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Literature summary for 1.11.1.B2 extracted from

  • Wiesner, W.; van Pee, K.H.; Lingens, F.
    Purification and characterization of a novel bacterial non-heme chloroperoxidase from Pseudomonas pyrrocinia (1988), J. Biol. Chem., 263, 13725-13732.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
azide no inhibition Burkholderia pyrrocinia
F- 0.18 mM, 50% inhibition Burkholderia pyrrocinia
H2O2 above 50 mM Burkholderia pyrrocinia
KCN 0.01 mM, 50% inhibition Burkholderia pyrrocinia

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.7
-
H2O2
-
Burkholderia pyrrocinia
30
-
Br-
-
Burkholderia pyrrocinia

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
32000
-
2 * 32000, SDS-PAGE Burkholderia pyrrocinia
64000
-
-
Burkholderia pyrrocinia

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-(2-amino-3-chlorophenyl)pyrrole + Cl- + H2O2 Burkholderia pyrrocinia enzyme is involved in the biosynthesis of the antibiotic pyrrolnitrin aminopyrrolnitrin + ?
-
?

Organism

Organism UniProt Comment Textmining
Burkholderia pyrrocinia
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Burkholderia pyrrocinia

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.24
-
bromoperoxidase activity Burkholderia pyrrocinia
4.23
-
chloroperoxidase activity Burkholderia pyrrocinia

Storage Stability

Storage Stability Organism
4°C, 0.1 M sodium acetate buffer, pH 3.5-5.5, 0.1 M ammonium acetate buffer, pH 6.0-7.0, 0.1 M potassium phosphate buffer, pH 7.0-8.5, stable for over 2 months Burkholderia pyrrocinia

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-(2-amino-3-chlorophenyl)pyrrole + Cl- + H2O2
-
Burkholderia pyrrocinia aminopyrrolnitrin + ?
-
?
4-(2-amino-3-chlorophenyl)pyrrole + Cl- + H2O2 enzyme is involved in the biosynthesis of the antibiotic pyrrolnitrin Burkholderia pyrrocinia aminopyrrolnitrin + ?
-
?
indole + Cl- + H2O2
-
Burkholderia pyrrocinia oxindole + monochloroindole + H2O
-
?
monochlorodimedon + Cl- + H2O2 no activity Burkholderia pyrrocinia dichlorodimedon + H2O
-
?
monochlorodimedone + Br- + H2O2
-
Burkholderia pyrrocinia ?
-
?
additional information no peroxidase activity, no catalase activity Burkholderia pyrrocinia ?
-
?

Subunits

Subunits Comment Organism
dimer 2 * 32000, SDS-PAGE Burkholderia pyrrocinia

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
-
Burkholderia pyrrocinia

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
2 h, stable Burkholderia pyrrocinia
70
-
10 min, 50% loss of activity Burkholderia pyrrocinia

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4 4.5
-
Burkholderia pyrrocinia

pH Stability

pH Stability pH Stability Maximum Comment Organism
3.5 8.5 stable Burkholderia pyrrocinia

Cofactor

Cofactor Comment Organism Structure
additional information non-heme chloroperoxidase Burkholderia pyrrocinia