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
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biosensors
-
electrode
- esterase
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electrochemical
- brevibacterium
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fabric
- oxidases
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amperometric
-
film
- rhodococcus
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raft
- cholestenone
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voltammetry
- 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
- erythropolis
- filipin
- 4-cholesten-3-one
- nocardia
- medicine
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3hcholesterol
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electropolymerization
- lavendulae
- biotechnology
- agriculture
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co-immobilized
- methyl-beta-cyclodextrin
- diagnostics
-
bioelectrode
- luminol
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screen-printed
-
electrocatalytic
- analysis
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3.1.1.13
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polypyrrole
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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
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results (General Information
General Information on EC 1.1.3.6 - cholesterol oxidase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
drug target
cholesterol oxidase can alter the structure of the cell membrane in pathogenic bacteria and is thus a potential antimicrobial drug target
evolution
malfunction
metabolism
physiological function
additional information
evolution
CgChoA belongs to the non-covalent FAD-dependent enzymes belonging to the class I family
evolution
the type I CO from Streptomyces sp. SA-COO is a member of the glucosemethanolcholine (GMC) oxidoreductase family and contains a single molecule of flavin adenine dinucleotide (FAD) noncovalently but tightly bound to the protein
evolution
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CgChoA belongs to the non-covalent FAD-dependent enzymes belonging to the class I family
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malfunction
the disruption of the choG gene does not alter the ability of strain CECT3014 cells to grow on cholesterol, but it abolishes the production of extracellular cholesterol oxidase
malfunction
the deletion mutant of choM1 completely lose the ability to form colonies on the cholesterol agar, the catabolism of sterols is greatly blocked, phenotype, overview
malfunction
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intracellular replication of an Mycobacterium tuberculosis mutant lacking a functional choD gene (DELTAchoD) is less efficient in macrophages than that of the wild-type strain. In contrast to wild-type tb, the DELTA strain inducesnitric oxide production in macrophages, an action that depends on the TLR2, but not the CR3, signaling pathway. Both wild-type and mutant strains inhibit the production of reactive oxygen species, but the DELTAchoD strain does so to a significantly lesser extent. Blocking TLR2-mediated signaling abolishes the inhibitory effect of wild-type Mycobacterium tuberculosis on reactive oxygen species production by macrophages. The mutant DELTAchoD strain, does not decrease phorbol myristate acetate-induced phosphorylation of extracellular signal-regulated kinases 1 and 2 (ERK1/2) ib contrast to the wild-type. The production of interleukin 10 by macrophages is significantly lower in DELTAchoD-infected macrophages than in wild-type Mtb-infected macrophages
malfunction
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the disruption of the choG gene does not alter the ability of strain CECT3014 cells to grow on cholesterol, but it abolishes the production of extracellular cholesterol oxidase
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metabolism
PimE is a key enzyme in the biosynthesis of the polyene macrolide pimaricin
metabolism
cholesterol oxidase ChoM1 is involved in the oxidation of sterols to sterones, a rate-limiting step in the catabolic pathway of sterols in Mycobacterium neoaurum. The bacterium exhibits definite preference for steroidal substrates possessing the 3-keto-4-ene moiety rather than the 3beta-ol-5-ene moiety
metabolism
cholesterol oxidase ChoM2 is involved in the oxidation of sterols to sterones, a rate-limiting step in the catabolic pathway of sterols in Mycobacterium neoaurum
metabolism
the enzyme catalyzes the first step in the biodegradation of cholesterol
metabolism
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the enzyme that is involved but is dispensable in the process of cholesterol degradation by Mycobacterium tuberculosis
physiological function
ChoD plays a significant role in the pathogenesis of Mycobacterium tuberculosis
physiological function
the conversion of sterols from 3beta-ol-5-ene moiety to 3-keto-4-ene moiety, i.e. the transformation of sterols to sterones, is a rate-limiting step in the catabolic pathway of sterols in Mycobacterium neoaurum. The conversion of 3beta-ol-5-ene moiety to 3-keto-4-ene moiety of sterols is indispensible for the catabolism of sterols in strain ATCC25795
physiological function
