Information 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.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
1.11.1.5
-
RECOMMENDED NAME
GeneOntology No.
cytochrome-c peroxidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2 ferrocytochrome c + H2O2 = 2 ferricytochrome c + 2 H2O
show the reaction diagram
reaction scheme
-
2 ferrocytochrome c + H2O2 = 2 ferricytochrome c + 2 H2O
show the reaction diagram
kinetics, energy, catalysis information
-
2 ferrocytochrome c + H2O2 = 2 ferricytochrome c + 2 H2O
show the reaction diagram
kinetics
-
2 ferrocytochrome c + H2O2 = 2 ferricytochrome c + 2 H2O
show the reaction diagram
the enzyme uses hydrogen peroxide as an electron acceptor to oxidize cytochrome c. The enzyme is not essential for both cell viability and respiration. Its biological function is to reduce H2O2 generated during aerobic respiratory process. The enzyme may also act as a peroxynitrite scavenger
-
2 ferrocytochrome c + H2O2 = 2 ferricytochrome c + 2 H2O
show the reaction diagram
pseudo-first-order kinetics
-
2 ferrocytochrome c + H2O2 = 2 ferricytochrome c + 2 H2O
show the reaction diagram
only ferrocytochrome c bound at the Pelletier-Kraut site of enzyme is oxidized during turnover
-
2 ferrocytochrome c + H2O2 = 2 ferricytochrome c + 2 H2O
show the reaction diagram
the intermediate Compound I forms once H2O2 is heterolytically cleaved, releasing a water molecule. The remaining O atom oxidizes the heme iron to Fe(IV) and an organic moiety to a cation radical. For most heme peroxidases, this moiety is the porphyrin ring. Upon two electron transfer events from two substrate molecules, the enzyme returns to the resting state with water occupying the active site
-
2 ferrocytochrome c + H2O2 = 2 ferricytochrome c + 2 H2O
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ferrocytochrome-c:hydrogen-peroxide oxidoreductase
A hemoprotein.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
apocytochrome c peroxidase
-
-
-
-
CCP
-
-
-
-
CCP
Campylobacter jejuni 81-176
-
-
-
CCP
Marinobacter hydrocarbonoclasticus 617
-
-
-
CCP
Paracoccidioides brasiliensis Pb01
-
-
-
CCP
Paracoccus pantotrophus LMD 52.44
-
-
-
CCP
Q5NNF0
-
CcpA
Q749D0
bacterial di-heme cytochrome c peroxidase
Cjj0382
-
putative cytochrome c peroxidase
Cjj0382
Campylobacter jejuni 81-176
-
putative cytochrome c peroxidase
-
CytC
Q5NNF0
gene name
cytochrome c peroxidase
-
-
-
-
cytochrome c peroxidase
-
-
cytochrome c peroxidase
Q749D0
-
cytochrome c peroxidase
-
-
cytochrome c peroxidase
-
-
cytochrome c peroxidase
Paracoccus pantotrophus LMD 52.44
-
-
-
cytochrome c peroxidase
-
-
cytochrome c peroxidase
P00431
-
cytochrome c peroxidase
Saccharomyces cerevisiae Red Star
-
-
-
cytochrome c peroxidase
-
-
cytochrome c peroxidase
Q5NNF0
-
cytochrome c-551 peroxidase
-
-
-
-
cytochrome c-H2O oxidoreductase
-
-
-
-
cytochrome peroxidase
-
-
-
-
di-heme cytochrome c peroxidase
-
-
diheme cytochrome c peroxidase
-
-
diheme cytochrome c peroxidase
-
-
DocA
-
putative cytochrome c peroxidase
DocA
Campylobacter jejuni 81-176
-
putative cytochrome c peroxidase
-
MacA
Geobacter sulfurreducens DSM 12127
Q74FY6
-
-
mesocytochrome c peroxidase azide
-
-
-
-
mesocytochrome c peroxidase cyanate
-
-
-
-
mesocytochrome c peroxidase cyanide
-
-
-
-
peroxidase, cytochrome c
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9029-53-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain 81-176
-
-
Manually annotated by BRENDA team
Campylobacter jejuni 81-176
strain 81-176
-
-
Manually annotated by BRENDA team
strain H99
SwissProt
Manually annotated by BRENDA team
Cryptococcus neoformans H99
strain H99
SwissProt
Manually annotated by BRENDA team
gene macA, i.e. gsu0466
UniProt
Manually annotated by BRENDA team
Geobacter sulfurreducens DSM 12127
gene macA, i.e. gsu0466
UniProt
Manually annotated by BRENDA team
strain 617; strain 617, microaerophilically grown
-
-
Manually annotated by BRENDA team
Marinobacter hydrocarbonoclasticus 617
strain 617; strain 617, microaerophilically grown
-
-
Manually annotated by BRENDA team
enzyme expression is regulated by the availabilty of copper
SwissProt
Manually annotated by BRENDA team
strain Pb01 (ATCC-MYA-826)
-
-
Manually annotated by BRENDA team
Paracoccidioides brasiliensis Pb01
strain Pb01 (ATCC-MYA-826)
-
-
Manually annotated by BRENDA team
also Paracoccus pantotrophus
-
-
Manually annotated by BRENDA team
strain A.T.C.C. 19367, N.C.I.B. 8944, L.M.D. 52.44
-
-
Manually annotated by BRENDA team
strain LMD 52.44
-
-
Manually annotated by BRENDA team
Paracoccus pantotrophus LMD 52.44
strain LMD 52.44
-
-
Manually annotated by BRENDA team
white rot fungus
-
-
Manually annotated by BRENDA team
strain 9721
-
-
Manually annotated by BRENDA team
Pseudomonas stutzeri 9721
strain 9721
-
-
Manually annotated by BRENDA team
Rhodobacter capsulatus B10
strain B10
-
-
Manually annotated by BRENDA team
bakers yeast
-
-
Manually annotated by BRENDA team
bakers yeast
-
-
Manually annotated by BRENDA team
recombinant enzyme
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae Red Star
-
-
-
Manually annotated by BRENDA team
gene SO2178
-
-
Manually annotated by BRENDA team
gene ZmcytC
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
Q74FY6
MacA belongs to the family of diheme cytochrome c peroxidases
evolution
Geobacter sulfurreducens DSM 12127
-
MacA belongs to the family of diheme cytochrome c peroxidases
-
malfunction
-
while the wild-type CcP is very stable to oxidative degradation by excess hydrogen peroxide, CcP mutant R48A/W51A/H52A is inactivated within four cycles of the peroxygenase reaction
malfunction
-
significantly higher H2O2 accumulation in ccp1-null cells and catalytically inactive Ccp1W191F mutant cells. Ccp1W191F is a more persistent H2O2 signaling protein than wild-type Ccp1
malfunction
Q5NNF0, -
an enzyme knockout mutant DELTAZmcytC exhibits filamentous shapes and reduction in growth under a shaking condition at a high temperature compared to the parental strain and became hypersensitive to exogenous H2O2. Under the same condition, the mutation causes increased expression of genes for three other antioxidant enzymes. Peroxidase activity almost abolished in mutant DELTA ZmcytC. The enzyme knockout mutant strain shows activity with ubiquinol-1 as a substrate but not with reduced horse heart cytochrome c, and it shows antimycin A-sensitive NADH oxidase activity
malfunction
-
significantly higher H2O2 accumulation in ccp1-null cells and catalytically inactive Ccp1W191F mutant cells. Ccp1W191F is a more persistent H2O2 signaling protein than wild-type Ccp1
-
physiological function
-
electron transfer
physiological function
Q749D0
bacterial di-heme cytochrome c peroxidases (CcpAs) protect the cell from reactive oxygen species by reducing hydrogen peroxide to water
physiological function
-
CcP catalyzes reduction of hydroperoxides using the electrons provided by its physiological binding partner cytochrome c
physiological function
-
cytochrome c peroxidase is a mitochondrial heme-based H2O2 sensor that modulates antioxidant defense. The enzyme in intermembrane space functions primarily as a mitochondrial H2O2 sensing and signaling protein in yeast cells. Ccp1 H2O2 sensing and signaling regulate Sod2 activity to control superoxide levels. Respiration-derived H2O2 is removed principally by mitochondrial catalase Cta1, which is regulated in a H2O2-dependent manner by Ccp1, overview
physiological function
Q5NNF0, -
involvement of ZmCytC in the aerobic respiratory chain via the cytochrome bc1 complex in addition to the previously proposed direct interaction with ubiquinol and its contribution to protection against oxidative stress
physiological function
-
the parasite's peroxidase LmP helps to protect the parasite from oxidative stress. LmP is a heme peroxidase that catalyzes the peroxidation of mitochondrial cytochrome c
physiological function
-
cytochrome c peroxidase is a mitochondrial heme-based H2O2 sensor that modulates antioxidant defense. The enzyme in intermembrane space functions primarily as a mitochondrial H2O2 sensing and signaling protein in yeast cells. Ccp1 H2O2 sensing and signaling regulate Sod2 activity to control superoxide levels. Respiration-derived H2O2 is removed principally by mitochondrial catalase Cta1, which is regulated in a H2O2-dependent manner by Ccp1, overview
-
metabolism
-
bacterial diheme c-type cytochrome peroxidases catalyze the periplasmic reduction of hydrogen peroxide to water. CcpA does not seem to be part of a CymAMtrA-FccA-based electron transfer network in the periplasm of Shewanella oneidensis
additional information
-
enzyme-cytochrome c protein-protein docking and modeling, overview
additional information
-
CcP requires reductive activation for full activity. The rates of catalysis and activation differ between maltose-binding-protein-fusion and tag-free CcP and also depend on the identity of the electron donor
additional information
-
