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Literature summary for 1.11.1.5 extracted from

  • Pulcu, G.S.; Frato, K.E.; Gupta, R.; Hsu, H.R.; Levine, G.A.; Hendrich, M.P.; Elliott, S.J.
    The diheme cytochrome c peroxidase from Shewanella oneidensis requires reductive activation (2012), Biochemistry, 51, 974-985.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.11.1.5

Activating Compound

Activating Compound Comment Organism Structure
additional information CcP requires reductive activation for full activity Shewanella oneidensis

Cloned(Commentary)

Cloned (Comment) Organism
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) Shewanella oneidensis

Protein Variants

Protein Variants Comment Organism
M219Q/F247N site-directed mutagenesis Shewanella oneidensis
P75T/H81K/E84Q site-directed mutagenesis Shewanella oneidensis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics Shewanella oneidensis

Organism

Organism UniProt Comment Textmining
Shewanella oneidensis
-
 gene SO2178
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Shewanella oneidensis

Synonyms

Synonyms Comment Organism
CCP
-
 Shewanella oneidensis
cytochrome c peroxidase
-
 Shewanella oneidensis
diheme cytochrome c peroxidase
-
 Shewanella oneidensis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
23
-
 assay at Shewanella oneidensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 assay at Shewanella oneidensis

Cofactor

Cofactor Comment Organism Structure
heme diheme cytochrome c peroxidase Shewanella oneidensis

General Information

General Information Comment Organism
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 Shewanella oneidensis