25810
Chloroperoxidase from Caldariomyces fumago
aqueous suspension, brown, >10,000 U/mL
Synonym(s):
Chloride Peroxidase, Chloride:hydrogen-peroxide oxidoreductase
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Recommended Products
biological source
fungus (Caldariomyces fumago)
Quality Level
form
aqueous suspension
concentration
>10,000 U/mL
color
brown
storage temp.
2-8°C
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General description
Chloroperoxidase (CPO) is a major heme-containing, synthetic and versatile enzyme, obtained from Caldariomyces fumago.
Application
A useful alternative to lactoperoxidase for 131I ion labeling studies, for bromination of proteins, and for 36Cl labeling of macromolecules in long-term isolation procedures.
Biochem/physiol Actions
Chloroperoxidase (CPO) helps in the catalysis of oxidation reactions with the help of hydrogen peroxide. It displays peroxidase, catalase and cytochrome P450-like functions. CPO also plays a role in catalyzing halogenation reactions.
Unit Definition
1 U corresponds to the amount of enzyme which converts 1 μmol of monochlorodimedone to dichlorodimedone per minute at pH 2.75 and 25 °C in the presence of KCl and H2O2.
Physical form
Supplied as a suspension in 0.1 M sodium phosphate pH 4.0.
Other Notes
Oxidation of aminopyrine; Chloroperoxidase, a peroxidase with potential; Chloroperoxidase-catalyzed asymmetric transformations.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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H Sayo et al.
Chemical & pharmaceutical bulletin, 37(12), 3347-3350 (1989-12-01)
Although in the absence of halide ion chloroperoxidase did not catalyze the ethylhydroperoxide (EHP)-supported oxidation of aminopyrine, in the presence of Br- or Cl-, chloroperoxidase did catalyze the oxidation of aminopyrine, generating the aminopyrine cation radical (AP+). The initial rate
M.A. Pickard et al.
Journal of Industrial Microbiology, 7, 235-235 (1991)
Fast and efficient purification of chloroperoxidase from C. fumago
Yazbik V and Ansorge SM
Process. Biochem., 45(2), 279-283 (2010)
H. Fu et al.
The Journal of Organic Chemistry, 57, 7265-7265 (1992)
Daniel Andrew et al.
Biochemical and biophysical research communications, 415(4), 646-649 (2011-11-15)
Azide is a well-known inhibitor of heme-enzymes. Herein, we report the counter-intuitive observation that at some concentration regimes, incorporation of azide in the reaction medium enhances chloroperoxidase (CPO, a heme-enzyme) mediated one-electron abstractions from several substrates. A diffusible azidyl radical
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