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Information on EC 1.1.3.6 - cholesterol oxidase

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EC Tree
     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.3 With oxygen as acceptor
                1.1.3.6 cholesterol oxidase
IUBMB 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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This record set is specific for:
UNIPROT: Q157H4
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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
cholesterol oxidase, coase, chom2, chori, chorii, cholox, chom1, cho-u, cod-b, cholesterol oxidase ii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3beta-hydroxy steroid oxidoreductase
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3beta-hydroxysteroid:oxygen oxidoreductase
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CHOD
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cholesterol-O2 oxidoreductase
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oxidase, cholesterol
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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reduction
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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 hide
9028-76-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
beta-sitosterol + O2
stigmast-5-en-3-one + H2O2
show the reaction diagram
64% activity compared to cholesterol
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?
beta-stigmasterol + O2
stigmasta-5,22-dien-3-one + H2O2
show the reaction diagram
33% activity compared to cholesterol
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?
cholesterol + O2
cholest-4-en-3-one + H2O2
show the reaction diagram
100% activity
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?
additional information
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no activity with cholic acid, progesterone and 4-androsten-3,17-dione
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.032
cholesterol
pH 7.0, 50°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8
relative high activities in a broad pH range of 6.0-8.0, however activity rapidly declines under pH 5.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
pI-value about 9.0, isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q157H4_9NOCA
551
0
59091
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45 - 55
after 1 h of incubation, more than 70 and 50% of activity remains at 45 and 55°C, respectively
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to purify the recombinant enzyme, 500 mg cholesterol is added to 50 ml of crude extract, and then incubated for 2 h at 4°C followed by centrifugation at 10000g for 10 min
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)pLysS cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ghasemian, A.; Yazdi, M.; Sepehrizadeh, Z.; Yazdi, Z.; Zarrini, G.
Overexpression, one-step purification, and characterization of a type II cholesterol oxidase from a local isolate Rhodococcus sp. PTCC 1633
World J. Microbiol. Biotechnol.
25
773-779
2009
Rhodococcus sp. (Q157H4), Rhodococcus sp. PTCC 1633 (Q157H4)
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Manually annotated by BRENDA team