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Information on EC 1.11.1.5 - cytochrome-c peroxidase and Organism(s) Pseudomonas aeruginosa and UniProt Accession P14532

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EC Tree
     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.5 cytochrome-c peroxidase
IUBMB Comments
A hemoprotein.
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This record set is specific for:
Pseudomonas aeruginosa
UNIPROT: P14532
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Word Map
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
cytochrome c peroxidase, cytochrome-c peroxidase, diheme cytochrome c peroxidase, cytochrome peroxidase, cjj0382, apocytochrome c peroxidase, cytochrome c-551 peroxidase, di-heme cytochrome c peroxidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cytochrome c peroxidase
-
apocytochrome c peroxidase
-
-
-
-
cytochrome c peroxidase
cytochrome c-551 peroxidase
-
-
-
-
cytochrome c-H2O oxidoreductase
-
-
-
-
cytochrome peroxidase
-
-
-
-
mesocytochrome c peroxidase azide
-
-
-
-
mesocytochrome c peroxidase cyanate
-
-
-
-
mesocytochrome c peroxidase cyanide
-
-
-
-
peroxidase, cytochrome c
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 ferrocytochrome c + H2O2 = 2 ferricytochrome c + 2 H2O
show the reaction diagram
reaction scheme
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
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reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ferrocytochrome-c:hydrogen-peroxide oxidoreductase
A hemoprotein.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-53-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
azurin + H2O2
oxidized azurin + ?
show the reaction diagram
-
blue copper protein
-
-
?
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
ferrocytochrome c551 + H2O2
ferricytochrome c551 + OH-
show the reaction diagram
-
-
-
?
reduced cytochrome c551 + H2O2
oxidized cytochrome c551 + H2O
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ferrocytochrome c + H2O2
ferricytochrome c + H2O
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.025
H2O2
protein film voltammetry, the midpoint potentials of the turnover signals are used to calculate Michaelis-Menten kinetics
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36230
-
calculated
36250
-
electrospray mass spectrometry
36270
-
MALDI-TOF mass spectrometry
44000
-
amino acid analysis
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no glycoprotein
-
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
with 24% PEG 600, 0.2 M imidazole malate pH 5.5, 20 mM dithiothreitol
diffraction limit 2.5 A
-
resolution 2.4 A
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H71G/W94A
additional information
-
an unactivated mutant devoid of the protein loop shows 10% of turnover activity of the wild type enzyme in the activated form
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
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
702343
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable during degassing under vacuum except in presence of detergent
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
precipitation, DEAE-Sepharose followed by S-100 size exclusion chromatography
S-Sepharose column chromatography and Superdex-75 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli JM109 (DE3) cells
expression in Escherichia coli JM109(DE3) with pETCCP coexpressed with pEC86
expressed in Escherichia coli JM109 (DE3) cells
-
expression in Escherichia coli
-
mutants expressed in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ellfolk, N.; Rnnberg, M.; Aasa, R.; Andreasson, L.E.; Vnngard, T.
Properties and function of the two hemes in Pseudomonas cytochrome c peroxidase
Biochim. Biophys. Acta
743
23-30
1983
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Foote, N.; Thompson, A.C.; Barber, D.; Greenwood, C.
Pseudomonas cytochrome C-551 peroxidase. A purification procedure and study of CO-binding kinetics
Biochem. J.
209
701-707
1983
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Soininen, R.; Ellfolk, N.
Pseudomonas cytochrome c peroxidase. 8. The amino acid composition of the enzyme
Acta Chem. Scand.
27
2193-2198
1973
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Samyn, B.; Van Craenenbroeck, K.; De Smet, L.; Vandenberghe, I.; Pettigrew, G.; Van Beeumen, J.
A reinvestigation of the covalent structure of Pseudomonas aeruginosa cytochrome c peroxidase
FEBS Lett.
377
145-149
1995
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Ronnberg, M.; Araiso, T.; Ellfolk, N.; Dunford, H.B.
The reaction between reduced azurin and oxidized cytochrome c peroxidase from Pseudomonas aeruginosa
J. Biol. Chem.
256
2471-2474
1981
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Fulop, V.; Little, R.
Crystallization and preliminary X-ray analysis of the di-haem cytochrome c peroxidase from Pseudomonas aeruginosa
J. Mol. Biol.
232
1208 - 1210
1993
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Fulop, V.; Ridout, C.J.; Greenwood, C.; Hajdu, J.
Crystal structure of the di-haem cytochrome c peroxidase from Pseudomonas aeruginosa
Structure
3
1225-1233
1995
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Lee, Y.; Boycheva, S.; Brittain, T.; Boyd, P.D.
Intramolecular electron transfer in the dihaem cytochrome c peroxidase of Pseudomonas aeruginosa
Chembiochem
8
1440-1446
2007
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Echalier, A.; Brittain, T.; Wright, J.; Boycheva, S.; Mortuza, G.B.; Fueloep, V.; Watmough, N.J.
Redox-linked structural changes associated with the formation of a catalytically competent form of the diheme cytochrome c peroxidase from Pseudomonas aeruginosa
Biochemistry
47
1947-1956
2008
Pseudomonas aeruginosa (P14532), Pseudomonas aeruginosa
Manually annotated by BRENDA team
Hsiao, H.C.; Boycheva, S.; Watmough, N.J.; Brittain, T.
Activation of the cytochrome c peroxidase of Pseudomonas aeruginosa. The role of a heme-linked protein loop: a mutagenesis study
J. Inorg. Biochem.
101
1133-1139
2007
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Becker, C.F.; Watmough, N.J.; Elliott, S.J.
Electrochemical evidence for multiple peroxidatic heme states of the diheme cytochrome c peroxidase of Pseudomonas aeruginosa
Biochemistry
48
87-95
2009
Pseudomonas aeruginosa (P14532), Pseudomonas aeruginosa
Manually annotated by BRENDA team