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
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high-spin
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paramagnetic
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low-spin
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ferrous
- porphyrin
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ferryl
-
peroxidatic
- paracoccus
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iso-1-cytochrome
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soret
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electron-transfer
- ferricytochrome
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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
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pi-cation
- chloroperoxidase
- protoheme
-
5-coordinate
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half-reduced
- pantotrophus
- nitrosomonas
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hyperfine-shifted
- metmyoglobins
- biotechnology
Reaction
2 ferrocytochrome c + + 2 H+ = + 2 H2O
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
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Subunits
Subunits on EC 1.11.1.5 - cytochrome-c peroxidase
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dimer
heterodimer
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SDS-PAGE, H2O2 oxidation induces heterodimerization between cytochrome c and both wild-type and W191F enzymes, but not with W51F mutant
homodimer
monomer
monomer or dimer
additional information
dimer
Marinobacter nauticus
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the dimer is stabilized by hydrophobic interactions between both C-terminal coiled coils of the two monomers. There are also hydrophobic interactions among residues 39-66. The presence of Ca2+ triggers conformational changes, which contribute to stronger interactions within the dimer
dimer
Marinobacter nauticus 617
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2 * 36500, SDS-PAGE
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with no addition of Ca2+, the monomer/dimer ratio is shifted toward the monomeric form, sedimentation equilibrium analysis
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the enzyme exhibits a monomer-dimer equilibrium that is dependent not only on the presence of calcium ions but also on pH, ionic strength, and protein concentration
monomer or dimer
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the enzyme exhibits a monomer-dimer equilibrium that is dependent not only on the presence of calcium ions but also on pH, ionic strength, and protein concentration
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dimerization of wild-type enzyme is observed at H2O2/enzyme ratios of 3 and 10. W191F mutant dimerizes irrespectively of the H2O2/enzyme ratio. W51F mutant exhibits extensive dimerization on H2O2 oxidation and formation of higher molecular weight polymeric species indicating nonspecific crosslinking
additional information
three-dimensional structure of MacA by molecular replacement, model building, overview
additional information
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three-dimensional structure of MacA by molecular replacement, model building, overview
additional information
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three-dimensional structure of MacA by molecular replacement, model building, overview
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additional information
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expression of two protein after induction of the enzyme expression, 45000 Da and 47000 Da, SDS-PAGE. The 45000 Da protein is solubilized in 0.1% sodium deoxycholate, which indicates that the protein is only loosely associated with the membrane. The 47000 Da protein is probably initially synthesized with a signal peptide that is later cleaved
additional information
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in the presence of added Ca2+ or higher protein concentrations, the enzyme partially shifts to a higher state of aggregation, presumably tetramer
additional information
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pair of dimers related by local dyads. Functional dimers can dimerize
additional information
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recombinant His-tagged enzyme is used for structure analysis by multidimensional NMR spectroscopy, structure modeling, overview
additional information
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CcpA three-dimensional structure analysis, overview