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Information on EC 1.3.1.72 - DELTA24-sterol reductase and Organism(s) Rattus norvegicus and UniProt Accession Q5BQE6
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1.3.1.72 DELTA24-sterol reductaseIUBMB Comments
Acts on a range of steroids with a 24(25)-double bond, including lanosterol, desmosterol and zymosterol.
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Word Map
- 1.3.1.72
- alzheimer
-
24-dehydrocholesterol
-
indicator-1
-
desmosterolosis
- ebp
-
smith-lemli-opitz
- triparanol
-
post-squalene
- medicine
- agriculture
- pharmacology
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
dhcr24, seladin-1, dwarf1, 24-dehydrocholesterol reductase, 24-reductase, dehydrocholesterol reductase, diminuto/dwarf1, delta24-reductase, zmdwf1, sterol c-24 reductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
24,25-reductase
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-
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24,25-sterol reductase
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24-reductase
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C-24 reductase
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DELTA24 reductase
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DELTA24-reductase
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desmosterol reductase
hydroxy steroid DELTA24-reductase
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lanosterol 24-reductase
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lanosterol DELTA24-reductase
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lanosterol reductase
reductase, hydroxy steroid DELTA24-
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sterol 24,25-reductase
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sterol 24-reductase
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sterol DELTA24 reductase
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sterol DELTA24-reductase
sterol-DELTA24-reductase
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desmosterol reductase
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lanosterol reductase
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sterol DELTA24-reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5alpha-cholest-7-en-3beta-ol + NADP+ = 5alpha-cholesta-7,24-dien-3beta-ol + NADPH + H+
anaerobic reduction of 24(25)-enes of lanosterol and other obligatory intermediates of cholesterol biosynthesis from lanosterol
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5alpha-cholest-7-en-3beta-ol + NADP+ = 5alpha-cholesta-7,24-dien-3beta-ol + NADPH + H+
regulation, enzyme induction, dietary induction
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
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-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
sterol:NADP+ DELTA24-oxidoreductase
Acts on a range of steroids with a 24(25)-double bond, including lanosterol, desmosterol and zymosterol.
CAS REGISTRY NUMBER
COMMENTARY
9033-57-2
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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
4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + NADPH
4,4-dimethyl-5alpha-cholesta-8-en-3beta-ol + NADP+
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-
-
-
?
cholesta-5,7,24-trien-3beta-ol + NADPH + H+
cholesta-5,7-dien-3beta-ol + NADP+
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-
-
-
?
5alpha-cholesta-7,24-dien-3beta-ol + NADPH
5alpha-cholest-7-en-3beta-ol + NADP+
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i.e. lathosterol
-
?
5alpha-cholesta-7,24-dien-3beta-ol + NADPH
5alpha-cholest-7-en-3beta-ol + NADP+
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best substrate
i.e.lathosterol
-
?
5alpha-cholesta-7,24-dien-3beta-ol + NADPH
5alpha-cholest-7-en-3beta-ol + NADP+
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step in the biosynthesis of cholesterol from lanosterol
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-
?
5alpha-cholesta-7,24-dien-3beta-ol + NADPH
5alpha-cholesta-7-en-3beta-ol + NADP+
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most reactive, best substrate, 17.8fold activity compared with lanosterol, 4,4',14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
lathosterol
?
5alpha-cholesta-7,24-dien-3beta-ol + NADPH
5alpha-cholesta-7-en-3beta-ol + NADP+
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C-24 reduction of sterols probably takes place straight after sterol DELTA8-7 isomerization of zymosterol, which occurs several steps after C-32 demethylation of lanosterol in the 19-step pathway of cholesterol biosynthesis from lanosterol
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-
?
5alpha-cholesta-7,24-dien-3beta-ol + NADPH
5alpha-cholesta-7-en-3beta-ol + NADP+
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C-24 reduction of DELTA7,24-diene
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-
?
5alpha-cholesta-7,24-dien-3beta-ol + NADPH
5alpha-cholesta-7-en-3beta-ol + NADP+
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most reactive, probably natural substrate
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-
?
cholesta-5,7,24-trien-3beta-ol + NADPH
cholest-5,7-dien-3beta-ol + NADP+
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-
-
-
?
cholesta-5,7,24-trien-3beta-ol + NADPH
cholest-5,7-dien-3beta-ol + NADP+
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step in the biosynthesis of cholesterol from lanosterol
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-
?
desmosterol + NADPH
cholesterol + NADP+
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5.5fold activity compared with lanosterol, 4,4',14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
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-
?