the catalytic mechanism of H2O2 reduction involves formation of CcP Compound I (CpdI), an intermediate oxidized 2 equiv above the CcP Fe(III) resting state and containing Fe(IV)=O heme oxyferryl and W191 cation radical. Subsequent CpdI reduction occurs in two one-electron steps, involving complex formation with ferrous Cc, intermolecular electron transfer (ET), and product dissociation
additional information
-
structural features that are important for accelerating cyanide binding are also important for accelerating the rate of hydrogen peroxide binding to the heme iron
additional information
-
resting ferric (FeIII) Ccp1III is oxidized by H2O2 to compound I,which has a FeIV heme and a cation radical on residue W191. Compound I reacts with ferrous (FeII) Cyc1II to form compound II with a FeIV heme but no W191 radical. Reaction with a second Cyc1II reduces the FeIV heme to yield resting Ccp1III. The Ccp1W191F variant rapidly reacts with H2O2 but is very slowly reduced by Cyc1II such that it exhibits negligible Cyc1II-oxidizing activity, reaction mechanism, overview
additional information
-
His175 and Asp235 in the proximal heme pocket form another H-bonding cluster that provides a proton-binding site that is responsive to changes in the redox state of the heme iron. Arg-48 is not a good candidate for the proton-binding site. Arg48 interacts with multiple waters, is located near the bottom of the solvent-access channel in CcP. The carboxylate group of heme propionate-7, His181, and Asp37 form a hydrogen-bonded cluster near the heme iron
additional information
-
cytochrome c peroxidase-cytochrome c complex: the binding interface between LmP and LmCytc has one strong and one weak ionic interaction, the Lm redox pair is more dependent on ionic interactions than on nonpolar interactions
additional information
-
resting ferric (FeIII) Ccp1III is oxidized by H2O2 to compound I,which has a FeIV heme and a cation radical on residue W191. Compound I reacts with ferrous (FeII) Cyc1II to form compound II with a FeIV heme but no W191 radical. Reaction with a second Cyc1II reduces the FeIV heme to yield resting Ccp1III. The Ccp1W191F variant rapidly reacts with H2O2 but is very slowly reduced by Cyc1II such that it exhibits negligible Cyc1II-oxidizing activity, reaction mechanism, overview
-
additional information
Saccharomyces cerevisiae Red Star
-
His175 and Asp235 in the proximal heme pocket form another H-bonding cluster that provides a proton-binding site that is responsive to changes in the redox state of the heme iron. Arg-48 is not a good candidate for the proton-binding site. Arg48 interacts with multiple waters, is located near the bottom of the solvent-access channel in CcP. The carboxylate group of heme propionate-7, His181, and Asp37 form a hydrogen-bonded cluster near the heme iron
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-methoxynaphthalene + H2O2
Russig's blue + 2 H2O
show the reaction diagram
-
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
show the reaction diagram
-
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
show the reaction diagram
-
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
show the reaction diagram
-
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
show the reaction diagram
-, Q749D0
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
show the reaction diagram
-
horse cytochrome c
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
show the reaction diagram
-
Pseudomonas aeruginosa cytochrome c-551
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
show the reaction diagram
Marinobacter hydrocarbonoclasticus 617
-
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
show the reaction diagram
Pseudomonas stutzeri 9721
-
Pseudomonas aeruginosa cytochrome c-551
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
show the reaction diagram
-
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
show the reaction diagram
-
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
show the reaction diagram
Q5NNF0, -
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Saccharomyces cerevisiae Red Star
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
?
show the reaction diagram
-, Q749D0
-
-
-
?
2,2'-azino-bis(3-ethylenbenzthiazoline-6-sulfonic acid) + H2O2
?
show the reaction diagram
Geobacter sulfurreducens, Geobacter sulfurreducens DSM 12127
Q74FY6
-
-
-
?
2,2-azinobis(3-ethylbenzthiazolinesulfonic acid) + H2O2
?
show the reaction diagram
-
-
-
-
?
2-aminothiazole + H2O2
?
show the reaction diagram
P00431
modified enzyme
-
-
?
ascorbate + H2O2
dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
ascorbate + H2O2
dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
-
ascorbate + H2O2
dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
ascorbate + H2O2
dehydroascorbate + H2O
show the reaction diagram
P00431
-
-
-
?
azurin + H2O2
oxidized azurin + ?
show the reaction diagram
-
blue copper protein
-
-
?
azurin + H2O2
oxidized azurin + ?
show the reaction diagram
-
blue copper protein
-
?
cytochrome c + H2O2
?
show the reaction diagram
-
-
-
-
?
cytochrome c + H2O2
?
show the reaction diagram
P00431
-
-
-
-
cytochrome c + H2O2
?
show the reaction diagram
-
-
-
-
?
cytochrome c + H2O2
?
show the reaction diagram
-
the reaction with hydrogen peroxide of the W51H/H52L mutant is much slower compared to those of the mutant W51H and W51H/H52W
-
-
?
ferrocyanide + H2O2
ferricyanide + OH-
show the reaction diagram
-
-
-
-
?
ferrocytochrome c + CN-
?
show the reaction diagram
-
dominant binding pathway for H52L mutant, biphasic reaction
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
-
-
-
-
ir
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
P14532
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
-, Q6URB0
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
P00431
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
-
H2O2 can be substituted by ethyl peroxide
-
-
ir
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
-
yeast
-
-
ir
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
-
horse heart
-
-
ir
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
-
horse heart
-
-
ir
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
-
horse heart
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
-
horse heart
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
-
horse heart
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
-, Q6URB0
antioxidant defense
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
-
investigation of the catalytic mechanism
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
Paracoccus pantotrophus LMD 52.44
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
Campylobacter jejuni 81-176
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
Cryptococcus neoformans H99
Q6URB0
-, antioxidant defense
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + 2 H2O
show the reaction diagram
-
-
-
-
?
ferrocytochrome c + HCN
?
show the reaction diagram
-
dominant binding pathway for wild-type enzyme
-
-
?
ferrocytochrome c + menadione
ferricytochrome + oxidized menadione
show the reaction diagram
-
menadione can be substituted by 1,4-naphthoquinone
-
-
?
ferrocytochrome c2 + H2O2
ferricytochrome c2 + OH-
show the reaction diagram
-
-
-
-
?
ferrocytochrome c4 + H2O2
ferricytochrome c4 + OH-
show the reaction diagram
-
-
-
?
ferrocytochrome c551 + H2O2
ferricytochrome c551 + OH-
show the reaction diagram
-
-
-
?
ferrocytochrome c551 + H2O2
ferricytochrome c551 + OH-
show the reaction diagram
-
-
-
?
ferrocytochrome c552 + H2O2
ferricytochrome c552 + OH-
show the reaction diagram
Marinobacter hydrocarbonoclasticus, Marinobacter hydrocarbonoclasticus 617
-
-
-
-
?
ferrocytochrome c553 + H2O2
ferriytochrome c553 + OH-
show the reaction diagram
-
-
-
-
?
ferrocytochrome c555 + H2O2
ferriytochrome c555 + OH-
show the reaction diagram
-
-
-
-
?
ferrocytochrome c555 + H2O2
ferricytochrome c555 + OH-
show the reaction diagram
-
-
-
-
?
guaiacol + H2O2
2-methoxy-cyclohexa-2,5-dienone + H2O
show the reaction diagram
-
-
-
-
?
guaiacol + H2O2
2-methoxy-cyclohexa-2,5-dienone + H2O
show the reaction diagram
-
-
-
-
-
guaiacol + H2O2
2-methoxy-cyclohexa-2,5-dienone + H2O
show the reaction diagram
-
-
-
-
?
guaiacol + H2O2
2-methoxy-cyclohexa-2,5-dienone + H2O
show the reaction diagram
P00431
-
-
-
?
horse heart ferrocytochrome c + H2O2
horse heart ferricytochrome c + H2O
show the reaction diagram
-
-
-
-
?
horse heart ferrocytochrome c + H2O2
horse heart ferricytochrome c + H2O
show the reaction diagram
Paracoccidioides brasiliensis, Paracoccidioides brasiliensis Pb01
-
-
-
-
?
hydroquinone + H2O2
benzoquinone + H2O
show the reaction diagram
-
-
-
-
?
iso-1 ferrocytochrome c + H2O2
?
show the reaction diagram
-
-
-
-
?
iso-1 ferrocytochrome c + H2O2
?
show the reaction diagram
-
C102T
-
-
?
iso-1 ferrocytochrome c mutant C102T + H2O2
iso-1 ferricytochrome c mutant C102T + 2 H2O
show the reaction diagram
-
-
-
-
?
iso-1-cytochrome c + ?
