Literature summary 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.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
1.11.1.5 |
expression in Escherichia coli |
Neisseria gonorrhoeae |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
1.11.1.5 |
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
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
1.11.1.5 |
nitrite |
2 mM, in the presence of 0.88 M of H2O2, inhibits 50% enzyme activity |
Neisseria gonorrhoeae |
|
Localization
EC Number |
Localization |
Comment |
Organism |
GeneOntology No. |
Textmining |
---|
1.11.1.5 |
membrane |
the enzyme is a lipoprotein sarkosyl-soluble |
Neisseria gonorrhoeae |
16020 |
- |
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
1.11.1.5 |
ferrocytochrome c + H2O2 |
Neisseria gonorrhoeae |
- |
ferricytochrome c + H2O |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.11.1.5 |
Neisseria gonorrhoeae |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
1.11.1.5 |
inner membrane proteins solubilized in sarkosyl solution and precipitated with ethanol are purified by affinity chromatography |
Neisseria gonorrhoeae |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
1.11.1.5 |
ferrocytochrome c + H2O2 |
- |
Neisseria gonorrhoeae |
ferricytochrome c + H2O |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
1.11.1.5 |
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 |