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Information on EC 1.1.3.6 - cholesterol oxidase and Organism(s) Streptomyces sp. and UniProt Accession P12676
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1.1.3.6 cholesterol oxidaseIUBMB Comments
Contains FAD. Cholesterol oxidases are secreted bacterial bifunctional enzymes that catalyse the first two steps in the degradation of cholesterol. The enzyme catalyses the oxidation of the 3beta-hydroxyl group to a keto group, and the isomerization of the double bond in the oxidized steroid ring system from the Delta5 position to Delta6 position (cf. EC 5.3.3.1, steroid Delta-isomerase).
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Word Map
- 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
The taxonomic range for the selected organisms is: Streptomyces sp.
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
cholesterol oxidase, coase, chom2, chori, chorii, cholox, cho-u, chom1, cod-b, cholesterol oxidase ii, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3beta-hydroxy steroid oxidoreductase
-
-
-
-
3beta-hydroxysteroid:oxygen oxidoreductase
-
-
-
-
CHOD
-
-
-
-
cholesterol-O2 oxidoreductase
-
-
-
-
oxidase, cholesterol
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cholesterol + O2 = cholest-5-en-3-one + H2O2
bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid
cholesterol + O2 = cholest-5-en-3-one + H2O2
bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
cholesterol:oxygen oxidoreductase
Contains FAD. Cholesterol oxidases are secreted bacterial bifunctional enzymes that catalyse the first two steps in the degradation of cholesterol. The enzyme catalyses the oxidation of the 3beta-hydroxyl group to a keto group, and the isomerization of the double bond in the oxidized steroid ring system from the Delta5 position to Delta6 position (cf. EC 5.3.3.1, steroid Delta-isomerase).
CAS REGISTRY NUMBER
COMMENTARY
9028-76-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
beta-cholestanol + O2
?
75% activity compared to cholesterol
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
72% activity compared to cholesterol
-
-
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
37% activity compared to cholesterol
-
-
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
24% activity compared to cholesterol
-
-
?
ergosterol + O2
dehydroergosterol + H2O2
12% activity compared to cholesterol
-
-
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
99% activity compared to cholesterol
-
-
?
cholest-5-en-3beta-ol 7-one + O2
cholest-5-en-3,17-dione + H2O2
-
low activity with wild-type and mutant enzymes L119A, L119F, V145Q, P357N, Q286R and S379T
-
-
?
dehydroisoandrosterone + O2
androst-5-en-3,17-dione + H2O
-
low activity with wild-type and mutant enzymes L119A, L119F, V145Q, P357N, Q286R and S379T
-
-
?
estrone + O2
estra-1,5(10)-dien-3,17-dione + H2O2
-
low activity with wild-type enzyme, no activity with mutant enzymes L119A, L119F, V145Q, P357N, Q286R and S379T
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
100% activity
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
cholesterol oxidase is required for the biosynthesis of the antifungal polyene pimaricin, apparently acting as an antifungal sensor
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
-
subsequent isomerization to cholest-4-en-3-one
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
assay with phenazine sulfate and dichlorophenylindophenol as electron acceptors
-
-
?
additional information
?
-
-
the wild-type enzyme also shows cholesterol dehydrogenase activity with 0.001 U/mg
-
-
?
additional information
?
-
-
the enzyme catalyzes the oxidation of steroid substrates which have a hydroxyl group at the 3beta-position of the steroid ring system
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
beta-cholestanol + O2
?
75% activity compared to cholesterol
-
-
?
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
72% activity compared to cholesterol
-
-
?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
37% activity compared to cholesterol
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
100% activity
-
-
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
24% activity compared to cholesterol
-
-
?
