0, 25°C, the W191F mutation dramatically reduces the activity toward cytochrome c, but in the other variants which do not contain the W191F mutation the activity toward cytochrome c is largely unaffected
0.002
ferrocytochrome c
-
recombinant wild-type, pH 7.5, 25°C, 100 mM phosphate buffer
0.0041
ferrocytochrome c
-
horse heart, with electron acceptor ethyl peroxide
0.0041
ferrocytochrome c
-
horse heart, with electron acceptor ethyl peroxide
0.0045
ferrocytochrome c
-
horse heart, with electron acceptor H2O2
0.008
ferrocytochrome c
-
wild-type substrate, pH and temperature not specified in the publication
0.01
ferrocytochrome c
-
DELTA10 deltion mutant substrate, pH and temperature not specified in the publication
0.011
ferrocytochrome c
-
covalent complex of mutant E290C, pH 7.5, 25°C, 100 mM phosphate buffer. Activity is due to unreacted enzyme copurifying with the complex
0.02
ferrocytochrome c
-
R24A substrate mutant, pH and temperature not specified in the publication
0.023
ferrocytochrome c
-
yeast, with electron acceptor ethyl peroxide
0.023
ferrocytochrome c
-
yeast, with electron acceptor ethyl peroxide
0.04
ferrocytochrome c
-
K98A substrate mutant, pH and temperature not specified in the publication
0.047
ferrocytochrome c
-
recombinant wild-type, pH 7.5, 25°C, 10 mM phosphate buffer
0.13
ferrocytochrome c
-
covalent complex of mutant E290C, pH 7.5, 25°C, 10 mM phosphate buffer. Activity is due to unreacted enzyme copurifying with the complex
14
guaiacol
mutant Y36A/N184R/W191F, pH 6.0, 25°C, guaiacol oxidation is not significantly affected by any of the mutations, including W191F, which is consistent with the idea that aromatic substrates such as guaiacol bind at a separate location close to the delta-heme edge and is clearly indicative of a different electron transfer pathway for the oxidation of these types of aromatic substrate
0.025
H2O2
protein film voltammetry, the midpoint potentials of the turnover signals are used to calculate Michaelis-Menten kinetics
0.042
horse heart ferrocytochrome c
-
bulk solution, 50 mM NaCl, at pH 7.0
-
0.066
horse heart ferrocytochrome c
-
membrane solution, 50 mM NaCl, at pH 7.0
-
0.0019
iso-1 ferrocytochrome c
-
mutant enzyme D210K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
0.002
iso-1 ferrocytochrome c
-
mutant enzyme D18K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
0.0021
iso-1 ferrocytochrome c
-
recombinant wild type enzyme, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
0.0023
iso-1 ferrocytochrome c
-
mutant enzyme E17K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
0.0024
iso-1 ferrocytochrome c
-
mutant enzyme D33K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
0.0028
iso-1 ferrocytochrome c
-
mutant enzyme E209K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
0.0029
iso-1 ferrocytochrome c
-
mutant enzyme E201K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
0.0031
iso-1 ferrocytochrome c
-
mutant enzyme E98K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
0.0035
iso-1 ferrocytochrome c
-
mutant enzyme E35K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
0.0038
iso-1 ferrocytochrome c
-
mutant enzyme E291K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
0.0045
iso-1 ferrocytochrome c
-
mutant enzyme E32K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
0.051
iso-1 ferrocytochrome c
-
mutant enzyme E118K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
0.06
iso-1 ferrocytochrome c
-
mutant enzyme E290K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
0.082
iso-1 ferrocytochrome c
-
mutant enzyme D37K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
0.1
iso-1 ferrocytochrome c
-
Km above 0.1 mM, mutant enzyme D34K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
0.1
iso-1 ferrocytochrome c
-
Km above 0.1 mM, mutant enzyme R31E, in 0.1 M potassium phosphate buffer, pH 7.5, at 25°C
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Rhodobacter capsulatus cytochrome c2 is slowly oxidized by peroxide in absence of presumed enzyme
-
additional information
additional information
-
Michaelis-Menten kinetics, overview
-
additional information
additional information
-
Michaelis-Menten steady-state kinetics with wild-type and mutant Leishmania major cytochrome c, overview. Comparison with kinetic of the enzyme from Saccharomyces cerevisiae
-
additional information
additional information
-
steady-state and transient kinetics, stopped-flow kinetics at pH 4.0 and pH 8.0 at 0.10 M ionic strength, 25 °C
-
