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The taxonomic range for the selected organisms is: Streptomyces sp.
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
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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
cholesterol + O2
cholest-5-en-3-one + H2O2
-
-
?
dehydroepiandrosterone + O2
androst-5-en-3,17-dione + H2O2
24% activity compared to cholesterol
-
-
?
dehydroisoandrosterone + O2
androst-5-en-3,17-dione + H2O
-
-
-
?
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
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
cholesterol + O2
cholest-5-en-3-one + H2O2
dehydroisoandrosterone + O2
androst-5-en-3,17-dione + H2O
-
low activity with wild-type and mutant enzymes L119A, L119F, V145Q, P357N, Q286R and S379T
-
-
?
dihydrocholesterol + O2
5alpha-cholestan-3-one + H2O2
-
-
-
-
?
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
-
-
?
pregnenolone + O2
5-pregnen-3,20-dione + H2O2
-
-
-
-
?
additional information
?
-
cholesterol + O2
cholest-4-en-3-one + H2O2
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
-
-
?
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 + O2
cholest-4-en-3-one + H2O2
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
-
-
?
cholesterol + O2
cholest-4-en-3-one + H2O2
-
-
-
-
?
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
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
-
-
?
cholesterol + O2
cholest-5-en-3-one + H2O2
-
-
-
-
?
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
-
-
?
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0.0015 - 0.007
cholesterol
0.0275
dehydroepiandrosterone
-
0.0000081 - 0.12
cholesterol
0.0000058 - 0.0001
pregnenolone
additional information
additional information
-
kinetics, modelling
-
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
wild-type enzyme, determined by H2O2 detection
0.0027
cholesterol
apparent value, wild type enzyme, pH 7.0, temperature not specified in the publication
0.004
cholesterol
mutant enzyme F359W, determined by H2O2 detection
0.0046
cholesterol
apparent value, mutant enzyme N485L, pH 7.0, temperature not specified in the publication
0.005
cholesterol
mutant enzyme G347N, determined by H2O2 detection
0.0062
cholesterol
mutant enzyme N485D, determined by H2O2 detection
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
0.3
O2
wild-type enzyme
0.617
O2
mutant enzyme F359W
0.0000081
cholesterol
-
pH 7.0, 37°C, mutant enzyme S379T
0.00002
cholesterol
-
pH 7.0, 37°C, wild-type enzyme
0.00003
cholesterol
-
pH 7.0, 37°C, mutant enzyme S379A
0.000046
cholesterol
-
pH 7.0, 37°C, mutant enzyme S379V
0.000072
cholesterol
-
pH 7.0, 37°C, mutant enzyme V145Q
0.000081
cholesterol
-
pH 7.0, 37°C, mutant enzyme L119A
0.00011
cholesterol
-
pH 7.0, 37°C, mutant enzyme P357N
0.00013
cholesterol
-
pH 7.0, 37°C, mutant enzyme Q286R
0.00017
cholesterol
-
pH 7.0, 37°C, mutant enzyme L119F
0.0004
cholesterol
-
pH 7.0, 37°C, mutant enzyme V145D
0.00067
cholesterol
-
pH 7.0, 37°C, mutant enzyme V145E
0.00245
cholesterol
-
recombinant mutant V191A, pH 7.0, 22°C
0.003
cholesterol
-
wild-type enzyme
0.003
cholesterol
-
mutant enzyme H447Q
0.005
cholesterol
-
mutant enzyme H447Q/E361Q
0.0054
cholesterol
-
mutant enzyme E361
0.011
cholesterol
-
V145E mutant
0.013
cholesterol
-
wild-type
0.013
cholesterol
-
S103T mutant
0.03
cholesterol
-
R135H mutant
0.0962
cholesterol
-
enzyme from cultured immobilized cells, pH and temperature not specified in the publication
0.1013
cholesterol
-
pH 7.0, 37°C
0.1013
cholesterol
-
enzyme from cultured free cells, pH and temperature not specified in the publication
0.12
cholesterol
-
recombinant wild-type enzyme, pH 7.0, 22°C
0.0000058
pregnenolone
-
pH 7.0, 37°C, mutant enzyme S379T
0.000023
pregnenolone
-
pH 7.0, 37°C, wild-type enzyme
0.000023
pregnenolone
-
pH 7.0, 37°C, mutant enzyme S379A
0.00004
pregnenolone
-
pH 7.0, 37°C, mutant enzyme L119A
0.00004
pregnenolone
-
pH 7.0, 37°C, mutant enzyme S379V
0.000056
pregnenolone
-
pH 7.0, 37°C, mutant enzyme Q286R
0.000058
pregnenolone
-
pH 7.0, 37°C, mutant enzyme V145Q
0.000077
pregnenolone
-
pH 7.0, 37°C, mutant enzyme L119F
0.000083
pregnenolone
-
pH 7.0, 37°C, mutant enzyme V145E
0.000098
pregnenolone
-
pH 7.0, 37°C, mutant enzyme P357N
0.0001
pregnenolone
-
pH 7.0, 37°C, mutant enzyme V145D
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0.69
dehydroepiandrosterone
-
0.035
cholesterol
