Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli, regions encoding the signal peptide and H8 epitope segments in the N-terminus of the protein are excluded | Neisseria gonorrhoeae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.004 | - |
H2O2 | pH 7.0, 25°C | Neisseria gonorrhoeae |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
periplasm | - |
Neisseria gonorrhoeae | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | presence of Ca2+ induces dimerization and an endothermic transition, with a Tm of 46.9°C | Neisseria gonorrhoeae |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
42000 | - |
gel filtration | Neisseria gonorrhoeae |
68000 | - |
gel filtration, presence of Ca2+ | Neisseria gonorrhoeae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Neisseria gonorrhoeae | Q5F809 | - |
- |
Neisseria gonorrhoeae FA 1090 | Q5F809 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2 | - |
Neisseria gonorrhoeae | ? + H2O | - |
? | |
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2 | - |
Neisseria gonorrhoeae FA 1090 | ? + H2O | - |
? | |
additional information | the rate-limiting step in the catalytic cycle is the electron transfer between the two hemes | Neisseria gonorrhoeae | ? | - |
? | |
additional information | the rate-limiting step in the catalytic cycle is the electron transfer between the two hemes | Neisseria gonorrhoeae FA 1090 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 38780, calculated for recombinant protein. The as-isolated BCCP is a monomer that does not show a tendency to dimerize at high ionic strength. In presence of Ca2+, dimerization takes place | Neisseria gonorrhoeae |
monomer | 1 * 38780, calculated for recombinant protein. The as-isolated BCCP is a monomer that does not show a tendency to dimerize at high ionic strength. In presence of Ca2+, dimerization takes place | Neisseria gonorrhoeae |
Synonyms | Comment | Organism |
---|---|---|
BCcP | - |
Neisseria gonorrhoeae |
NGO_0994 | - |
Neisseria gonorrhoeae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
- |
Neisseria gonorrhoeae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
- |
Neisseria gonorrhoeae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | holo-form binds two c-type hemes covalently bound to the polypeptide chain, a high-potential E heme and a low-potential P heme, with redox potentials of (+310 mV) and (-190 mV/-300 mV), respectively in the presence of calcium ions, at pH 7.5. A calcium dependent reductive activation mechanism is present, in which P heme is bis-His coordinated low-spin in the fully oxidized state of the enzyme, and becomes penta-coordinated high-spin upon reduction of E heme in the presence of calcium ions. The rate-limiting step in the catalytic cycle is the electron transfer between the two hemes | Neisseria gonorrhoeae |