desmosterol + NADPH
cholesterol + NADP+
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5alpha-cholesta-5,24-dien-3beta-ol
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-
?
desmosterol + NADPH
cholesterol + NADP+
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step in the biosynthesis of cholesterol from lanosterol
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-
?
lanosterol + NADPH
24-dihydrolanosterol + NADP+
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step in the biosynthesis of cholesterol from lanosterol
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-
?
lanosterol + NADPH
4,4,14alpha-trimethyl-5alpha-cholesta-8-en-3beta-ol + NADP+
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14alpha-methyl demethylase activity is dominant over 24-reductase activity, and blockade or removal of 14alpha-methyl demethylase activity is absolutely required for the detection of maximal 24-reductase activity when lanosterol substrate is present
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-
?
lanosterol + NADPH
4,4,14alpha-trimethyl-5alpha-cholesta-8-en-3beta-ol + NADP+
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4,4',14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
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-
?
zymosterol + NADPH
5alpha-cholesta-8-en-3beta-ol + NADP+
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6.1fold activity compared with lanosterol, 4,4',14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
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-
?
zymosterol + NADPH
5alpha-cholesta-8-en-3beta-ol + NADP+
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5alpha-cholesta-8,24-dien-3beta-ol
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?
additional information
?
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catalyzes reduction of DELTA24 double bond
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?
additional information
?
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anaerobic reduction of 24(25)-enes of lanosterol and other obligatory intermediates of cholesterol biosynthesis from lanosterol in mammals to produce 24(25)-dihydrosterols
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?
additional information
?
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C-24 reduction of sterols probably takes place straight after sterol DELTA8-7 isomerization of zymosterol, which occurs several steps after C-32 demethylation of lanosterol in the 19-step pathway of cholesterol biosynthesis from lanosterol
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-
?
additional information
?
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reduction of DELTA24 double bond is one of the necessary reactions during cholesterol synthesis
-
-
?
additional information
?
-
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important enzyme in the 19-step pathway of cholesterol biosynthesis from lanosterol
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-
?
additional information
?
-
-
important enzyme in the 19-step pathway of cholesterol biosynthesis from lanosterol
-
-
?
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
5alpha-cholesta-7,24-dien-3beta-ol + NADPH
5alpha-cholest-7-en-3beta-ol + NADP+
-
step in the biosynthesis of cholesterol from lanosterol
-
-
?
cholesta-5,7,24-trien-3beta-ol + NADPH
cholest-5,7-dien-3beta-ol + NADP+
-
step in the biosynthesis of cholesterol from lanosterol
-
-
?
lanosterol + NADPH
24-dihydrolanosterol + NADP+
-
step in the biosynthesis of cholesterol from lanosterol
-
-
?
5alpha-cholesta-7,24-dien-3beta-ol + NADPH
5alpha-cholesta-7-en-3beta-ol + NADP+
-
C-24 reduction of sterols probably takes place straight after sterol DELTA8-7 isomerization of zymosterol, which occurs several steps after C-32 demethylation of lanosterol in the 19-step pathway of cholesterol biosynthesis from lanosterol
-
-
?
5alpha-cholesta-7,24-dien-3beta-ol + NADPH
5alpha-cholesta-7-en-3beta-ol + NADP+
-
C-24 reduction of DELTA7,24-diene
-
-
?
5alpha-cholesta-7,24-dien-3beta-ol + NADPH
5alpha-cholesta-7-en-3beta-ol + NADP+
-
most reactive, probably natural substrate
-
-
?
desmosterol + NADPH
cholesterol + NADP+
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5alpha-cholesta-5,24-dien-3beta-ol
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-
?
desmosterol + NADPH
cholesterol + NADP+
-
step in the biosynthesis of cholesterol from lanosterol
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-
?
additional information
?
-
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anaerobic reduction of 24(25)-enes of lanosterol and other obligatory intermediates of cholesterol biosynthesis from lanosterol in mammals to produce 24(25)-dihydrosterols
-
-
?
additional information
?
-
-
C-24 reduction of sterols probably takes place straight after sterol DELTA8-7 isomerization of zymosterol, which occurs several steps after C-32 demethylation of lanosterol in the 19-step pathway of cholesterol biosynthesis from lanosterol
-
-
?
additional information
?
-
-
reduction of DELTA24 double bond is one of the necessary reactions during cholesterol synthesis
-
-
?
additional information
?
-
-
important enzyme in the 19-step pathway of cholesterol biosynthesis from lanosterol
-
-
?
additional information
?