mutant enzyme N485D, determined by H2O2 detection
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
0.85
cholesterol
mutant enzyme G347N, determined by H2O2 detection
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
1.3
cholesterol
mutant enzyme F359W, determined by H2O2 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
wild-type enzyme, determined by H2O2 detection
47
cholesterol
apparent value, wild type enzyme, pH 7.0, temperature not specified in the publication
0.0014
cholesterol
-
mutant enzyme H447E/E361Q
0.017
cholesterol
-
mutant enzyme H447E
0.093
cholesterol
-
mutant enzyme H447Q/E361Q
0.32
cholesterol
-
mutant enzyme H447Q
1.4
cholesterol
-
mutant enzyme E361
2.21
cholesterol
-
recombinant mutant V191A, pH 7.0, 22°C
9
cholesterol
-
pH 7.0, 37°C, mutant enzyme P357N
11
cholesterol
-
pH 7.0, 37°C, mutant enzyme V145D
11
cholesterol
-
pH 7.0, 37°C, mutant enzyme V145Q
15
cholesterol
-
pH 7.0, 37°C, mutant enzyme L119A
23
cholesterol
-
pH 7.0, 37°C, mutant enzyme Q286R
23
cholesterol
-
pH 7.0, 37°C, mutant enzyme V145E
27
cholesterol
-
pH 7.0, 37°C, mutant enzyme L119F
29
cholesterol
-
pH 7.0, 37°C, mutant enzyme S379T
40
cholesterol
-
pH 7.0, 37°C, wild-type enzyme
44
cholesterol
-
wild-type enzyme
47.3
cholesterol
-
recombinant wild-type enzyme, pH 7.0, 22°C
49
cholesterol
-
pH 7.0, 37°C, mutant enzyme S379A
51
cholesterol
-
pH 7.0, 37°C, mutant enzyme S379V
9
pregnenolone
-
pH 7.0, 37°C, mutant enzyme P357N
9
pregnenolone
-
pH 7.0, 37°C, mutant enzyme V145D
11
pregnenolone
-
pH 7.0, 37°C, mutant enzyme V145E
12
pregnenolone
-
pH 7.0, 37°C, mutant enzyme V145Q
13
pregnenolone
-
pH 7.0, 37°C, mutant enzyme L119A
19
pregnenolone
-
pH 7.0, 37°C, mutant enzyme Q286R
21
pregnenolone
-
pH 7.0, 37°C, mutant enzyme L119F
30
pregnenolone
-
pH 7.0, 37°C, wild-type enzyme
35
pregnenolone
-
pH 7.0, 37°C, mutant enzyme S379A
39
pregnenolone
-
pH 7.0, 37°C, mutant enzyme S379V
45
pregnenolone
-
pH 7.0, 37°C, mutant enzyme S379T
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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
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
L117P
-
mutant enzyme without activity
L119A
-
specific activity is similar to that of the wild-type enzyme
L119F
-
specific activity is similar to that of the wild-type enzyme
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
P357N
-
specific activity is similar to that of the wild-type enzyme
Q286R
-
specific activity is similar to that of the wild-type enzyme
R135H
-
random mutagenesis
S103T
-
random mutagenesis
S279R
-
mutant enzyme without activity on cholesterol and pregnenolone
S379D
-
mutant enzyme without activity on cholesterol and pregnenolone
S379T
-
specific activity is similar to that of the wild-type enzyme
V121A
-
random mutagenesis
V124A
-
site-directed mutagenesis, the dehydrogenase/oxidase ratio is 30fold increased compared with the ratio for the wild-type enzyme
V145E
-
random mutagenesis
V145Q
-
specific activity is similar to that of 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
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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.
brenda
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)
brenda
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
brenda
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
brenda
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
brenda
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.
brenda
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)
brenda
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.
brenda
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.
brenda
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)
brenda
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.
-
brenda
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)
brenda
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)
brenda
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.
brenda
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.
-
brenda
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)
brenda
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
brenda
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.
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brenda
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
brenda
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.
brenda
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.
-
brenda