?
show the reaction diagram
-
-
-
-
?
NADH + H2O2
NAD+ + H2O
show the reaction diagram
-
-
-
?
NADPH + H2O2
NADP+ + H2O
show the reaction diagram
-
-
-
-
?
pyrogallol + H2O2
?
show the reaction diagram
-
-
-
-
?
pyrogallol + H2O2
?
show the reaction diagram
-
-
-
-
-
pyrogallol + H2O2
?
show the reaction diagram
-
-
-
-
?
reduced cytochrome c2 + H2O2
oxidized cytochrome c2 + H2O
show the reaction diagram
Rhodobacter capsulatus, Rhodobacter capsulatus B10
-
-
-
-
?
reduced cytochrome c551 + H2O2
oxidized cytochrome c551 + H2O
show the reaction diagram
-
-
-
-
?
reduced horse cytochrome c + H2O2
oxidized horse cytochrome c + H2O
show the reaction diagram
Rhodobacter capsulatus, Rhodobacter capsulatus B10
-
-
-
-
?
reduced pseudoazurin + H2O2
oxidized pseudoazurin + H2O
show the reaction diagram
-
-
-
-
?
isoniazid + H2O2
?
show the reaction diagram
-
-
-
-
?
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
?
-
-
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
?
-
-
Leishmania major peroxidase (LmP) exhibits both ascorbate and cytochrome c peroxidase activities, but cytochrome c is the natural substrate
-
-
-
additional information
?
-
-
menaquinol pool-based origin of electrons that are transferred to CcpA
-
-
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 ferrocytochrome c + H2O2
2 ferricytochrome c + H2O
show the reaction diagram
-, Q749D0
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
show the reaction diagram
-
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
show the reaction diagram
-
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
show the reaction diagram
Q5NNF0, -
-
-
-
?
2 ferrocytochrome c + H2O2
2 ferricytochrome c + 2 H2O
show the reaction diagram
Saccharomyces cerevisiae Red Star
-
-
-
-
?
cytochrome c + H2O2
?
show the reaction diagram
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
-
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
-, Q6URB0
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
P00431
-
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
Cryptococcus neoformans H99
Q6URB0
-
-
-
?
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
?
-
-
Leishmania major peroxidase (LmP) exhibits both ascorbate and cytochrome c peroxidase activities, but cytochrome c is the natural substrate
-
-
-
additional information
?
-
-
menaquinol pool-based origin of electrons that are transferred to CcpA
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
heme
-
heme-associated peroxidase activity
heme
-
diheme cytochrome c peroxidase
heme
-
Fe(III) reduction to Fe(IV) in heme cofactor, pH dependence of the reduction potential and heme binding site structure analysis of wild-type and mutant enzymes using photoreduction and spectroscopic methods, respectively, overview
heme
Q5NNF0, -
the enzyme bears three heme c-binding motifs
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
pre-incubation with the cation has no effect on activity
Ca2+
-
a single, tightly bound, Ca2+ ion at the domain interface of both the fully oxidized and mixed-valence forms of the enzyme is absolutely required for catalytic activity, reduction of the electron-transferring (high-potential) heme in the presence of Ca2+ ions triggers substantial structural rearrangements around the active-site (low-potential) heme to allow substrate binding and catalysis
Ca2+
-
with added Ca2+, the peroxidatic heme is five-coordinate high-spin and active
Fe
-
two haemes per monomer, pyridine haemochrome spectra
Fe
-
two haeme groups
Fe
-
2 hemes per subunit
Fe
-
static titration of ferric cytochrome c peroxidase with reduced azurin shows that only one of the two hemes in the enzyme seems to be readily reduced
Fe2+
-
diheme cytochrome c peroxidase
Iron
-
heme prosthetic group
Iron
-
heme prosthetic group
Iron
-
heme prosthetic group
Iron
-
heme prosthetic group
Iron
-
heme prosthetic group
Iron
Q74FY6
heme iron Fe(III)
Iron
-
heme iron Fe(III)
Iron
-
Fe(III) reduction to Fe(IV) in heme cofactor
Iron
Q5NNF0, -
heme enzyme
Na+
-
maximum turnover occurs at 50 mM NaCl
Iron
-
heme
additional information
-
catalytic center activity increases with ionic strength in the case of cytochrome c551, with horse heart cytochrome c, the catalytic center activity decreases exponentially
additional information
-
the enzyme is sensitive to increasing ionic strength
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-heptyl-4-hydroxyquinoline N-oxide
-
-
3-Amino-1,2,4-triazole
-
2 mM, in the presence of 2 mM H2O2, noticeably retards the growth of the enzyme gene disrupted mutants
Ag+
-
inhibition of NADH oxidizing activity
azide
P55929
mixed-type inhibition. Inhibitor binding occurs at the low-potential heme active site, shifting the resulting catalytic midpoint potential in a negative direction
Ca2+
-
1 mM of the cation in the assay solution inhibits the oxidation of horse cytochrome c but not Pseudomonas stutzeri cytochrome c551
Cu2+
-
inhibition of NADH oxidizing activity
cyanide
P55929
competitive. Inhibitor binding occurs at the low-potential heme active site, shifting the resulting catalytic midpoint potential in a negative direction
cyanide
-
the W51H mutations have a weaker effect on cyanide binding, with the cyanide affinity only 2-8times weaker than for cytochrome c peroxidase. The cyanide association rate constants are between 5 and 85times slower for the W51H mutants, while the cyanide dissociation rate constants range from 3times slower to 6times faster than those of wild-type cytochrome c peroxidase
cyanide
-
cyanide binding can act as a surrogate for the hydrogen peroxide reaction. Structural features that are important for accelerating cyanide binding are also important for accelerating the rate of hydrogen peroxide binding to the heme iron, equilibrium dissociation constants of wild-type and mutant enzymes, and pH-independent equilibrium dissociation constants for the high- and low-affinity cyanide binding phases of the triple mutants, overview
cytochrome c551
-
above 0.05 mM, substrate inhibition
-
H2O2
-
2 mM, noticeably retards the growth of the enzyme gene disrupted mutants
H2O2
-, Q6URB0
at a concentration of 8% and 16% can inhibit the growth of wild-type strain H99
nitric oxide
-
complete suppression of activity. Nitrosyl complexes of cytochrome c produced during inhibition are sensitive to laser irradiation and are photolyzed during irradiation. Decomposition leads to partial restoration of enzyme activity
nitrite
-
2 mM, in the presence of 0.88 M of H2O2, inhibits 50% enzyme activity
Pb2+
-
inhibition of NADH oxidizing activity
Hg2+
-
inhibition of NADH oxidizing activity
additional information
-
mixed-monolayer protected colloids selectively interact with enzyme and cytochrome c based upon charge complementarity. Surface-functionalized colloids with gold cores and thiolates terminating in trimethyl-amine bind reversibly and proteins retain their native structure. Binding is reversed by high ionic strength
