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
-
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
- 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
Advanced search results
Cofactor
Cofactor on EC 1.1.3.6 - cholesterol oxidase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
FAD
combined quantum mechanical and molecular mechanical simulations of one- and two-electron reduction potentials of flavin cofactor
FAD
-
distortion of flavin geometry is linked to ligand binding in cholesterol oxidase
FAD
Streptoverticillum cholesterolicum
-
both as a covalently or noncovalently bound cofactor
FAD
-
the type II cholesterol oxidase fully active enzyme contains covalently bound FAD
FAD
dependent on, the enzyme contains a Rossmann fold (xh)2GxGxxGx(xxh)2(x) FAD binding site, where x is any amino acid and h an hydrophobic one, between V44 and E70 in the N-terminal region. CgChoA belongs to the non-covalent FAD-dependent enzymes belonging to the class I family. Residues N503 and Y464 are required for stabilization of the reduced form cofactor-enzyme binding
FAD
isozyme ChoM1 contains a typical consensus sequence (GXGXXGXXXAXXXXXXG) in the FAD-binding site, which is located near the N-terminal end at amino acids 11-27
FAD
isozyme ChoM2 contains a typical consensus sequence (GXGXXGXXXAXXXXXXG) in the FAD-binding site, which is located near the N-terminal end at amino acids 45-61
FAD
the structure of the dithionite-reduced enzyme reveals a sulfite molecule covalently bound to the FAD cofactor. The hydride transfer generates a tetrahedral geometry about the flavin N5 atom