ergosterol + O2
dehydroergosterol + H2O2
12% activity compared to cholesterol
-
-
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
99% activity compared to cholesterol
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
cholesterol oxidase is required for the biosynthesis of the antifungal polyene pimaricin, apparently acting as an antifungal sensor
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
no or poor effects at 5 mM by Ca2+, Zn2+, Mg2+, and Fe2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
fenpropimorph
-
morpholine derivative, 50 mg/l, 50% inhibition, instantenous inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0015
cholesterol
mutant enzyme G347N, determined by cholest-4-en-3-one detection
0.0027
cholesterol
mutant enzyme F359W, determined by cholest-4-en-3-one detection
0.0027
cholesterol
wild-type enzyme, determined by cholest-4-en-3-one detection
0.0027
cholesterol
apparent value, wild type enzyme, pH 7.0, temperature not specified in the publication
0.0046
cholesterol
apparent value, mutant enzyme N485L, pH 7.0, temperature not specified in the publication
0.0062
cholesterol
apparent value, mutant enzyme N485L, pH 5.1, temperature not specified in the publication
0.0063
cholesterol
apparent value, mutant enzyme N485D, pH 5.1, temperature not specified in the publication
0.0066
cholesterol
apparent value, mutant enzyme N485D, pH 7.0, temperature not specified in the publication
0.0067
cholesterol
apparent value, wild type enzyme, pH 5.1, temperature not specified in the publication
0.007
cholesterol
mutant enzyme N485D, determined by cholest-4-en-3-one detection
0.0962
cholesterol
-
enzyme from cultured immobilized cells, pH and temperature not specified in the publication
0.1013
cholesterol
-
enzyme from cultured free cells, pH and temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.035
cholesterol
apparent value, mutant enzyme N485L, pH 5.1, temperature not specified in the publication
0.044
cholesterol
apparent value, mutant enzyme N485L, pH 7.0, temperature not specified in the publication
0.073
cholesterol
mutant enzyme N485D, determined by cholest-4-en-3-one detection
0.073
cholesterol
apparent value, mutant enzyme N485D, pH 7.0, temperature not specified in the publication
0.86
cholesterol
mutant enzyme F359W, determined by cholest-4-en-3-one detection
1
cholesterol
mutant enzyme G347N, determined by cholest-4-en-3-one detection
1.4
cholesterol
apparent value, mutant enzyme N485D, pH 5.1, temperature not specified in the publication
42
cholesterol
wild-type enzyme, determined by cholest-4-en-3-one detection
46
cholesterol
apparent value, wild type enzyme, pH 5.1, temperature not specified in the publication
47
cholesterol
apparent value, wild type enzyme, pH 7.0, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
production of cholesterol oxidase under batch conditions through Ca-alginate immobilized cells of Streptomyces sp., optimization of immobilization method and production conditions, overview. The enzyme production with immobilized cells is higher in comparison to free cells under optimized conditions. Production medium inoculated with 2% v/v or 8.8 mg dry cell weight seed culture and incubated at 200 rpm and 30°C for 96 h gves maximum COD enzyme production after 96 h whereas the immobilized culture gives maximum production at 37°C and 300 rpm after 72 h of incubation. The immobilized cells can be used for three consecutive fermentation cycles for COD production in higher quantities as compared with free cells
additional information
-
effect of carbon and nitrogen sources on COD production, highest activity on lactose and sucrose and on yeast extract, respectively, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55000
55000
-
x * 55000, wild-type and mutant enzymes V145Q, V145E, S379A and S379V, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 55000, wild-type and mutant enzymes V145Q, V145E, S379A and S379V, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E361Q
H447Q mutant shows wild-type activity in isomerization, kcat for oxidation reaction is reduced 120fold, Km increases 2fold compared to wild-type, E361Q mutant has no isomerization activity, kcat is 30fold slower than for wild-type, Glu361 may therefore act as general base in oxidation reaction
F359W
kcat for the F359W mutant-catalyzed reaction decreases 13fold relative to that of the wild-type-catalyzed reaction. Transfer of hydride from the sterol to the flavin prosthetic group is no longer rate-limiting for the mutant enzyme. Kinetic cooperativity with respect to molecular oxygen is observed with the tunnel mutant, but not with the wild-type enzyme. 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. The size of the indole is proposed to limit conformational rearrangement of residue 359 that leads to tunnel opening in the wild-type enzyme
G347N
mutant can not be saturated with oxygen. Transfer of hydride from the sterol to the flavin prosthetic group is no longer rate-limiting for the mutant enzyme. Kinetic cooperativity with respect to molecular oxygen is observed with the tunnel mutant, but not with the wild-type enzyme
H447N
H447Q mutant shows wild-type activity in isomerization, kcat for oxidation reaction is reduced 120fold, Km increases 2fold compared to wild-type, E361Q mutant has no isomerization activity, kcat is 30fold slower than for wild-type, Glu361 may therefore act as general base in oxidation reaction
H447Q
H447Q mutant shows wild-type activity in isomerization, kcat for oxidation reaction is reduced 120fold, Km increases 2fold compared to wild-type, E361Q mutant has no isomerization activity, kcat is 30fold slower than for wild-type, Glu361 may therefore act as general base in oxidation reaction
