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Sigma-Aldrich

Chloroperoxidase from Caldariomyces fumago

aqueous suspension, brown, >10,000 U/mL

Sinónimos:

Chloride Peroxidase, Chloride:hydrogen-peroxide oxidoreductase

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About This Item

Número de CAS:
9055-20-3
Comisión internacional de enzimas:
1.11.1.10 (BRENDA, IUBMB)
MDL number:
MFCD00130774
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

fungus (Caldariomyces fumago)

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

enthält 0.1 M Natriumphosphat pH 4.0

Other Notes

Oxidation of aminopyrine; Chloroperoxidase, a peroxidase with potential; Chloroperoxidase-catalyzed asymmetric transformations.

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves

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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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