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Literature summary for 1.11.1.5 extracted from

  • Turner, S.; Reid, E.; Smith, H.; Cole, J.
    A novel cytochrome c peroxidase from Neisseria gonorrhoeae: a lipoprotein from a Gram-negative bacterium (2003), Biochem. J., 373, 865-873.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Neisseria gonorrhoeae

Protein Variants

Protein Variants Comment Organism
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 Neisseria gonorrhoeae

Inhibitors

Inhibitors Comment Organism Structure
nitrite 2 mM, in the presence of 0.88 M of H2O2, inhibits 50% enzyme activity Neisseria gonorrhoeae

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane the enzyme is a lipoprotein sarkosyl-soluble Neisseria gonorrhoeae 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ferrocytochrome c + H2O2 Neisseria gonorrhoeae
-
ferricytochrome c + H2O
-
?

Organism

Organism UniProt Comment Textmining
Neisseria gonorrhoeae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
inner membrane proteins solubilized in sarkosyl solution and precipitated with ethanol are purified by affinity chromatography Neisseria gonorrhoeae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ferrocytochrome c + H2O2
-
Neisseria gonorrhoeae ferricytochrome c + H2O
-
?

Subunits

Subunits Comment Organism
More 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 Neisseria gonorrhoeae