N485D
N485L
the kcat of N485D is diminished about 1110times compared with that of wild type, while the apparent Km value is minimally affected
E361A
-
site-directed mutagenesis, the mutant shows no dehydrogenase activity
E361Q
-
turnover number for cholesterol is decreased 31.4fold compared to wild-type enzyme, 1.8fold increase in Km-value for cholesterol compared to wild-type enzyme
F359A
-
site-directed mutagenesis, the dehydrogenase/oxidase ratio is 12fold increased compared with the ratio for the wild-type enzyme
F444A
-
site-directed mutagenesis, the dehydrogenase/oxidase ratio is 4fold increased compared with the ratio for the wild-type enzyme
H447E
-
turnover number for cholesterol is decreased about 2600fold compared to wild-type enzyme
H447E/E361Q
-
turnover number for cholesterol is decreased about 31500fold compared to wild-type enzyme. Mutant enzyme is not able to isomerize cholest-5-en-3-one. Mutant enzyme is folded like native enzyme and still associates with model membranes
H447Q
-
turnover number for cholesterol is decreased 137.5fold compared to wild-type enzyme, Km-value for cholesterol is identical to wild-type value
H447Q/E361Q
-
turnover number for cholesterol is decreased 473fold compared to wild-type enzyme, 1.7fold increase in Km-value for cholesterol compared to wild-type enzyme. Mutant enzyme is not able to isomerize cholest-5-en-3-one
M122A
-
site-directed mutagenesis, the dehydrogenase/oxidase ratio is 26fold increased compared with the ratio for the wild-type enzyme
N485A
-
site-directed mutagenesis, the mutant shows no dehydrogenase activity
V124A
-
site-directed mutagenesis, the dehydrogenase/oxidase ratio is 30fold increased compared with the ratio for the wild-type enzyme
V191A
-
site-directed mutagenesis, the mutant enzymes shows a significant decrease in its oxidase activity, but shows increased dehydrogenase activity. The dehydrogenase/oxidase ratio of Val191Ala is more than 150%, which is a 408fold increase compared with the ratio for the wild-type enzyme, substrate inhibition with cholesterol
Y446A
-
site-directed mutagenesis, the dehydrogenase/oxidase ratio is 3fold increased compared with the ratio for the wild-type enzyme
additional information
-
site-directed mutagenesis on oxygen-binding residues, which are observed in the high-resolution crystal structure, in order to elucidate the amino acid residues responsible for the oxidase activity, overview. Engineering of the enzyme for electrochemical monitoring of cholesterol
N485D
mutant can not be saturated with oxygen. Transfer of hydride from the sterol to the flavin prosthetic group is no longer rate-limiting for the mutant enzyme. Kinetic cooperativity with respect to molecular oxygen is observed with the tunnel mutant, but not with the wild-type enzyme
N485D
the kcat of N485D is diminished about 650times compared with that of wild type, while the apparent Km value is minimally affected. For the N485D mutant, pH 5.1results in a 20fold increase in the rate of oxidation compared with that at pH 7.0
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
-
half-lives of S103T, V121A, R135H, V145E mutants and wild-type: 11.3, 12.2, 11.0, 24.1 and 7.8 min respectively, half-lives of S103T/V145A double mutants and S103T/V145A/V121A triple mutants: 32.4 and 52.2 min respectively
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the enzyme shows moderate stability towards all organic solvents except acetone, benzene and chloroform. The activity increases in presence of isopropanol and ethanol
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
butyl-Sepharose column chromatography and DEAE-cellulose column chromatography
native extracellular enzyme 14.3fold by ammonium sulfate fractionation and affinity chromatography
-
recombinant wild-type and mutant enzymes with with His-tags both at the N-terminus and at the C-terminus from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant enzymes with with His-tags both at the N-terminus and at the C-terminus in Escherichia coli strain BL21 (DE3)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
diagnostics
medicine
-
determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments
analysis
-
simple, reliable, fast and reproducible method to prepare cholesterol oxidase electrodes is described
analysis
-
the steady state amperometric measurements of free cholesterol are performed by an enzyme electrode which is developed through electrostatic immobilization of the cholesterol oxidase in poly(vinylferrocenium) perchlorate, PVF+ClO4-, film that is coated on a Pt electrode
analysis
-
the development of an enzyme-based sensor employing the enzyme ChOx has great potential as a simple and economical sensor system, engineering of the enzyme for electrochemical monitoring of cholesterol, overview
diagnostics
-
the enzyme is used for a kinetic cholesterol assay for determination of cholesterol content in human serum, overview, the enzyme from Streptomyces is more effective than the enzyme from Brevibacterium
diagnostics
-
determination of cholesterol, by rapid, cheap and reliable methods, is very important in clinical diagnosis because its level in blood is closely related to human health. A reproducible cholesterol biosensors is prepared based on the direct adsorption of ChOx onto gold substrates (ChOx-Au)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nishiya, Y.; Harada, N.; Teshima, S-i.; Yamahita, M.; Fuji, I.; Hirayama, N.; Murooka, Y.
