C0887
Chloroperoxidase from Caldariomyces fumago
buffered aqueous suspension, 1,000-2,000 units/mg protein (E1%/280)
Sinónimos:
Chloride Peroxidase, Chloride:hydrogen-peroxide oxidoreductase
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About This Item
Número de CAS:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Productos recomendados
biological source
fungus (Caldariomyces fumago)
Quality Level
form
buffered aqueous suspension
specific activity
1,000-2,000 units/mg protein (E1%/280)
mol wt
42 kDa
absorbance ratio
RZ ~1.0
storage temp.
2-8°C
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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) is a 42,000 Da extracellular heme glycoenzyme containing ferriprotoporphyrin IX as the prosthetic group. CPO is secreted from fungus and exhibits a broad spectrum of chemical reactivities. It is a peroxide-dependent chlorinating enzyme. It also catalyzes peroxidase-, catalase- and cytochrome P450-type reactions of dehydrogenation, H2O2 decomposition and oxygen insertion, respectively. The enzyme has magnetic and spectroscopic properties similar to that of cyctochrome P-450. CPO from the fungus Caldariomyces fumago has the capacity to chlorinate aromatic hydrocarbons, including polycyclic aromatic hydrocarbons (PAHs).
Unit Definition
One unit will catalyze the conversion of 1.0 μmole of monochlorodimedon to dichlorodimedon per min at pH 2.75 at 25 °C in the presence of potassium chloride and H2O2.
Physical form
Purified suspension in 0.1 M sodium phosphate solution, pH approx. 4.5
Inhibitor
Referencia del producto
Descripción
Precios
Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
Certificados de análisis (COA)
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R Vázquez-Duhalt et al.
Phytochemistry, 58(6), 929-933 (2001-10-31)
Chloroperoxidase from Caldariomyces fumago was able to chlorinate 17 of 20 aromatic hydrocarbons assayed in the presence of hydrogen peroxide and chloride ions. Reaction rates varied from 0.6 min(-1) for naphthalene to 758 min(-1) for 9-methylanthracene. Mono-, di- and tri-chlorinated
René Ullrich et al.
Applied and environmental microbiology, 70(8), 4575-4581 (2004-08-06)
Agrocybe aegerita, a bark mulch- and wood-colonizing basidiomycete, was found to produce a peroxidase (AaP) that oxidizes aryl alcohols, such as veratryl and benzyl alcohols, into the corresponding aldehydes and then into benzoic acids. The enzyme also catalyzed the oxidation
Ilona F Persoon et al.
Journal of endodontics, 38(1), 72-74 (2011-12-14)
The aim of this study was to explore the antimicrobial effect of vanadium chloroperoxidase (VCPO) reaction products on Enterococcus faecalis biofilms of 4 different strains. Twenty-four-hour biofilms of E. faecalis strains V583, ER5/1, E2, and OS-16 were incubated in mixtures
Alexander N Morozov et al.
Biophysical journal, 100(4), 1066-1075 (2011-02-16)
Molecular dynamics simulations of an explicitly solvated cis-β-methylstyrene/chloroperoxidase-Compound I complex are performed to determine the cause of the high enantiospecificity of epoxidation. From the simulations, a two-dimensional free energy potential is calculated to distinguish binding potential wells from which reaction
Peter Bernhardt et al.
Journal of the American Chemical Society, 133(12), 4268-4270 (2011-03-10)
Halogenases catalyze reactions that introduce halogen atoms into electron-rich organic molecules. Vanadium-dependent haloperoxidases are generally considered to be promiscuous halogenating enzymes that have thus far been derived exclusively from eukaryotes, where their cellular function is often disputed. We now report
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