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
cardiolipin
-
strict concurrency between iron-sulfur of M80 bond breaking and enzyme activity enhancement at molar ratios of cardiolipin/cytochrome c of 0:1 to 50:1. Cardiolipin is 20times more effective than sodium dodecylsulfate, cardiolipin-activitated activity is reduced by high ionic strength solution, e.g. 1 M KCl
cardiolipin
-
specific activation of enzyme in liposomes. Activation is due to promotion of iron-sulfur (M80) bond breaking and also due to facilitation of H2O2 penetration to the reaction center
FNR protein
-
expression of cytochrome c peroxidase is dependent on the combination of FNR protein and OxyR protein under conditions of oxygen starvation
-
OxyR protein
-
expression of cytochrome c peroxidase is dependent on the combination of FNR protein and OxyR protein under conditions of oxygen starvation
-
sodium dodecylsulfate
-
strict concurrency between iron-sulfur of M80 bond breaking and enzyme activity enhancement at molar ratios of sodium dodecylsulfate/cytochrome c of 0:1 to 50:1. Cardiolipin is 20times more effective than sodium dodecylsulfate
H2O2
-
high-dose treatments with 50 mM H2O2 lead to an early increase in total CCP enzymatic activity, indicative of post-transcriptional regulation
additional information
-
model of the activation process based on the structures of the inactive oxidized and active mixed valence enzyme
-
additional information
-
CcP requires reductive activation for full activity
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0113
-
2,2-azinobis(3-ethylbenzthiazolinesulfonic acid)
-
pH 7.5, temperature not specified in the publication
-
0.31
-
ascorbate
-
mutant N184R/W191F, pH 6.0, 25C
0.45
-
ascorbate
-
mutant W191, pH 6.0, 25C
0.48
-
ascorbate
-
mutant FY36A/N184R, pH 6.0, 25C
0.5
-
ascorbate
-
mutant Y36A/W191F, pH 6.0, 25C
0.71
-
ascorbate
-
wild-type cytochrome c peroxidase, pH 6.0, 25C
1.3
-
ascorbate
-
mutant Y36A/N184R/W191F, pH 6.0, 25C
1.7
-
ascorbate
-
mutant N184R, pH 6.0, 25C; mutant Y36A, pH 6.0, 25C
93
-
cytochrome c
-
wild-type cytochrome c peroxidase, pH 6.0, 25C
100
-
cytochrome c
-
mutant W191F, pH 6.0, 25C, 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
110
-
cytochrome c
-
mutant FY36A/N184R, pH 6.0, 25C
140
-
cytochrome c
-
mutant N184R, pH 6.0, 25C
160
-
cytochrome c
-
mutant Y36A/W191F, pH 6.0, 25C
230
-
cytochrome c
-
mutant Y36A, pH 6.0, 25C
300
-
cytochrome c
-
mutant Y36A/N184R/W191F, pH 6.0, 25C
670
-
cytochrome c
-
mutant N184R/W191F, pH 6.0, 25C
0.005
-
Ferrocytochrome
-
horse heart
0.025
-
Ferrocytochrome
-
yeast, with electron acceptor H2O2
0.002
-
ferrocytochrome c
-
recombinant wild-type, pH 7.5, 25C, 100 mM phosphate buffer
0.003
-
ferrocytochrome c
-
horse
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
-
yeast
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, 25C, 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
0.04
-
ferrocytochrome c
-
K98A substrate mutant, pH and temperature not specified in the publication
0.047
-
ferrocytochrome c
-
recombinant wild-type, pH 7.5, 25C, 10 mM phosphate buffer
0.13
-
ferrocytochrome c
-
covalent complex of mutant E290C, pH 7.5, 25C, 10 mM phosphate buffer. Activity is due to unreacted enzyme copurifying with the complex
0.013
-
ferrocytochrome c550
-
-
-
510
-
ferrocytochrome c555
-
-
-
14
-
guaiacol
-
mutant Y36A/N184R/W191F, pH 6.0, 25C, 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
16
-
guaiacol
-
mutant FY36A/N184R, pH 6.0, 25C
27
-
guaiacol
-
mutant N184R, pH 6.0, 25C
34
-
guaiacol
-
mutant N184R/W191F, pH 6.0, 25C
36
-
guaiacol
-
mutant Y36A, pH 6.0, 25C
45
-
guaiacol
-
mutant Y36A/W191F, pH 6.0, 25C
53
-
guaiacol
-
wild-type cytochrome c peroxidase, pH 6.0, 25C
57
-
guaiacol
-
mutant W191, pH 6.0, 25C
0.0062
-
H2O2
Q749D0
pH5.5
0.025
-
H2O2
-
protein film voltammetry, the midpoint potentials of the turnover signals are used to calculate Michaelis-Menten kinetics
0.055
-
H2O2
-
; pH 7.0, 0C
0.006
-
horse cytochrome
-
pH 7.0
-
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 25C
-
0.002
-
iso-1 ferrocytochrome c
-
mutant enzyme D18K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25C
-
0.0021
-
iso-1 ferrocytochrome c
-
recombinant wild type enzyme, in 0.1 M potassium phosphate buffer, pH 7.5, at 25C
-
0.0023
-
iso-1 ferrocytochrome c
-
mutant enzyme E17K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25C
-
0.0024
-
iso-1 ferrocytochrome c
-
mutant enzyme D33K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25C
-
0.0028
-
iso-1 ferrocytochrome c
-
mutant enzyme E209K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25C
-
0.0029
-
iso-1 ferrocytochrome c
-
mutant enzyme E201K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25C
-
0.0031
-
iso-1 ferrocytochrome c
-
mutant enzyme E98K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25C
-
0.0035
-
iso-1 ferrocytochrome c
-
mutant enzyme E35K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25C
-
0.0038
-
iso-1 ferrocytochrome c
-
mutant enzyme E291K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25C
-
0.0045
-
iso-1 ferrocytochrome c
-
mutant enzyme E32K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25C
-
0.051
-
iso-1 ferrocytochrome c
-
mutant enzyme E118K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25C
-
0.06
-
iso-1 ferrocytochrome c
-
mutant enzyme E290K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25C
-
0.082
-
iso-1 ferrocytochrome c
-
mutant enzyme D37K, in 0.1 M potassium phosphate buffer, pH 7.5, at 25C
-
0.06
-
Rhodobacter capsulatus cytochrome c2
-
pH 7.0
-
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 25C; Km above 0.1 mM, mutant enzyme R31E, in 0.1 M potassium phosphate buffer, pH 7.5, at 25C
-
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 kinetics
-
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
-
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
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00007
-
1-methoxynaphthalene
-
pH 7.0, 25C, wild-type enzyme
0.0022
-
1-methoxynaphthalene
-
pH 7.0, 25C, mutant R48L/W51L/H52L
0.0023
-
1-methoxynaphthalene
-
pH 7.0, 25C, mutant R48V/W51V/H52V
0.0025
-
1-methoxynaphthalene
-
pH 7.0, 25C, mutant R48A/W51A/H52A
23.1
-
2,2-azinobis(3-ethylbenzthiazolinesulfonic acid)
-
pH 7.5, temperature not specified in the publication
-
0.25
-
ascorbate
-
mutant W191, pH 6.0, 25C
0.27
-
ascorbate
-
mutant N184R/W191F, pH 6.0, 25C
0.45
-
ascorbate
-
mutant Y36A/W191F, pH 6.0, 25C
0.66
-
ascorbate
-
mutant FY36A/N184R, pH 6.0, 25C
0.83
-
ascorbate
-
wild-type cytochrome c peroxidase, pH 6.0, 25C
1.3
-
ascorbate
-
mutant Y36A, pH 6.0, 25C
1.5
-
ascorbate
-
