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Literature summary for 1.11.1.7 extracted from

  • Nobrega, C.S.; Raposo, M.; Van Driessche, G.; Devreese, B.; Pauleta, S.R.
    Biochemical characterization of the bacterial peroxidase from the human pathogen Neisseria gonorrhoeae (2017), J. Inorg. Biochem., 171, 108-119 .
    View publication on PubMed
Search for more literature for 1.11.1.7

Cloned(Commentary)

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 [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.004
-
 H2O2 pH 7.0, 25°C Neisseria gonorrhoeae

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
-
 Neisseria gonorrhoeae
-
-

Metals/Ions

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 [Da] Molecular Weight Maximum [Da] Comment Organism
42000
-
 gel filtration Neisseria gonorrhoeae
68000
-
 gel filtration, presence of Ca2+ Neisseria gonorrhoeae

Organism

Organism UniProt Comment Textmining
Neisseria gonorrhoeae Q5F809
-
-
Neisseria gonorrhoeae FA 1090 Q5F809
-
-

Substrates and Products (Substrate)

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

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

Synonyms Comment Organism
BCcP
-
 Neisseria gonorrhoeae
NGO_0994
-
 Neisseria gonorrhoeae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
 Neisseria gonorrhoeae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Neisseria gonorrhoeae

Cofactor

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