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C0278
Chloroperoxidase from Caldariomyces fumago
buffered aqueous suspension, ≥3,000 units/mL
Synonim(y):
Chloride Peroxidase, Chloride:hydrogen-peroxide oxidoreductase
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About This Item
Numer CAS:
Numer MDL:
Kod UNSPSC:
12352204
NACRES:
NA.54
Polecane produkty
Formularz
buffered aqueous suspension
masa cząsteczkowa
42 kDa
stężenie
≥3,000 units/mL
Warunki transportu
wet ice
temp. przechowywania
2-8°C
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Opis ogólny
Chloroperoxidase is a heme containing glycoprotein that is secreted from fungus. Chloroperoxidase (CPO) is a extracellular heme glycoenzyme containing ferriprotoporphyrin IX as the prosthetic group.
Zastosowanie
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.
Chloroperoxidase from Caldariomyces fumagois is useful alternative to lactoperoxidase for 131I ion labeling studies, for bromination of proteins, and for 36Cl labeling of macromolecules in long-term isolation procedures. It has been used to study biocatalytic oxidation in polymersome nanoreactors .
It has been used to study biocatalytic oxidation in polymersome nanoreactors.
Działania biochem./fizjol.
Chloroperoxidase (CPO) is secreted from fungus and exhibits a broad spectrum of chemical reactivities. It is a peroxide-dependent chlorinating enzyme and it also catalyzes peroxidase, catalase and cytochrome P450-type reactions of dehydrogenation, hydrogenperoxide (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). PAHs are considered to be a potential health risk because of their possible carcinogenic and mutagenic activities and are widely dispersed in the environment.
Definicja jednostki
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.
Postać fizyczna
Crude suspension in 0.1 M sodium phosphate, pH ~4.5
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Inhibitor
Numer produktu
Opis
Cennik
Hasło ostrzegawcze
Danger
Zwroty wskazujące rodzaj zagrożenia
Zwroty wskazujące środki ostrożności
Klasyfikacja zagrożeń
Resp. Sens. 1
Kod klasy składowania
10 - Combustible liquids
Klasa zagrożenia wodnego (WGK)
WGK 3
Temperatura zapłonu (°F)
Not applicable
Temperatura zapłonu (°C)
Not applicable
Środki ochrony indywidualnej
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
C M Hosten et al.
The Journal of biological chemistry, 269(19), 13966-13978 (1994-05-13)
Near-ultraviolet resonance Raman spectra of chloroperoxidase derivatives and high valent intermediates show frequencies that can be systematically assigned. In accord with previous observations of low v4 frequencies for the ferric enzyme, and quite low v4 frequencies for the ferrous enzyme
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
Chaonan Li et al.
Applied biochemistry and biotechnology, 165(7-8), 1691-1707 (2011-09-29)
Chloroperoxidase (CPO) is thought to be the most versatile heme-containing enzyme with enormous applications in organic synthesis, biotransformation, pharmaceutical production, and detoxification of environmental pollutants. Any improvement in the stability of this enzyme will greatly enhance its application in the
Kelath Murali Manoj et al.
PloS one, 5(5), e10601-e10601 (2010-05-26)
Many heme enzymes show remarkable versatility and atypical kinetics. The fungal extracellular enzyme chloroperoxidase (CPO) characterizes a variety of one and two electron redox reactions in the presence of hydroperoxides. A structural counterpart, found in mammalian microsomal cytochrome P450 (CYP)
Rabindra Kumar Behera et al.
Journal of inorganic biochemistry, 104(11), 1185-1194 (2010-08-17)
The site specific mutants of the thermophilic P450 (P450 175A1 or CYP175A1) were designed to introduce residues that could act as acid-base catalysts near the active site to enhance the peroxidases activity. The Leu80 in the distal heme pocket of
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