mutant N184R, pH 6.0, 25C
2.6
-
ascorbate
-
mutant Y36A/N184R/W191F, pH 6.0, 25C
0.06
-
cytochrome c
-
mutant Y36A/W191F, pH 6.0, 25C
0.08
-
cytochrome c
-
mutant N184R/W191F, pH 6.0, 25C
1.6
-
cytochrome c
-
mutant Y36A/N184R/W191F, pH 6.0, 25C
1.7
-
cytochrome c
-
mutant W191, pH 6.0, 25C
570
-
cytochrome c
-
mutant N184R, pH 6.0, 25C
580
-
cytochrome c
-
mutant Y36A, pH 6.0, 25C
600
-
cytochrome c
-
mutant FY36A/N184R, pH 6.0, 25C
1510
-
cytochrome c
-
wild-type cytochrome c peroxidase, pH 6.0, 25C
17.2
-
ferrocytochrome c
-
horse
23.6
-
ferrocytochrome c
-
horse
1500
-
ferrocytochrome c
-
yeast
2000
-
ferrocytochrome c
-
horse heart
17.7
-
ferrocytochrome c2
-
-
3.05
-
ferrocytochrome c555
-
-
-
0.9
-
guaiacol
-
mutant FY36A/N184R, pH 6.0, 25C
1.5
-
guaiacol
-
mutant Y36A/N184R/W191F, pH 6.0, 25C
3
-
guaiacol
-
mutant N184R, pH 6.0, 25C
3.2
-
guaiacol
-
mutant Y36A/W191F, pH 6.0, 25C
4.1
-
guaiacol
-
wild-type cytochrome c peroxidase, pH 6.0, 25C
4.9
-
guaiacol
-
mutant N184R/W191F, pH 6.0, 25C
5.4
-
guaiacol
-
mutant Y36A, pH 6.0, 25C
14
-
guaiacol
-
mutant W191, pH 6.0, 25C
15.5
-
H2O2
Q749D0
pH 5.5
40
-
horse cytochrome c
-
pH 7.0
-
4.2
-
horse heart cytochrome c
-
pH 6, 200 mM potassium phosphate, covalent complex
-
20.7
-
horse heart cytochrome c
-
pH 6, 20 mM potassium phosphate, covalent complex
-
166.8
-
horse heart cytochrome c
-
pH 6, 200 mM potassium phosphate, V197C/C128A mutant
-
175.1
-
horse heart cytochrome c
-
pH 6, 200 mM potassium phosphate, wild-type enzyme
-
803.4
-
horse heart cytochrome c
-
pH 6, 20 mM potassium phosphate, V197C/C128A mutant
-
40
-
Rhodobacter capsulatus cytochrome c2
-
pH 7.0
-
15.7
-
yeast cytochrome c
-
pH 6, 20 mM potassium phosphate, covalent complex
-
76.2
-
yeast cytochrome c
-
pH 6, 200 mM potassium phosphate, covalent complex
-
219.1
-
yeast cytochrome c
-
pH 6, 20 mM potassium phosphate, wild-type enzyme
-
240.9
-
yeast cytochrome c
-
pH 6, 20 mM potassium phosphate, V197C/C128A mutant
-
1167
-
yeast cytochrome c
-
pH 6, 200 mM potassium phosphate, V197C/C128A mutant
-
1362
-
yeast cytochrome c
-
pH 6, 200 mM potassium phosphate, wild-type enzyme
-
850.3
-
horse heart cytochrome c
-
pH 6, 20 mM potassium phosphate, wild-type enzyme
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00015
-
cyanide
P55929
-
0.05
-
cyanide
-
pH 7, 25 microM H2O2, protein film voltammetry, the midpoint potentials of the turnover signals are used to calculate Michaelis-Menten kinetics
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
12.9
-
-
supernatant, pH 7.5, 25C
26.4
-
Q749D0
2,2-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) and H2O2 as electron donor and acceptor
104.6
-
-
; purified enzyme, pH 7.5, 25C
additional information
-
-
total activity 481.2 micromol/min/g of cells, pH 7.0
additional information
-
-
total activity 2.5 micromol/min/g of cells, pH 7.0
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
assay at
7.5
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
10
-
by using the maximum current in the cathodic and anodic halfscans in the course of altering the pH a shift in potential is observed, at pH 7, a single redox couple (I) is dominant, but at more acidic pH values, a second couple (II) is clearly discernible at a more positive value of potential
4
8.6
-
the association rate constant for the binding of cyanide to H52L mutant varies almost 4 orders of magnitude in this pH range. Above pH 8 cyanide binds more rapidly to H52L mutant than to wild-type enzyme
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
23
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-, Q604F4
noncovalent association with cell surface, exposed to cell exterior
Manually annotated by BRENDA team
Campylobacter jejuni 81-176
-
-
-
Manually annotated by BRENDA team
-
the enzyme is a lipoprotein sarkosyl-soluble
Manually annotated by BRENDA team
Cryptococcus neoformans H99
-
-
-
Manually annotated by BRENDA team
-
98% of nonmembrane-bound enzyme activity
-
Manually annotated by BRENDA team
-
92% of total enzyme activity
-
Manually annotated by BRENDA team
Campylobacter jejuni 81-176
-
-
-
-
Manually annotated by BRENDA team
Pseudomonas stutzeri 9721
-
92% of total enzyme activity
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Nitrosomonas europaea (strain ATCC 19718 / NBRC 14298)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Saccharomyces cerevisiae (strain RM11-1a)
Shewanella oneidensis (strain MR-1)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
32000
-
-
gel filtration
32000
-
-
sedimentation equilibrium analysis, in the presence of 1 mM EGTA, pH 7.5
33560
-
-
MALDI-TOF
34000
-
-
DocA, SDS-PAGE
34100
35240
-
amino acid composition of tryptic peptides
34100
35240
-
sedimentation and diffusion constants, partial specific volume
34100
35240
-
amino acid sequence of apoprotein: 33419, of holoenzyme: 34036
36000
-
-
SDS-PAGE
36230
-
-
calculated
36250
-
-
electrospray mass spectrometry
36270
-
-
MALDI-TOF mass spectrometry
36580
-
-
electrospray mass spectrometry
37000
-
-
Cjj0382, SDS-PAGE
37510
-
-
predicted from cDNA sequence for monomer
37510
-
-
electrospray mass spectrometry
39570
-
-
calculated from amino acid composition
42000
-
-
SDS-PAGE
44000
-
-
amino acid analysis
48000
-
-
sedimentation equilibrium analysis, 0.002 mM protein, pH 6
51000
-
-
sedimentation velocity experiments, in the presence of EGTA
54000
-
-
sedimentation equilibrium analysis, 0.01 mM protein, pH 6
57500
-
-
gel filtration; gel filtration chromatography
59100
-
-
sedimentation equilibrium analysis, 0.04 mM protein, pH 6
63000
-
-
gel filtration
67000
-
-
sedimentation velocity experiments, untreated enzyme
68700
-
-
sedimentation equilibrium analysis, 0.04 mM protein, in the presence of 2 mM Ca2+, pH 6
69100
-
-
sedimentation equilibrium analysis, 0.01 mM protein, in the presence of 2 mM Ca2+, pH 6
70000
-
-
gel filtration
72500
-
-
sedimentation equilibrium analysis, 0.002 mM protein, in the presence of 2 mM Ca2+, pH 6
73000
-
-
sedimentation equilibrium analysis, in the presence of 5 mM Ca2+, pH 7.5
75000
-
-
SDS-PAGE
75030
-
-
predicted from cDNA sequence for dimer
78000
80000
-
gel filtration
80000
-
-
sedimentation velocity experiments, in the presence of Ca2+
87000
-
-
sedimentation velocity experiments, at higher protein concentrations
90000
-
-
gel filtration
94000
-
-
sedimentation velocity ultracentrifugation, with enzyme/horse heart cytochrome c ratio of 4 to 1
108000
-
-
sedimentation velocity ultracentrifugation, with Paracoccus cytochrome c ratio of 4 to 1
additional information
-
-
mutant W191F molecular weight 34196 Da after treatment with H2O2, covalent attachment of the heme (617 Da) to the apoenzyme (33561 Da)
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-, Q604F4
x ? 78000, calculated, mature protein, x * 80000, SDS-PAGE
?
