HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 1.14.13.141 - cholest-4-en-3-one 26-monooxygenase [(25S)-3-oxocholest-4-en-26-oate forming]
Word Map on EC 1.14.13.141
- 1.14.13.141
- tuberculosis
- cholesterol
- sterol
- iron
- azole
- heme
-
low-spin
- bovis
-
methyl-branched
- 4-cholesten-3-one
-
antitubercular
- clotrimazole
-
27-hydroxylation
-
raman
-
thiolate
-
rhodococcus
- jostii
- econazole
-
uv-vis
-
anti-mycobacterial
-
high-spin
-
ligand-free
-
phthiocerol
-
dimycocerosates
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The enzyme appears in viruses and cellular organisms
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
1.14.13.141
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
cholest-4-en-3-one 26-monooxygenase [(25S)-3-oxocholest-4-en-26-oate forming]
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(25S)-26-hydroxycholest-4-en-3-one + NADH + H+ + O2 = (25S)-26-oxocholest-4-en-3-one + NAD+ + 2 H2O
(1b)
-
-
-
(25S)-26-oxocholest-4-en-3-one + NADH + H+ + O2 = (25S)-3-oxocholest-4-en-26-oate + NAD+ + H2O
(1c)
-
-
-
cholest-4-en-3-one + 3 NADH + 3 H+ + 3 O2 = (25S)-3-oxocholest-4-en-26-oate + 3 NAD+ + 4 H2O
overall reaction
-
-
-
cholest-4-en-3-one + NADH + H+ + O2 = (25S)-26-hydroxycholest-4-en-3-one + NAD+ + H2O
(1a)
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
cholest-4-en-3-one,NADH:oxygen oxidoreductase [(25S)-3-oxocholest-4-en-26-oate forming]
This enzyme, found in several bacterial pathogens, is involved in degradation of the host's cholesterol. It catalyses the hydroxylation of the C-26 carbon, followed by oxidation of the alcohol to the carboxylic acid via the aldehyde intermediate, initiating the degradation of the alkyl side-chain of cholesterol [4]. The products are exclusively in the (25S) configuration. It is a two-component system consisting of a P-450 (heme thiolate) oxygenase (Cyp125) and a ferredoxin reductase (most likely KshB, which is also a part of EC 1.14.13.142, 3-ketosteroid 9alpha-monooxygenase). The enzyme also accepts cholesterol as a substrate. cf. EC 1.14.13.221, cholest-4-en-3-one 27-monooxygenase.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
-
CYP125 performs an obligate first step in cholesterol degradation. CYP125 is involved in steroid C26-carboxylic acid formation, catalysing the oxidation of C26 either to the corresponding carboxylic acid or to an intermediate state
metabolism
CYP125A1 is a key enzyme in cholesterol metabolism and plays a crucial role in circumventing the deleterious effect of cholest-4-en-3-one
physiological function
-
Cyp125 is essential for the growth of Mycobacterium bovis strain bacillus Calmette-Guerin on cholesterol
physiological function
-
Cyp125 is not essential for the growth of Mycobacterium tuberculosis on cholesterol
physiological function
-
cyp125 is essential for Rhodococcus jostii strain RHA1 to grow on 3-hydroxysterols such as cholesterol, but not on 3-oxo sterol derivatives
physiological function
CYP125A1 is required to incorporate the cholesterol side chain carbon atoms into cellular lipids. CYP125A1 is essential for growth of CDC1551 in media containing cholesterol or cholest-4-en-3-one
physiological function
-
Cyp125 is essential for the growth of Mycobacterium bovis strain bacillus Calmette-Guerin on cholesterol
-
physiological function
-
Cyp125 is not essential for the growth of Mycobacterium tuberculosis on cholesterol
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
27-hydroxycholest-4-en-3-one + O2
cholest-4-en-3-one-27-oic acid + H2O
-
-
-
?
cholest-4-en-3-one + O2 + NADPH + H+
27-hydroxycholest-4-en-3-one + H2O + NADP+
physiological substrate, the enzyme hydroxylates cholest-4-en-3-one at C-27
-
-
?
cholesterol + O2 + NADPH + H+
27-hydroxycholesterol + H2O + NADP+
-
-
-
-
?
cholest-4-en-3-one + O2 + NADH + H+
(25S)-26-hydroxycholest-4-en-3-one + H2O + NAD+
-
-
CYP125A1 generates oxidized sterols of the (25S)-26-hydroxy configuration
-
?
cholest-4-en-3-one + O2 + NADH + H+
(25S)-26-hydroxycholest-4-en-3-one + H2O + NAD+
-
-
CYP125A1 generates oxidized sterols of the (25S)-26-hydroxy configuration
-
?
