C8649
Cholesterol Oxidase from Streptomyces sp.
lyophilized powder, ≥20 units/mg protein
Synonyme(s) :
Cholesterol: oxygen oxidoreductase
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A propos de cet article
Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-842-1
MDL number:
Specific activity:
≥20 units/mg protein
Biological source:
Streptomyces sp.
Service technique
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Streptomyces sp.
Quality Level
form
lyophilized powder
specific activity
≥20 units/mg protein
mol wt
~34 kDa
composition
protein, 55-65% biuret
solubility
50 mM potassium phosphate buffer, pH 7.0: soluble (Cold)
shipped in
dry ice
storage temp.
−20°C
General description
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)
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.
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.
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.
Physical form
lyophilized powder containing bovine serum albumin and amino acids as stabilizers
Preparation Note
CHOD is soluble in cold 50 mM potassium phosphate buffer, pH 7.0. Prepare solutions immediately before use.
Other Notes
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.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Classe de stockage
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Contenu apparenté
QC Methods
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)
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)