-
x * 34418, mass spectrometry
dimer
-
2 * 37500, SDS-PAGE
dimer
-
2 * 36500, SDS-PAGE
dimer
-
2 * 44000, SDS-PAGE
dimer
-
in the presence of Ca2+, sedimentation equilibrium analysis
dimer
-
SDS-PAGE, wild type and W191F mutant enzymes
dimer
-
ultracentrifugation, untreated enzyme
dimer
-
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 hydrocarbonoclasticus 617
-
2 * 36500, SDS-PAGE
-
heterodimer
-
SDS-PAGE, H2O2 oxidation induces heterodimerization between cytochrome c and both wild-type and W191F enzymes, but not with W51F mutant
homodimer
-
crystal analysis
homodimer
-
2 * 37500, dihemic subunits
monomer
-
1 * 32500, SDS-PAGE
monomer
-
with no addition of Ca2+, the monomer/dimer ratio is shifted toward the monomeric form, sedimentation equilibrium analysis
monomer or dimer
-
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
polymer
-
SDS-PAGE, W51F mutant
trimer
-
SDS-PAGE, W51F mutant
monomer or dimer
Paracoccus pantotrophus LMD 52.44
-
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
-
additional information
-
pair of dimers related by local dyads. Functional dimers can dimerize
additional information
-
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
-
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
-
in the presence of added Ca2+ or higher protein concentrations, the enzyme partially shifts to a higher state of aggregation, presumably tetramer
additional information
-
CcpA three-dimensional structure analysis, overview
additional information
Q74FY6
three-dimensional structure of MacA by molecular replacement, model building, overview
additional information
-
recombinant His-tagged enzyme is used for structure analysis by multidimensional NMR spectroscopy, structure modeling, overview
additional information
Geobacter sulfurreducens DSM 12127
-
three-dimensional structure of MacA by molecular replacement, model building, overview
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
-, Q604F4
sequence contains a leader peptide with a putative cleavage site between A41 and H42
no glycoprotein
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purified recombinant Strep-tagged mutant enzyme H93G, and wild-type enzyme in reduced, oxidized, and semireduced states, sitting drop vapor diffusion method, 0.001 ml of 7.5 mg/ml protein is mixed with 0.001 ml of reservoir solution containing for the oxidized enzyme 0.1 M ammonium acetate buffer, pH 5.5, 1.3 M Na/K phosphate and 6% v/v of ethanol, for the ascorbate reduced enzyme 0.1 M HEPES/NaOH buffer, pH 7.5, 0.2 M ammonium acetate, and 25% w/v PEG 3350, and for the dithionite reduced enzyme 0.1 M sodium citrate buffer, pH 5.6, and 1 M ammonium phosphate, mutant MacA_H93G crystals are obtained in 1 M ammonium sulfate, pH 5.4, X-ray diffraction structure determination and analysis at 1.2-2.3 A resolution
Q74FY6
sitting-drop vapor diffusion, 16% PEG 10000, 0.1 HEPES/NaOH, pH 7.4, 293K, wild-type enzyme, space group P1, 2.00 A resolution, mutant enzyme G94K/K97Q/R100I, space group P4321, 3.21 A resolution, mutant enzyme S134P/V135K, space group P21, 2.40 A resolution, mutant enzame S134P, space group P21, 2.40 A resolution
Q749D0
enzyme in complex with wild-type cytochrome c or cytochrome c mutant DELTA10LmCytc, hanging-drop vapour diffusion method, protein in 40mMpotassium phosphate, pH 6.5, 32-33% pentaerythritol ethoxylate and 4% acetone as precipitant, X-ray diffraction structure determination and analysis at 1.84-2.29 A resolution
-
the enzyme crystallizes in two different forms obtained at pH 4 and pH 5.3, corresponding to form IN, inactive, and OUT, active. In the form OUT, the calcium binding site is fully occupied by Ca2+, coordinated by seven ligands in a distorted pentagonal bipyramidal geometry, and four water molecules
-
resolution 1.8 A
-
hanging-drop vapour-diffusion method
-
structures of the inactive oxidized and active mixed valence enzyme, model of the activation process
-
of mutant D37E/V45E/H181E in a metal-free form and with Co2+ at the designed Mn2+ site, mutant is a close structural model of the Mn2+ binding site in manganese peroxidase
-
diffraction limit 2.5 A
-
resolution 2.4 A
-
with 24% PEG 600, 0.2 M imidazole malate pH 5.5, 20 mM dithiothreitol
-
under cryogenic conditions using synchrotron radiation
-
fully oxidized form, reveals that a segment of 10 amino acids near the peroxide binding site is disordered in all four molecules of the asymmetric unit of the crystal. Flexibility in this part of the molecular scaffold correlates with the levels of activity seen in cytochrome c peroxidases characterized so far
-
hanging-drop vapour-diffusion method
-
apo- and holoenzyme
-
apo- and holoenzyme
-
crystal structure
-
microdialysis, in 500 mM potassium phosphate, pH 6.0, against 50 mM potassium phosphate, pH 6.0, containing 30% 2-methyl-2,4-pentanediol
-
of iron-free enzyme, removal of iron has no effect on porphyrin geometry and distortion, indicating that iron coordination is not responsible for prophyrin conformation. Iron depletion leads to changes in solvent structure in the distal pocket which result in changes in the distal H52 acid-base catalyst
-
protein channel mutant with surrogate protein (N-benzimidazole-propionic acid)-Gly-Ala-Ala (BzGAA), vapor diffusion, 200 mM KPi, 25% MPD, pH 6.0, temperature 282K, space group P212121, resolution 1.6 A
-
structure of fluoride-inhibited enzyme
-
structure of NO-inhibited enzyme
-
structures for mutants N184R, Y36A, W191F, N184R/W191F, Y36A/W191, FY36A/N184R, Y36A/N184R/W191F, Y36A/N184R/W191F-ascorbate complex, no major perturbations compared to the wild type protein
-
with comercial kit
-
purified recombinnat His-tagged CcpA, sitting drop vapor diffusion, mixing of 0.001 ml 7.5 mg/ml dithionite-reduced protein solution with 0.001 ml of reservoir solution containing 26% w/v PEG 2000 monomethyl ether and 0.1 M bis-(2-hydroxyethyl)-amino-tris-(hydroxymethyl)methane, pH 5.0, equilibration against 0.2 ml of reserrvoir solution, 10% v/v (2R,3R)-butanediol as a cryoprotectant, X-ray diffraction structure determination and analysis
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
10
-
by using the maximum current in the cathodic and anodic halfscans in the course of altering the pH a shift in potential is observed, at pH 7, a single redox couple (I) is dominant, but at more acidic pH values, a second couple (II) is clearly discernible at a more positive value of potential
4
8
-
mutants W51H, W51H/H52W and W51H/H52L are significantly less stable at pH 4.0 than wild-type cytochrome c peroxidase, at pH 4, the Soret band of the spectra for all three mutants undergoes a loss of absorptivity, suggesting the beginning of acid denaturation
8
-
-
CCP is not stable above pH 8.0
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
70
-
-
15 min, 80% loss of peroxidizing activity, 50% loss of NADH oxidizing activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
unstable during degassing under vacuum except in presence of detergent
-
crystals stable in water-saturated atmosphere for more than 5 h at 23C
-
no dimerization after 7 years
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
while the wild-type CcP is very stable to oxidative degradation by excess hydrogen peroxide, CcP mutant R48A/W51A/H52A is inactivated within four cycles of the peroxygenase reaction
-
724658
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 0.1 M phosphate buffer, pH 7.0, two months
-
-20C, 0.5 M phosphate buffer, pH 6
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
partially purified
-
chromatography
Q749D0
recombinant N-terminally Strep-tagged protein from Escherichia coli strain BL21(DE3) by streptactin affinity chromatography and gel filtration
Q74FY6
four-step purification protocol
-
inner membrane proteins solubilized in sarkosyl solution and precipitated with ethanol are purified by affinity chromatography
-
purified to homogeneity in three steps
-
precipitation, DEAE-Sepharose followed by S-100 size exclusion chromatography
-
S-Sepharose column chromatography and Superdex-75 gel filtration
-
gel filtration and ion exchange chromatography
-
purified to homogeneity
-
high-purity V197C/C128A mutant is obtained after an anion-exchange chromatography and gel filtration
-
native enzyme partially by preparation of mitochondria
-
recombinant soluble His-tagged Ccp from Escherichia coli strain BL21(DE3) by immobilized metal affinity chromatography and gel filtration
-
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by anion exchange chromatography and dialysis
-
recombinant His-tagged CcpA from Escherichia coli strain AS457
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
Q749D0
gene macA, expression as N-terminally Strep-tagged protein in Escherichia coli strain BL21(DE3)
Q74FY6
expression in Escherichia coli
-
expressed in Escherichia coli JM109 (DE3) cells
-
expression in Escherichia coli JM109(DE3) with pETCCP coexpressed with pEC86
-
expression in Escherichia coli; mutants expressed in Escherichia coli
-
expression in Escherichia coli
-
overexpression in Escherichia coli
-
expressed in Escherichia coli strain BL21(DE3)
-
expression in Escherichia coli
-
expression of V197C/C128A mutant in Escherichia coli
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
