C0887
氯过氧化物酶 来源于Caldariomyces fumago
buffered aqueous suspension, 1,000-2,000 units/mg protein (E1%/280)
别名:
氯化物过氧化物酶, 氯化物：过氧化氢氧化还原酶
产品名称
氯过氧化物酶 来源于Caldariomyces fumago, buffered aqueous suspension, 1,000-2,000 units/mg protein (E1%/280)
biological source
fungus (Caldariomyces fumago)
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
Quality Level
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Application
在 131 I 离子标记研究、蛋白质溴化和 36 Cl 标记大分子的长期分离程序中，可作为乳过氧化物酶的有效替代品。
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).
Other Notes
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
存储类别
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
常规特殊物品
此项目有
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
Adam C Chamberlin et al.
The journal of physical chemistry. B, 115(13), 3642-3647 (2011-03-18)
OLYP/TZP calculations on two symmetrized model complexes [Fe(TPP)(py)(2)](2+) and [Fe(TPP)(PhNC)(2)](2+) (TPP = meso-tetraphenylporphyrin, py = pyridine, PhNC = phenylisocyanide) reveal dense manifolds of low-energy electronic states. For the latter complex, broken-symmetry calculations successfully reproduce the unique S = 0 ground
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
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)
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