1.1.3.6: cholesterol oxidase
This is an abbreviated version!
For detailed information about cholesterol oxidase, go to the full flat file.
Word Map on EC 1.1.3.6
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1.1.3.6
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biosensors
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electrode
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esterase
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electrochemical
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brevibacterium
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fabric
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oxidases
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amperometric
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film
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rhodococcus
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raft
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cholestenone
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voltammetry
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cholest-4-en-3-one
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flavoenzyme
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cholesteryl
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nanocomposite
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biosensing
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erythropolis
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filipin
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4-cholesten-3-one
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nocardia
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medicine
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3hcholesterol
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electropolymerization
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lavendulae
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biotechnology
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agriculture
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co-immobilized
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methyl-beta-cyclodextrin
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diagnostics
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bioelectrode
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luminol
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screen-printed
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electrocatalytic
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analysis
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3.1.1.13
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polypyrrole
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multiwalled
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beta-ol
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synthesis
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drug development
- 1.1.3.6
-
biosensors
-
electrode
- esterase
-
electrochemical
- brevibacterium
-
fabric
- oxidases
-
amperometric
-
film
- rhodococcus
-
raft
- cholestenone
-
voltammetry
- cholest-4-en-3-one
-
flavoenzyme
-
cholesteryl
-
nanocomposite
-
biosensing
- erythropolis
- filipin
- 4-cholesten-3-one
- nocardia
- medicine
-
3hcholesterol
-
electropolymerization
- lavendulae
- biotechnology
- agriculture
-
co-immobilized
- methyl-beta-cyclodextrin
- diagnostics
-
bioelectrode
- luminol
-
screen-printed
-
electrocatalytic
- analysis
-
3.1.1.13
-
polypyrrole
-
multiwalled
- beta-ol
- synthesis
- drug development
Reaction
Synonyms
3beta-hydroxy steroid oxidoreductase, 3beta-hydroxysteroid: oxygen oxidoreductase, 3beta-hydroxysteroid:oxygen oxidoreductase, 3beta-hydroxysterol oxidase, BsChOx, CgChoA, CHO, CHO-U, ChO3, ChoA, choBb, CHOD, ChoG, ChoL, cholesterol oxidase, cholesterol oxidase I, cholesterol oxidase II, cholesterol-O2 oxidoreductase, CHOLOX, choM, ChoM1, ChoM2, choP, ChoRI, ChoRII, ChoS, ChOx, CO, CO1, COase, COD, COD-B, COX, HCEO-forming enzyme, HMPREF0204_11499, oxidase, cholesterol, PimE, ShChOx, type I ChOx
ECTree
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Crystallization
Crystallization on EC 1.1.3.6 - cholesterol oxidase
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crystals of recombinant His-tagged enzyme, vapor diffusion by hanging drop, space group P21
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structure of substrate-enzyme complex, 1.8 A resolution, substrate binds in internal cavity which is totally sealed from solvent
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hanging-drop vapour-diffusion method using polyethylene glycol as a precipitating agent. The crystals belong to space group P3(1)21 with unit-cell parameters a = b = 119.6, c = 101.1 A, and has one subunit in the asymmetric unit
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crystal screen based on sparse matrix formulation, using 500 mM ammonium sulfate, 1.0 M lithium sulfate and 10 mM sodium citrate
crystals of the H447Q/E361Q mutant protein are grown by hanging-drop vapor diffusion method, high-resolution crystal structure of mutant enzyme H447Q/E361Q with glycerol and without glycerol
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mutant enzymes N485D and N485L, hanging drop vapor diffusion method, using 9-11% (w/v) polyethylene glycol 8000, 75 mM MnSO4 and 100 mM sodium cacodylate pH 5.2
structure of the F359W mutant enzyme, hanging drop vapor diffusion method. In the atomic-resolution structure of F359W, the indole ring of the tryptophan completely fills the tunnel and is observed in only a single conformation
Sub-atomic resolution crystal structure, crystallographic data: space group P2(1), a = 52.23 A, b * 72.9 A, c = 62.95 A, beta = 105.1
vapor diffusion by hanging drop method, 1.5 A resolution, wild-type, E361Q, H447N and H447Q mutant, structure consists of FAD-binding and a steroid-binding domain with a large active site cavity in between
purified nontagged and His6-tagged enzyme reduced with dithionite under aerobic conditions and in the presence of the substrate 2-propanol under both aerobic and anaerobic conditions, vapour diffusion using the hanging-drop method, mixing of 7 mg/ml protein in 50 mM HEPES pH 7.0 with reservoir solution containing 7% PEG 8000, 100 mM cacodylate, pH 5.2, 125 mM MnSO4, followed by microseeding in 12% PEG 8000, 100 mM sodium cacodylate, pH 5.2, 125 mM MnSO4, X-ray diffraction structure determination and analysis at 1.12-1.34 A resolution