functional expression of deuterated and soluble His-tagged Ccp in Escherichia coli strain BL21(DE3). Introduction of a His-tag at either protein terminus dramatically increases its solubility, allowing preparation of concentrated, stable CcP samples. The engineered His tags neither perturb the structure of the enzyme nor alter the heme environment or its reactivity toward known ligands
-
overexpression in Escherichia coli in deuterated medium
-
overexpression of modified enzyme in Escherichia coli
-
recombinant expression of wild-type and mutant enzymes
-
expression of maltose-binding-protein-fusion and tag-free CcP in Escherichia coli strain JM 109, the presence of the MBP tag affects the availability of certain binding sites, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
gene ccpA, expression of His-tagged CcpA in Escherichia coli strain AS457
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
W191F
-
less efficient at catalytic turnover than the wild-type enzyme
W191G
-
the mutant exhibits a loop-gated artificial protein cavity
W51F
-
exhibits extensive dimerization
A124K/K128A
Q749D0
site-directed mutagenesis, no significant changes
G94K/K97Q/R100I
Q749D0
site-directed mutagenesis, triple point mutant is created to mimic the critical loop region of, but its crystal structure reveals that the inactive, bishistidinyl-coordinated form of the active-site heme group is retained
H93G
Q74FY6
site-directed mutagenesis
M297H
Q74FY6
site-directed mutagenesis
S134P
Q749D0
site-directed mutagenesis, distortion of the loop region, accompanied by an opening of the active-site loop, leaving the enzyme in a constitutively active state
S134P/V135K
Q749D0
site-directed mutagenesis, distortion of the loop region, accompanied by an opening of the active-site loop, leaving the enzyme in a constitutively active state
H93G
Geobacter sulfurreducens DSM 12127
-
site-directed mutagenesis
-
D37E/P44D/V45D
-
redesign of a manganese-binding site, ratio kcat/KM values for manganese oxidation is 0.33 per mM and s at pH 5.0
D37E/V45E/H181E
-
redesign of a manganese-binding site, ratio kcat/KM values for manganese oxidation is 0.25 per mM and s at pH 5.0
G41E/V45E/H181D
-
redesign of a manganese-binding site, ratio kcat/KM values for manganese oxidation is 0.10 per mM and s at pH 5.0
G41E/V45E/W51F/H181D/W191F
-
redesign of a manganese-binding site, ratio kcat/KM values for manganese oxidation is 0.6 per mM and s at pH 5.0
H71G
-
55% activity compared to the wild type enzyme, contains a high-spin, presumably five-coordinate, peroxidatic heme site; about 55% of wild-type activity. Five-coordinate, peroxidatic heme structure contrary to six-coordinate structure of wild-type, formation of a tryptophan radical species during catalysis
H71G
-
the unactivated H71G mutant shows 75% of turnover activity of the wild-type enzyme in the activated form
W94A
-
less than 1% activity compared to the wild type enzyme, the mutant retains the normal six-coordinate heme structures; less than 1% of wild-type activity. Six-coordinate heme structure similar to wild-type
E117H
-
no enzymatic activity
E117K
-
no enzymatic activity
E117L
-
no enzymatic activity
H74M
-
no enzymatic activity, reduced redox potential. The introduced methionine does not ligate the N-terminal heme
M118H
-
no enzymatic activity
M118L
-
7.3% of wild-type activity
M278H
-
no enzymatic activity, reduced redox potential. Mutant contains two low-potential hemes
Q107L
-
no enzymatic activity
W97A
-
no enzymatic activity. W97 is the mediator of intramolecular electron transfer of the enzyme
W97F
-
no enzymatic activity. W97 is the mediator of intramolecular electron transfer of the enzyme
A193F
-
surface mutant, shift in reduction potential to -170 mV. Analysis of spectroscopic properties
D146N
-
surface mutant, shift in reduction potential to -173 mV. Analysis of spectroscopic properties
D146N/D148N
-
surface mutant, shift in reduction potential to -173 mV. Analysis of spectroscopic properties
D18K
-
positive-to-negative charge-reversal mutant
D210K
-
positive-to-negative charge-reversal mutant
D235A
-
proximal pocket mutant, shift in reduction potential to -78 mV. Analysis of spectroscopic properties
D235E
-
proximal pocket mutant, shift in reduction potential to -113 mV. Analysis of spectroscopic properties
D235N
-
predominantly hexacoordinate between pH 4 and pH8
D235N
-
proximal pocket mutant, shift in reduction potential to -79 mV. Analysis of spectroscopic properties
D33K
-
positive-to-negative charge-reversal mutant
D34K
-
the mutation causes large increases in the Michaelis constant indicating a reduced affinity for cytochrome c
D34N
-
surface mutant, shift in reduction potential to -175 mV. Analysis of spectroscopic properties
D37K
-
positive-to-negative charge-reversal mutant
D37K
-
the mutation causes large increases in the Michaelis constant indicating a reduced affinity for cytochrome c
E118K
-
positive-to-negative charge-reversal mutant
E118K
-
the mutation causes large increases in the Michaelis constant indicating a reduced affinity for cytochrome c
E17K
-
positive-to-negative charge-reversal mutant
E201K
-
positive-to-negative charge-reversal mutant
E209K
-
positive-to-negative charge-reversal mutant
E290C
-
formation of a covalent complex with cytochrome c mutant K79C, kinetic studies. Residual activity of complex is due to unreacted enzyme that copurifies with the complex. In the complex, the Pelletier-Kraut site is blocked which results in zero catalytic activity
E290K
-
positive-to-negative charge-reversal mutant
E290K
-
the mutation causes large increases in the Michaelis constant indicating a reduced affinity for cytochrome c
E290N
-
surface mutant, shift in reduction potential to -177 mV. Analysis of spectroscopic properties
E291K
-
positive-to-negative charge-reversal mutant
E291Q
-
surface mutant, shift in reduction potential to -162 mV. Analysis of spectroscopic properties
E32K
-
positive-to-negative charge-reversal mutant
E32Q
-
surface mutant, shift in reduction potential to -168 mV. Analysis of spectroscopic properties
E35K
-
positive-to-negative charge-reversal mutant
E98K
-
positive-to-negative charge-reversal mutant
H52D
-
distal pocket mutant, shift in reduction potential to -221 mV. Analysis of spectroscopic properties
H52E
-
distal pocket mutant, reduction potential -183 mV, comparable to wild-type
H52K
-
distal pocket mutant, shift in reduction potential to -157 mV. Analysis of spectroscopic properties
H52L
-
reacts with H2O2 at a lower rate
H52L
-
with slower cyanide dissociation rate constant for the heme group with respect to the wild-type enzyme
H52L
-
exhibits multiple forms in solution, with a reversible temperature-dependent interconversion, indicating the presence of a dynamic equilibrium between enzyme forms, which favors an apparent single form at low temperature and low pH, and a different form at high temperature and high pH
H52L
-
distal pocket mutant, shift in reduction potential to -170 mV. Analysis of spectroscopic properties
H52L |
-
site-directed mutagenesis, a distal pocket mutant
H52L/W191F
-
proximal pocket mutant, shift in reduction potential to -151 mV. Analysis of spectroscopic properties
H52N |
-
distal pocket mutant, shift in reduction potential to -259 mV, most negative reduction potential of all mutants analyzed. Analysis of spectroscopic properties
H52Q
-
distal pocket mutant, shift in reduction potential to -224 mV. Analysis of spectroscopic properties
H52Q |
-
site-directed mutagenesis, a distal pocket mutant
K12C
-
characterization of complex with yeast cytochrome c mutant K79C. Cytochrome c is covalently bound and located 90 from its primary binding site. Catalytic activity is similar to wild-type cytochrome c peroxidase
K149D
-
positive-to-negative charge-reversal mutant
N184R
-
the N184R variant introduces potential hydrogen bonding interactions for ascorbate binding
N184R/W191F
-
site-directed mutagenesis
N78C
-
characterization of complex with yeast cytochrome c mutant K79C. Cytochrome c is covalently bound and located 90 from its primary binding site. Catalytic activity is similar to wild-type cytochrome c peroxidase
R31E
-
positive-to-negative charge-reversal mutant
R48A/W51A/H52A
-
distal pocket mutant, shift in reduction potential to -163 mV. Analysis of spectroscopic properties
R48A/W51A/H52A
-
site-directed mutagenesis, the mutant has altered pKA values compred to the wild-type enzyme
R48A/W51A/H52A
-
site-directed mutagenesis, the mutant shows 34fold higher activity with 1-methoxynaphthalene than the wild-type enzyme. While wild-type CcP is very stable to oxidative degradation by excess hydrogen peroxide, mutant CcP is inactivated within four cycles of the peroxygenase reaction
R48E
-
distal pocket mutant, shift in reduction potential to -179 mV. Analysis of spectroscopic properties
R48K
-
hexacoordinate, high-spin, unreactive against H2O2
R48K
-
distal pocket mutant, reduction potential -186 mV, comparable to wild-type. Analysis of spectroscopic properties
R48L
-
reacts with H2O2 at a lower rate
R48L
-
distal pocket mutant, shift in reduction potential to -164 mV. Analysis of spectroscopic properties
R48L/W51L/H52L
-
distal pocket mutant, shift in reduction potential to -146 mV. Analysis of spectroscopic properties
R48L/W51L/H52L
-
site-directed mutagenesis, the mutant has altered pKA values compred to the wild-type enzyme