Improvement of thermal stability of Streptomyces cholesterol oxidase by random mutagenesis and a structural interpretation
Protein Eng.
10
231-235
1997
Streptomyces sp.
Kimberley Yue, Q.; Kass, I.J.; Sampson, N.S.; Vrielink, A.
Crystal structure determination of cholesterol oxidase from Streptomyces and structural characterization of key active site mutants
Biochemistry
38
4277-4286
1999
Streptomyces sp. (P12676)
MacLachlan, J.; Wotherspoon, A.T.L.; Ansell, R.O.; Brooks, C.J.W.
Cholesterol oxidase: sources, physical properties and analytical applications
J. Steroid Biochem. Mol. Biol.
72
169-195
2000
Streptomyces lavendulae, Streptomyces violascens, Pimelobacter simplex, Brevibacterium sterolicum, Streptomyces sp., Comamonas testosteroni, Rhodococcus equi, Corynebacterium cholesterolicum, Mycobacterium sp., Nocardia erythropolis, Nocardia rhodochrous, Nocardia sp., Pseudomonas sp., Rhodococcus erythropolis, Rhodococcus sp., Schizophyllum commune, Streptomyces griseocarneus, Streptomyces hygroscopicus, Streptomyces lividans, Rhodococcus sp. GK1
Doukyu, N.; Aono, R.
Cloning, sequence analysis and expression of a gene encoding an organic solvent- and detergent-tolerant cholesterol oxidase of Burkholderia cepacia strain ST-200
Appl. Microbiol. Biotechnol.
57
146-152
2001
Brevibacterium sterolicum, Burkholderia cepacia, Streptomyces sp., Nocardia erythropolis, Pseudomonas sp., Burkholderia cepacia ST-200
Ghoshroy, K.B.; Zhu, W.; Sampson, N.S.
Investigation of membrane disruption in the reaction catalyzed by cholesterol oxidase
Biochemistry
36
6133-6140
1997
Streptomyces sp., Streptomyces sp. A19249
Yin, Y.; Liu, P.; Anderson, R.G.; Sampson, N.S.
Construction of a catalytically inactive cholesterol oxidase mutant: investigation of the interplay between active site-residues glutamate 361 and histidine 447
Arch. Biochem. Biophys.
402
235-242
2002
Streptomyces sp.
Lario, P.I.; Sampson, N.; Vrielink, A.
Sub-atomic resolution crystal structure of cholesterol oxidase: what atomic resolution crystallography reveals about enzyme mechanism and the role of the FAD cofactor in redox activity
J. Mol. Biol.
326
1635-1650
2003
Streptomyces sp. (P12676)
Toyama, M.; Yamashita, M.; Yoneda, M.; Zaborowski, A.; Nagato, M.; Ono, H.; Hirayama, N.; Murooka, Y.
Alteration of substrate specificity of cholesterol oxidase from Streptomyces sp. by site-directed mutagenesis
Protein Eng.
15
477-484
2002
Streptomyces sp.
Srisawasdi, P.; Jearanaikoon, P.; Wetprasit, N.; Sriwanthana, B.; Kroll, M.H.; Lolekha, P.H.
Application of Streptomyces and Brevibacterium cholesterol oxidase for total serum cholesterol assay by the enzymatic kinetic method
Clin. Chim. Acta
372
103-111
2006
Brevibacterium sp., Streptomyces sp.
Chen, L.; Lyubimov, A.Y.; Brammer, L.; Vrielink, A.; Sampson, N.S.
The binding and release of oxygen and hydrogen peroxide are directed by a hydrophobic tunnel in cholesterol oxidase
Biochemistry
47
5368-5377
2008
Streptomyces sp. (P12676)
Oezer, B.C.; Oezyoeruek, H.; Celebi, S.S.; Yildiz, A.
Amperometric enzyme electrode for free cholesterol determination prepared with cholesterol oxidase immobilized in poly(vinylferrocenium) film
Enzyme Microb. Technol.
40
262-265
2007
Streptomyces sp.
-
Bhattacharyya, S.; Stankovich, M.T.; Truhlar, D.G.; Gao, J.
