| Identification | Back Directory | [Name]
Cholesterol oxidase | [CAS]
9028-76-6 | [Synonyms]
REC-COD
C:C&B11
9028-76-6
EC 1.1.3.6
EC: 1.1.3.6
Choleterol oxidase
CHOLESTEROL OXIDASE
Cholesterin oxidase
Oxidase, cholesterol
Cholesterol oxidase20.4
3-Hydroxysteroid oxidase
Cholecalciferol(VitaminD)
CHOLESTEROL OXIDASE extrapure
CHOLESTEROL OXIDASE MICROBIAL
Cholesterol oxidase USP/EP/BP
CholesterolOxidaseExNocardiaSp.
Cholesterol Oxidase, Nocardia sp.
CHOLESTEROL: OXYGEN OXIDOREDUCTASE
CHOLESTEROL OXIDASE, NOCARDIA SPECIES
Cholesterol Oxidase, Streptomyces sp.
cholesterol oxidase F. pseudomonas sp.
rCO, Cholesterol: oxygen oxidoreductase
Cholesterol Oxidase from microorganisms
Cholesterol Oxidase from Brevibacterium
Cholesterol Oxidase from Pseudomonas sp.
Native Microorganism Cholesterol Oxidase
cholesterol oxidase from cellulomonas sp.
cholesterol oxidase from streptomyces sp.
Cholesterol Oxidase Nocardia erythropolis
Cholesterol oxidase recombinant, solution
fromnocardiaerythropolislyophilizedpowder
CHOLESTEROL OXIDASE FROM BREVIBACTERIUM
Native Streptomyces sp. Cholesterol Oxidase
CHOLESTEROL: OXYGEN OXIDOREDUCTASE MICROBIAL
CHOLESTEROL OXIDASE FROMSTREPTOMYCES SPE CIES
CHOLESTEROL OXIDASE FROM CELLULOMONASSPE CIES
Cholesterol oxidase from E. coli, Recombinant
Cholesterol Oxidase from Brevibacterium sp.
CHOLESTEROL OXIDASE F. PSEUDOMONAS SP., ~5 U/MG
cholesterol oxidase from nocardia ery-thropolis
CHOLESTEROL OXIDASE FROM PSEUDOMONASFLUO RESCENS
Native Nocardia erythropolis Cholesterol Oxidase
Cholesterol oxidase from Nocardia sp., Recombinant
Cholesterol oxidase, recombinant from Nocardia sp.
Cholesterol oxidase, recombinant E.coli min. 300 U/ml
Cholesterol oxidase from E. coli, Recombinant (liquid)
Cholesterol oxidase, from E.coli, >=50 units/mg protein
CHOLESTEROL OXIDASE FROM NOCARDIA ERY-TH ROPOLIS, ~25 U/ML
Cholesterol Oxidase microbial,Cholesterol: oxygen oxidoreductase
Cholesterol Oxidase from Cellulomonas sp.,Cholesterol:oxygen oxidoreductase
Cholesterol Oxidase from Streptomyces sp.,Cholesterol: oxygen oxidoreductase
Cholesteroloxidase/cholesterol oxidase/recoMbinantcholesteroloxidase /REC-COD
Cholesterol Oxidase from Brevibacterium sp.,Cholesterol: oxygen oxidoreductase
Cholesterol Oxidase from Pseudomonas fluorescens,Cholesterol: oxygen oxidoreductase | [EINECS(EC#)]
232-842-1 | [Molecular Formula]
NULL | [MDL Number]
MFCD00130783 |
| Chemical Properties | Back Directory | [storage temp. ]
2-8°C
| [solubility ]
50 mM potassium phosphate buffer, pH 7.0: soluble (Cold) | [form ]
solution (slightly hazy)
| [color ]
pale yellow
| [Uses]
Cholesterol oxidases are part of a unique class of enzymes that are soluble proteins although they interact with highly insoluble substrates. The natural substrate, cholesterol, is an important membrane component exhibiting low solubility in the aqueous medium of the cell, hence the enzyme must interact with the lipid bilayer in order to for the substrate to partition out of the membrane and undergo oxidation at the enzyme active site. In this regard cholesterol oxidase is an interfacial enzyme as it binds transiently to the membrane surface during catalysis and can only access the substrate from the membrane phase. Other examples of interfacial enzymes include phospholipases (Berg et al., 2001; Gelb et al., 1995; Jain et al., 1995).
Cholesterol oxidase has a number of important commercial applications. Initial studies on the enzyme focused on its use for the determination of cholesterol in serum, HDL or LDL (see review, Smith and Brooks, 1976). Serum cholesterol levels are determined using a three-enzyme assay, including cholesterol esterase, cholesterol oxidase and peroxidase (Richmond, 1973; Allain et al., 1974; Richmond, 1976). More recently electrochemical biosensors with immobilized cholesterol oxidase have been employed to determine cholesterol levels in serum or food (Arya et al., 2007; Basu et al., 2007; Vidal et al., 2004). Determining the serum cholesterol levels is critical for the assessment of a variety of diseases including hypercholesterolemia, coronary heart disease and lipid disorders for estimating the risk of thrombosis and myocardial infarction. | [EPA Substance Registry System]
Oxidase, cholesterol (9028-76-6) |
| Hazard Information | Back Directory | [Chemical Properties]
Cholesterol oxidase is a bacterial-specific flavoenzyme that catalyzes the oxidation and isomerisation of steroids containing a 3β hydroxyl group and a double bond at the 5–6 of the steroid ring system. The enzyme is a member of a large family of flavin-specific oxidoreductases and is found in two different forms: one where the flavin adenine dinucleotide (FAD) cofactor is covalently linked to the protein and one where the cofactor is non-covalently bound to the protein.
Cholesterol oxidases are secreted bacterial enzymes that catalyze the first step in the degradation of cholesterol. They are flavoenzymes containing the redox cofactor, flavin adenine dinucleotide (FAD). The enzyme catalyzes three chemical conversions. In the first step, called the reductive half-reaction, the 3β-hydroxyl group of the steroid ring system is oxidized to the corresponding ketone. Key to this conversion is the FAD cofactor, which becomes reduced in the process. In the second step the enzyme catalyzes isomerization of the double bond in the oxidized steroid ring system from the 5–6 position to 4–5 position, to give the final steroid product, cholest-4-en-3-one. In the final step of the enzyme, called the oxidative half-reaction, the reduced cofactor reacts with dioxygen and is thus reoxidized while O2 is reduced to H2O2. | [General Description]
Cholesterol Oxidase produced from Streptomyces sp corresponds to a molecular weight of 62 kDa. It has a pH and temperature optimum of 7 and 37 °C, respectively. Cholesterol Oxidase comprises a FAD-binding and a steroid-binding domain. | [Biochem/physiol Actions]
Cholesterol oxidase (CHOD) is a monomeric flavoprotein containing FAD that catalyzes the first step in cholesterol catabolism. This bifunctional enzyme oxidizes cholesterol to cholest-5-en-3-one in an FAD-requiring step, which is then isomerized to cholest-4-en-3-one with the release of H2O2. |
|
|