cholest-4-en-3-one + O2 + NADH + H+
(25S)-26-hydroxycholest-4-en-3-one + H2O + NAD+
-
-
CYP125A1 generates oxidized sterols of the (25S)-26-hydroxy configuration
-
?
cholest-4-en-3-one + O2 + NADH + H+
26-hydroxycholest-4-en-3-one + H2O + NAD+
-
hydroxylation occurs at carbon 26 of the steroid side chain
-
-
?
cholest-4-en-3-one + O2 + NADH + H+
26-hydroxycholest-4-en-3-one + H2O + NAD+
-
hydroxylation occurs at carbon 26 of the steroid side chain
-
-
?
cholest-4-en-3-one + O2 + NADH + H+
26-hydroxycholest-4-en-3-one + H2O + NAD+
-
-
-
?
cholest-4-en-3-one + O2 + NADH + H+
26-hydroxycholest-4-en-3-one + H2O + NAD+
-
hydroxylation occurs at carbon 26 of the steroid side chain
-
-
?
cholest-4-en-3-one + O2 + NADH + H+
26-hydroxycholest-4-en-3-one + H2O + NAD+
-
hydroxylation occurs at carbon 26 of the steroid side chain
-
-
?
cholest-4-en-3-one + O2 + NADH + H+
26-hydroxycholest-4-en-3-one + H2O + NAD+
-
-
-
?
cholesterol + O2 + NADH + H+
?
-
hydroxylation occurs at carbon 26 of the steroid side chain
-
-
?
cholesterol + O2 + NADH + H+
?
-
hydroxylation occurs at carbon 26 of the steroid side chain
-
-
?
cholesterol + O2 + NADH + H+
?
-
hydroxylation occurs at carbon 26 of the steroid side chain
-
-
?
cholesterol + O2 + NADH + H+
?
-
hydroxylation occurs at carbon 26 of the steroid side chain
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
27-hydroxycholest-4-en-3-one + O2
cholest-4-en-3-one-27-oic acid + H2O
P9WPP0
-
-
-
?
cholest-4-en-3-one + O2 + NADPH + H+
27-hydroxycholest-4-en-3-one + H2O + NADP+
P9WPP0
physiological substrate, the enzyme hydroxylates cholest-4-en-3-one at C-27
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alpha-[(4-methylcyclohexyl)carbonyl amino]-N-4-pyridinyl-1H-indole-3-propanamide
LP10, 30% inhibition at 0.2 mM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0208
cholest-4-en-3-one
-
pH and temperature not specified in the publication
0.0107
cholesterol
-
pH and temperature not specified in the publication
1.2
O2
-
apparent value, Km above 1.2 mM, in 0.1 M potassium phosphate at pH 7.0, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.92
cholest-4-en-3-one
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.47
cholesterol
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11000
O2
Mycobacterium tuberculosis
-
apparent value, in 0.1 M potassium phosphate at pH 7.0, temperature not specified in the publication
9
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
ORGANISM
UNIPROT
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme bound to cholest-4-en-3-one, hanging drop vapor diffusion method, using 0.2 M ammonium sulfate, 0.1 M bis-Tris, pH 5.5, and 25% (w/v) PEG 3350
hanging drop vapor diffusion method, using 2.0 M ammonium sulfate, 0.1 M bis-Tris (pH 5.5) and 0.5 M NaCl (truncated enzyme C429L in complex with inhibitor) or 0.1 M ammonium acetate, 0.1 M bis-Tris (pH 5.5) and 17% PEG 10000, or 2.0 M ammonium sulfate and 0.1 M Tris HCl pH 8.5 (truncated enzyme C429L without any ligand)
sitting drop vapor diffusion method, using MgCl2 with 0.1 M HEPES, pH 7.0 or 7.5, and 20% (w/v) PEG 6000 or 25% (w/v) PEG 3350, respectively
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65
65
-
the enzyme is heat inactivated by incubation at 65°C for 30 min
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA resin column chromatography, Resource-Q column chromatography, and Sephacryl S-200 gel filtration
-
Ni2+-affinity column chromatography and Q Sepharose column chromatography
-
Source 15Q column chromatography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Rhodococcus jostii strain RHA1
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cyp125 is up-regulated 7.1fold with growth on cholesterol
cyp125 is up-regulated 7.1fold with growth on cholesterol
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C429L
C429L
the modification affect neither the binding nor the catalytic properties of the enzyme
C429L
-
the modification affect neither the binding nor the catalytic properties of the enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.141)
html completed
Information