Combined quantum mechanical and molecular mechanical simulations of one- and two-electron reduction potentials of flavin cofactor in water, medium-chain acyl-CoA dehydrogenase, and cholesterol oxidase
J. Phys. Chem. A
111
5729-5742
2007
Streptomyces sp. (P12676)
Aparicio, J.F.; Martin, J.F.
Microbial cholesterol oxidases: bioconversion enzymes or signal proteins?
Mol. Biosyst.
4
804-809
2008
Arthrobacter sp., Streptomyces sp., Rhodococcus equi, Rhodococcus erythropolis, Rhodococcus rhodochrous, Schizophyllum commune, Brevibacterium sterolicum (P22637)
Lyubimov, A.Y.; Heard, K.; Tang, H.; Sampson, N.S.; Vrielink, A.
Distortion of flavin geometry is linked to ligand binding in cholesterol oxidase
Protein Sci.
16
2647-2656
2007
Streptomyces sp.
Parra, A.; Casero, E.; Pariente, F.; Vazquez, L.; Lorenzo, E.
Cholesterol oxidase modified gold electrodes as bioanalytical devices
Sens. Actuators B Chem.
B124
30-37
2007
Streptomyces sp.
-
Lyubimov, A.Y.; Chen, L.; Sampson, N.S.; Vrielink, A.
A hydrogen-bonding network is important for oxidation and isomerization in the reaction catalyzed by cholesterol oxidase
Acta Crystallogr. Sect. D
65
1222-1231
2009
Streptomyces sp. (P12676)
Doukyu, N.
Characteristics and biotechnological applications of microbial cholesterol oxidases
Appl. Microbiol. Biotechnol.
83
825-837
2009
Arthrobacter sp., Arthrobacter sp. (Q56DL0), Arthrobacter sp. IM79, Brevibacterium sterolicum (P22637), Burkholderia cepacia (Q93RE1), Burkholderia cepacia ST-200 (Q93RE1), Burkholderia pseudomallei, Burkholderia thailandensis (Q2T0X3), Chromobacterium sp. (B5MGF8), Corynebacterium cholesterolicum, Corynebacterium urealyticum (B1VGH1), Corynebacterium urealyticum DSM 7109 (B1VGH1), Mycobacterium leprae (Q59530), Mycobacterium tuberculosis (P9WMV9), Mycobacterium tuberculosis H37Rv (P9WMV9), Nocardia farcinica (Q5YRJ2), Nocardia farcinica IFM 10152 (Q5YRJ2), Nocardia rhodochrous, Nocardia sp., Paraburkholderia xenovorans (Q13UN0), Pimelobacter simplex, Pseudomonas aeruginosa, Pseudomonas sp., Pseudomonas sp. COX629, Rhodococcus equi (A0A3S5YA89), Rhodococcus equi 103S (A0A3S5YA89), Rhodococcus erythropolis (A9QAE7), Schizophyllum commune, Streptomyces avermitilis (Q93H76), Streptomyces coelicolor (Q9L0H6), Streptomyces fradiae, Streptomyces griseus (A7RA76), Streptomyces natalensis (Q9EW96), Streptomyces sp. (P12676), Streptomyces sp. (Q55020), Streptomyces violascens, Streptoverticillium cholesterolieum, uncultured Gammaproteobacteria bacterium, uncultured Gammaproteobacteria bacterium Y-134
Kojima, K.; Kobayashi, T.; Tsugawa, W.; Ferri, S.; Sode, K.
Mutational analysis of the oxygen-binding site of cholesterol oxidase and its impact on dye-mediated dehydrogenase activity
J. Mol. Catal. B
88
41-46
2013
Streptomyces sp.
-
Niwas, R.; Singh, V.; Singh, R.; Tripathi, D.; Tripathi, C.K.
Production, purification and characterization of cholesterol oxidase from a newly isolated Streptomyces sp.
World J. Microbiol. Biotechnol.
29
2077-2085
2013
Streptomyces sp., Streptomyces sp. R-6
Niwas, R.; Singh, V.; Singh, R.; Pant, G.; Mitra, K.; Tripathi, C.K.
Cholesterol oxidase production from entrapped cells of Streptomyces sp.
J. Basic Microbiol.
54
1233-1239
2014
Streptomyces sp.
Parra, A.; Casero, E.; Pariente, F.; Vazquez, L.; Lorenzo, E.
Cholesterol oxidase modified gold electrodes as bioanalytical devices
Sens. Actuators B Chem.
B124
30-37
2007
Streptomyces sp.
-
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