R48L/W51L/H52L
-
site-directed mutagenesis, the mutant shows higher activity with 1-methoxynaphthalene than the wild-type enzyme
R48L/W51L/H52L |
-
site-directed mutagenesis, a distal pocket mutant
R48V/W51V/H52V
-
distal pocket mutant, shift in reduction potential to -150 mV. Analysis of spectroscopic properties
R48V/W51V/H52V
-
site-directed mutagenesis, the mutant has altered pKA values compred to the wild-type enzyme
R48V/W51V/H52V
-
site-directed mutagenesis, the mutant shows higher activity with 1-methoxynaphthalene than the wild-type enzyme
V197C/C128A
-
as active as the wild-type enzyme. Used to generate a covalent complex with a mutant cytochrome c
V5C
-
characterization of complex with yeast cytochrome c mutant K79C. Cytochrome c is covalently bound via disulfide formation of the mutated residues and located on the back-side of the enzyme, 180 from its primary binding site. Catalytic activity is similar to wild-type cytochrome c peroxidase. Significant electrostatic repulsion of the two cytochrome c molecules bound in an 2:1 complex which decreases as the ionic strength of buffer increases
W191F
-
reacts with H2O2 at a slightly higher rate
W191F
-
proximal pocket mutant, shift in reduction potential to -202 mV. Analysis of spectroscopic properties
W191F
-
site-directed mutagenesis
W191F
-
side chain replacement followed by four iterations of side chain sampling plus minimization of a region within 6 A of Trp191, in W191F partial formation of a covalent link from Trp51 to the heme is observed
W191F
-
catalytically inactive mature Ccp1 mutant, Ccp1W191F is a more persistent H2O2 signaling protein than wild-type Ccp1
W191G
-
provides a specific site near heme from which substrates might be oxidized
W51H
-
distal pocket mutant, shift in reduction potential to -200 mV. Analysis of spectroscopic properties
W51H
-
altered electronic absorption spectra, indicating that the heme group in the mutants is six-coordinate rather than five-coordinate as it is in wild-type cytochrome c peroxidase, weaker effect on cyanide binding, with the cyanide affinity only 2-8times weaker than for cytochrome c peroxidase
W51H/H52L
-
distal pocket mutant, shift in reduction potential to -162 mV. Analysis of spectroscopic properties
W51H/H52L
-
altered electronic absorption spectra, indicating that the heme group in the mutants is six-coordinate rather than five-coordinate as it is in wild-type cytochrome c peroxidase, weaker effect on cyanide binding, with the cyanide affinity only 2-8times weaker than for cytochrome c peroxidase
W51H/H52W
-
altered electronic absorption spectra, indicating that the heme group in the mutants is six-coordinate rather than five-coordinate as it is in wild-type cytochrome c peroxidase, weaker effect on cyanide binding, with the cyanide affinity only 2-8times weaker than for cytochrome c peroxidase
Y36A
-
site-directed mutagenesis, Tyr36 directly blocks the equivalent ascorbate binding site in CcP and was therefore replaced with a less bulky residue
Y36A/N184R
-
site-directed mutagenesis, no significant spectroscopic changes on reaction with stoichiometric or higher amounts of H2O2 are seen
Y36A/N184R/W191F
-
site-directed mutagenesis, cytochrome c peroxidase enzyme can duplicate the substrate binding properties of ascorbate peroxidase through the introduction of relatively modest structural changes at Tyr36 and Asn184, no evidence for a porphyrin pi-cation radical
Y36A/W191F
-
site-directed mutagenesis, no significant spectroscopic changes on reaction with stoichiometric or higher amounts of H2O2 are seen
W191F
-
catalytically inactive mature Ccp1 mutant, Ccp1W191F is a more persistent H2O2 signaling protein than wild-type Ccp1
-
H52L |
Saccharomyces cerevisiae Red Star
-
site-directed mutagenesis, a distal pocket mutant
-
R48L/W51L/H52L |
Saccharomyces cerevisiae Red Star
-
site-directed mutagenesis, a distal pocket mutant
-
P75T/H81K/E84Q
-
site-directed mutagenesis
additional information
-
a mutant lacking the putative cytochrome c peroxidase DocA shows a 10fold reduction in colonization of the chick cecum compared to wild-type enzyme, a mutant lacking the putative cytochrome c peroxidase CJJ0382 demonstrates a maximal 50fold colonization defect that is dependent on the inoculum dose
additional information
Campylobacter jejuni 81-176
-
a mutant lacking the putative cytochrome c peroxidase DocA shows a 10fold reduction in colonization of the chick cecum compared to wild-type enzyme, a mutant lacking the putative cytochrome c peroxidase CJJ0382 demonstrates a maximal 50fold colonization defect that is dependent on the inoculum dose
-
additional information
-, Q6URB0
disruption and deletion mutants show intracellular growth defects in macrophage like cells in vitro. The enzyme provides protection against oxidative stress within macrophages in vitro
additional information
Cryptococcus neoformans H99
-
disruption and deletion mutants show intracellular growth defects in macrophage like cells in vitro. The enzyme provides protection against oxidative stress within macrophages in vitro
-
M297H
Geobacter sulfurreducens DSM 12127
-
site-directed mutagenesis
-
additional information
-
mutant with deletion of the translation start codon and 800 bp of the enzyme gene. Almost as active as the wild-type enzyme
H71G/W94A
-
4% activity compared to the wild type enzyme, contains a high-spin, presumably five-coordinate, peroxidatic heme site; about 4% of wild-type activity. Five-coordinate, peroxidatic heme structure contrary to six-coordinate structure of wild-type, formation of a porphyrin radical species during catalysis
additional information
-
an unactivated mutant devoid of the protein loop shows 10% of turnover activity of the wild type enzyme in the activated form
K264C
-
characterization of complex with yeast cytochrome c mutant K79C. Cytochrome c is covalently bound and located 90 from its primary binding site. Catalytic activity is similar to wild-type cytochrome c peroxidase
additional information
-
distal pocket mutants, proximal pocket mutants, channel mutants, surface mutations
additional information
-
variant of cytochrome c peroxidase in which the proposed electron transfer pathway is excised from the structure, leaving a water filled channel in its place
additional information
-
significant decreases in the rate of reaction with hydrogen peroxide with 56-, 300-, and 6200fold decreases for mutant (W51H), mutant (W51H/H52W), and mutant (W51H/H52L), respectively, compared to that of wild-type cytochrome c peroxidase, indicating that the position of the distal histidine has a significant effect on the rate of reaction with H2O2
additional information
-
construction of three apolar distal heme pocket mutants of CcP with altered pH dependencies compared to the wild-type enzyme
additional information
-
construction of three apolar distal heme pocket mutants of CcP with enhanced binding of 1-methoxynaphthalene near the heme and enhanced hydroxylation activity of 1-methoxynaphthalene
additional information
-
generation of enzyme disruption mutant DELTAccp1, SOD2 activity is significantly lower in W191F ccp1 mutant cells than in DELTAccp1 deletion mutant cells
additional information
-
pH dependence of the reduction potential and heme binding site structure analysis of wild-type and mutant enzymes using photoreduction and spectroscopic methods, respectively, overview
Y39A
-
site-directed mutagenesis, mutation has a destabilizing effect on binding
additional information
-
generation of enzyme disruption mutant DELTAccp1, SOD2 activity is significantly lower in W191F ccp1 mutant cells than in DELTAccp1 deletion mutant cells
-
H52Q |
Saccharomyces cerevisiae Red Star
-
site-directed mutagenesis, a distal pocket mutant
-
additional information
Saccharomyces cerevisiae Red Star
-
pH dependence of the reduction potential and heme binding site structure analysis of wild-type and mutant enzymes using photoreduction and spectroscopic methods, respectively, overview
-
M219Q/F247N
-
site-directed mutagenesis
additional information
-
construction of a DELTAccpA mutant Shewanella oneidensis line
W191F
-
study of the role of intracomplex dynamics in controlling electron transfer, use of Zn-enzyme in 1:1 complex with cytochrome c
additional information
Q5NNF0, -
construction of disruption knockout mutant DELTAZmcytC, phenotype, overview
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
complete suppression of enzyme activity by niric oxide. Nitrosyl complexes of cytochrome c produced during inhibition are sensitive to laser irradiation and are photolyzed during irradiation. Decomposition leads to partial restoration of enzyme activity. nitric oxide and laser irradiation may serve as instruments for regulating the peroxidase activity of cytochrome c and, probably, apoptosis
-
mixed-monolayer protected colloids selectively interact with enzyme and cytochrome c based upon charge complementarity. Surface-functionalized colloids with gold cores and thiolates terminating in trimethyl-amine bind reversibly and proteins retain their native structure. Binding is reversed by high ionic strength
-
reconstitution of holoenzyme
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
biotechnology
-
cytochrome c peroxidase as a platform to develop specific peroxygenation catalysts