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Literature summary for 1.11.1.10 extracted from

  • Hallenberg, P.F.; Hager, L.P.
    Purification of chloroperoxidase from Caldariomyces fumago (1978), Methods Enzymol., 52, 521-529.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
azide
-
Leptoxyphium fumago
cyanide
-
Leptoxyphium fumago

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Leptoxyphium fumago
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
42000
-
equilibrium sedimentation Leptoxyphium fumago

Organism

Organism UniProt Comment Textmining
Leptoxyphium fumago
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
-
Leptoxyphium fumago

Purification (Commentary)

Purification (Comment) Organism
-
Leptoxyphium fumago

Source Tissue

Source Tissue Comment Organism Textmining
culture medium
-
Leptoxyphium fumago
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2200
-
-
Leptoxyphium fumago

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2O2
-
Leptoxyphium fumago H2O + O2
-
?
monochlorodimedon + Cl- + H2O2
-
Leptoxyphium fumago dichlorodimedon + H2O
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
2.8
-
halide-anion dependent evolution of oxygen from hydrogen peroxide Leptoxyphium fumago
3
-
halogenation and halogen-dependent peroxidation Leptoxyphium fumago
4.8
-
halide ion independent evolution of oxygen from hydrogen peroxide Leptoxyphium fumago

pH Stability

pH Stability pH Stability Maximum Comment Organism
1.5
-
4°C, stable for several h Leptoxyphium fumago
3 6.5 4°C, in presence of 0.1 M fluoride, stable for several days Leptoxyphium fumago

Cofactor

Cofactor Comment Organism Structure
heme enzyme contains 1 mol of ferriprotoporphyrin IX per mol of enzyme Leptoxyphium fumago