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cholesterol oxidase ChoD is capable of modifying the bactericidal and pro-inflammatory activity of human macrophages. and is indispensable in the pathogenesis of Mycobacterium tuberculosis. The enzyme is enzyme capable of converting cholesterol to its 3-keto-4-ene derivative, cholestenone. The wild-type strain inhibits the production of reactive oxygen species. Wild-type Mycobacterium tuberculosis, but not the DELTAchoD strain, decreases phorbol myristate acetate-induced phosphorylation of extracellular signal-regulated kinases 1 and 2 (ERK1/2), which are involved in both TLR2-and CR3-mediated signaling pathways
physiological function
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cholesterol oxidase from Bordetella species promotes irreversible cell apoptosis in lung adenocarcinoma by cholesterol oxidation in vitro and in vivo. COD-B treatment results in JNK and p38 phosphorylation, downregulation of Bcl-2, upregulation of Bax, activated caspase-3 and cytochrome C release, which likely responds to freshly produced hydrogen peroxide that accompanies cholesterol oxidation. COD-B leads to irreversible cell apoptosis by decreasing cholesterol content and increasing reactive oxygen species level. Cholesterol oxidase (COD) is a flavoprotein that catalyzes the oxidation of cholesterol to 4-cholesten-3-one with the reduction of oxygen to hydrogen peroxide. COD can convert membrane cholesterol to 4-cholesten-3-one and can inhibit the formation of lipid rafts. Different from other cholesterol-depleting agents, COD disrupts lipid rafts by displacing cholesterol with 4-cholesten-3-one. COD-B catalyzes the oxidation of membrane cholesterol in lung adenocarcinoma cell. When cells are pretreated with catalase before adding COD-B and cholesterol, the phosphorylation of Akt and ERK1/2 remaines attenuated compared with the group without catalase treatment. Catalase pretreatment also partially blocks the activation of caspase-3, effect of catalase on the COD-B-induced signaling response, overview. COD-B induces the reversible translocation of caveolin-1, which is involved in trafficking membrane cholesterol, in a cholesterol-reversable manner
physiological function
cholesterol oxidase (ChoD) is a virulence factor that enables Mycobacterium tuberculosis to disturb the TLR2-related signalling pathway in macrophages and modulate their response
physiological function
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the enzyme (ChoD) is a virulence factor of Mycobacterium tuberculosis, and it strongly modulates the function of human macrophages in vitro, allowing the intracellular survival of bacteria. It is an active protein, which is able to induce the immune response both in vivo and in vitro
physiological function
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ChoD plays a significant role in the pathogenesis of Mycobacterium tuberculosis
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physiological function
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cholesterol oxidase (ChoD) is a virulence factor that enables Mycobacterium tuberculosis to disturb the TLR2-related signalling pathway in macrophages and modulate their response
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additional information
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a extracellular halo tolerant, detergent and organic solvent stable alkaline cholesterol oxidase. The enzyme is stable in presence of chemical reagents (NaN3, EDTA), detergents (Tween-80, Tween-20, Triton X-100, sodium cholate) and various organic solvents (isopropanol, ethanol, benzene, chloroform, methanol, toluene, ethyl acetate, butanol and dimethylsulfoxide)
additional information
key amino acid residues involved in substrate oxidation are His470 and Asn513 in ChoM1
additional information
key amino acid residues involved in substrate oxidation are His470 and Asn513 in ChoM1
additional information
key amino acid residues involved in substrate oxidation are His479 and Asn517 in ChoM1
additional information
key amino acid residues involved in substrate oxidation are His479 and Asn517 in ChoM1
additional information
the structure of the dithionite-reduced enzyme reveals a sulfite molecule covalently bound to the FAD cofactor. The isoalloxazine ring system displays a bent structure relative to that of the oxidized enzyme, and alternate conformations of a triad of aromatic residues near to the cofactor are evident. The strutcure of anaerobically trapped reduced enzyme structure in the presence of 2-propanol does not show a similar bending of the flavin ring system, but does show alternate conformations of the aromatic triad. The hydride transfer generates a tetrahedral geometry about the flavin N5 atom
additional information
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a extracellular halo tolerant, detergent and organic solvent stable alkaline cholesterol oxidase. The enzyme is stable in presence of chemical reagents (NaN3, EDTA), detergents (Tween-80, Tween-20, Triton X-100, sodium cholate) and various organic solvents (isopropanol, ethanol, benzene, chloroform, methanol, toluene, ethyl acetate, butanol and dimethylsulfoxide)
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additional information
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key amino acid residues involved in substrate oxidation are His470 and Asn513 in ChoM1
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additional information
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key amino acid residues involved in substrate oxidation are His479 and Asn517 in ChoM1
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