C8649
Cholesterol Oxidase from Streptomyces sp.
lyophilized powder, ≥20 units/mg protein
Synonyme(s) :
Cholesterol: oxygen oxidoreductase
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About This Item
Source biologique
Streptomyces sp.
Forme
lyophilized powder
Activité spécifique
≥20 units/mg protein
Poids mol.
~34 kDa
Composition
protein, 55-65% biuret
Solubilité
50 mM potassium phosphate buffer, pH 7.0: soluble (Cold)
Conditions d'expédition
dry ice
Température de stockage
−20°C
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Description générale
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.
Application
Cholesterol oxidase from Streptomyces has been used in a study to assess the relationship between the micellar structure of model bile and the activity of esterase. Cholesterol oxidase from Streptomyces has also been used in a study to investigate the effects of sphingomyelin degradation on cell cholesterol oxidizability and steady-state distribution between the cell surface and the cell interior.
Cholesterol oxidase is used to determine serum cholesterol. The enzyme also finds application in the microanalysis of steroids in food samples and in distinguishing 3-ketosteroids from 3β-hydroxysteroids. Transgenic plants expressing cholesterol oxidase are being investigated in the fight against the cotton boll weevil. CHOD has also been used as a molecular probe to elucidate cellular membrane structures.
Actions biochimiques/physiologiques
Cholesterol Oxidase from microorganisms use cholesterol for carbon and energy. It is useful in diagnostic assays involving cholesterol, especially in lipid disorders. Cholesterol oxidase has an insecticidal property and aids protection against boll weevil larvae. The Streptomyces sp cholesterol oxidase has long shelf-life with good performance.
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.
Propriétés physiques
Isoelectric point : 5.1 ± 0.1 and 5.4 ± 0.1
Michaelis constant : 4.3 x 10‾5M(Cholesterol)
Inhibitors : Ionic detergents, Hg++, Ag+
Optimum pH : 6.5 − 7.0
Optimum temperature : 45 – 50°C
pH Stability : pH 5.0 – 10.0 (25°C, 20hr)
Thermal stability : Below 45°C (pH 7.0, 15min)
Michaelis constant : 4.3 x 10‾5M(Cholesterol)
Inhibitors : Ionic detergents, Hg++, Ag+
Optimum pH : 6.5 − 7.0
Optimum temperature : 45 – 50°C
pH Stability : pH 5.0 – 10.0 (25°C, 20hr)
Thermal stability : Below 45°C (pH 7.0, 15min)
Définition de l'unité
One unit will convert 1.0 μmole of cholesterol to 4-cholesten-3-one per min at pH 7.5 at 25 °C. Note: 4-cholesten-3-one may undergo isomerization.
Forme physique
lyophilized powder containing bovine serum albumin and amino acids as stabilizers
Notes préparatoires
CHOD is soluble in cold 50 mM potassium phosphate buffer, pH 7.0. Prepare solutions immediately before use.
Mention d'avertissement
Danger
Mentions de danger
Conseils de prudence
Classification des risques
Resp. Sens. 1
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
Certificats d'analyse (COA)
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Les clients ont également consulté
J P Slotte et al.
Biochimica et biophysica acta, 985(1), 90-96 (1989-10-02)
This study addresses questions related to (i) the distribution of cholesterol between the cell surface and intracellular membranes in cultured fibroblasts and (ii) the effects of plasma membrane sphingomyelin on this distribution. Cholesterol oxidase (Streptomyces sp.) converts cell cholesterol to
Crystal structure determination of cholesterol oxidase from Streptomyces and structural characterization of key active site mutants
Yue QK, et al.
Biochemistry, 38(14), 4277-4286 (1999)
Extracellular cholesterol oxidase production by Streptomyces aegyptia, in vitro anticancer activities against rhabdomyosarcoma, breast cancer cell-lines and in vivo apoptosis
NEA El-Naggar, et al.
Scientific reports, 8(1), 2706-2706 (2018)
Laura Caldinelli et al.
The Journal of biological chemistry, 280(24), 22572-22581 (2005-04-09)
Cholesterol oxidase from Brevibacterium sterolicum is a monomeric flavoenzyme catalyzing the oxidation and isomerization of cholesterol to cholest-4-en-3-one. This protein is a class II cholesterol oxidases, with the FAD cofactor covalently linked to the enzyme through the His(69) residue. In
Effect of cholesterol concentration on organization of viral and vesicle membranes. Probed by accessibility to cholesterol oxidase.
R Pal et al.
The Journal of biological chemistry, 255(12), 5802-5806 (1980-06-25)
Protocoles
Assay Procedure for Cholesterol Oxidase
Enzymatic Assay of Cholesterol Oxidase
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