Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.11.1.B2 extracted from

  • Bantleon, R.; Altenbuchner, J.; van Pee, K.H.
    Chloroperoxidase from Streptomyces lividans: isolation and characterization of the enzyme and the corresponding gene (1994), J. Bacteriol., 176, 2339-2347.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
3000fold overexpression in Streptomyces aureofaciens Tü24-88 Streptomyces lividans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1 2.3 H2O2 bromination of monochlorodimedone Streptomyces lividans
11
-
Br- bromination of monochlorodimedone Streptomyces lividans

Metals/Ions

Metals/Ions Comment Organism Structure
additional information enzyme contains no metal Streptomyces lividans

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
32000
-
2 * 32000, SDS-PAGE Streptomyces lividans
64000
-
gel filtration Streptomyces lividans

Organism

Organism UniProt Comment Textmining
Streptomyces lividans
-
TK64
-
Streptomyces lividans TK64
-
TK64
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Streptomyces lividans

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Streptomyces lividans

Storage Stability

Storage Stability Organism
-20°C, sodium acetate buffer, pH 5.5, stable for months Streptomyces lividans
6°C, 20 mM sodium acetate buffer, pH 3.5-6, or ammonium acetate buffer, pH 6-8, stable for weeks Streptomyces lividans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
indole + Br- + H2O2
-
Streptomyces lividans ?
-
?
indole + Br- + H2O2
-
Streptomyces lividans TK64 ?
-
?
indole + Cl- + H2O2
-
Streptomyces lividans oxindole + monochloroindole + H2O
-
?
indole + Cl- + H2O2
-
Streptomyces lividans TK64 oxindole + monochloroindole + H2O
-
?
monochlorodimedon + Cl- + H2O2 no activity Streptomyces lividans dichlorodimedon + H2O
-
?
monochlorodimedon + Cl- + H2O2 no activity Streptomyces lividans TK64 dichlorodimedon + H2O
-
?
monochlorodimedone + Br- + H2O2 all bacterial nonheme haloperoxidases catalyze the bromination, but not the chlorination of monochlorodimedone. Therefore, they are isolated as bromoperoxidases. While the bromination of organic compounds is very unspecific, a substrate specificity exists for the chlorination. Appropriate substrates such as indole or phenyl pyrrole derivatives are chlorinated Streptomyces lividans ?
-
?
monochlorodimedone + Br- + H2O2 all bacterial nonheme haloperoxidases catalyze the bromination, but not the chlorination of monochlorodimedone. Therefore, they are isolated as bromoperoxidases. While the bromination of organic compounds is very unspecific, a substrate specificity exists for the chlorination. Appropriate substrates such as indole or phenyl pyrrole derivatives are chlorinated Streptomyces lividans TK64 ?
-
?

Subunits

Subunits Comment Organism
dimer 2 * 32000, SDS-PAGE Streptomyces lividans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5 5.5 bromination of monochlorodimedone Streptomyces lividans

Cofactor

Cofactor Comment Organism Structure
additional information non-heme chloroperoxidase Streptomyces lividans