-
-
important enzyme in the 19-step pathway of cholesterol biosynthesis from lanosterol
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
tamoxifen
-
inhibition mechanism and pattern, uncompetitive, 50% inhibition at 0.004 mM, cytotoxic in vivo, inhibitory effect on th whole cholesterol biosynthetic pathway, overview
3-beta-(2-(diethylamino)ethoxy)androst-5-en-17-one
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U18666A, non-competitive inhibition, Ki: 0.000157 mM, IC50 about 0.00015 mM, 690fold higher affinity for the enzyme than substrate lanosterol
Calmodulin antagonists
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calmodulin antagonists inhibit reduction of DELTA24 double bond
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N-(6-aminohexyl)-5-chloro-1-naphthalene sulfonamide
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W-7, specific, dose-dependent inhibition
Triparanol
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4-chloro-alpha-[4-[2-diethylaminoethoxy]phenyl]-alpha-(4-methylphenyl)benze-methanol
Triparanol
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non-competitive inhibition, specific inhibitor, Ki: 0.000523 mM, IC50 about 0.0008 mM, 208fold higher affinity for the enzyme than substrate lanosterol
Triparanol
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1-[p-(beta-diethylaminoethoxy)-phenyl]-1-(p-tolyl)-2-(p-chlorophenyl)-ethanol, MER 29
additional information
-
no inhibition by lovastatin, mevalonolactone, Squalestatin 1, (E)-N-ethyl-N-(6,6-dimethyl-2-hepten-4-ynyl)-3-((3,3'-bithiophen-5-yl)methoxy)benzenemethanamine, NB-598, trans-1,4-bis(2-chlorobenzylaminomethyl)cyclohexane dihydrochloride, AY-9944 and CN- ion
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additional information
-
inhibition mechanism of DELTA22-unsaturated phytosterols
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cholestyramine
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120fold induction and activation by feeding 5% cholestyramine plus 0.1% lovastatin, CL-diet, and by modulating diurnal variation
CO
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substrate lanosterol: required to inhibit 14alpha-methyl demethylase, 14alpha-demethylation of lanosterol. 14alpha-methyl demethylase activity is dominant over 24-reductase activity, and blockade or removal of 14alpha-methyl demethylase activity is absolutely required for the detection of maximal 24-reductase activity when lanosterol substrate is present. 24-reductase activity is activated in time-dependent manner when 14alpha-methyl demethylase is blocked by CO treatment
ketoconazole
-
substrate lanosterol: dose-dependent activation, less effective than miconazole, required to inhibit 14alpha-methyl demethylase, 14alpha-demethylation of lanosterol. 14alpha-methyl demethylase activity is dominant over 24-reductase activity, and blockade or removal of 14alpha-methyl demethylase activity is absolutely required for the detection of maximal 24-reductase activity when lanosterol substrate is present
lovastatin
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120fold induction and activation by feeding 5% cholestyramine plus 0.1% lovastatin, CL-diet, and by modulating diurnal variation
miconazole
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substrate lanosterol: dose-dependent activation, maximum activation with about 0.01 mM miconazole, required to inhibit 14alpha-methyl demethylase, 14alpha-demethylation of lanosterol. 14alpha-methyl demethylase activity is dominant over 24-reductase activity, and blockade or removal of 14alpha-methyl demethylase activity is absolutely required for the detection of maximal 24-reductase activity when lanosterol substrate is present
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.109
4,4',14alpha-trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
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lanosterol
additional information
additional information
-
kinetic behaviour and kinetic data
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00015
3-beta-(2-(diethylamino)ethoxy)androst-5-en-17-one
Rattus norvegicus
-
U18666A, non-competitive inhibition, Ki: 0.000157 mM, IC50 about 0.00015 mM, 690fold higher affinity for the enzyme than substrate lanosterol
0.0008
Triparanol
Rattus norvegicus
-
non-competitive inhibition, specific inhibitor, Ki: 0.000523 mM, IC50 about 0.0008 mM, 208fold higher affinity for the enzyme than substrate lanosterol
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzyme has neuroprotective and cholesterol-synthesizing activities. DHCR24 overexpression confers neuroprotection against apoptosis caused by amyloid beta deposition
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DHC24_RAT
516
2
60047
Swiss-Prot
Secretory Pathway (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
construction of a recombinant adenovirus driving DHCR24 expression vector specific for neurons with neuron-specific promoter, synapsin-1 (SYN1), cloning of a SYN1 promoter DNA fragment of rat enzyme DHCR24, and transfection of recombinant Ad-rSYN1-DHCR24 into HEK AD-293, N2A (mouse neuroblastoma), and MIN6 (mouse pancreatic carcinoma) cells. DHCR24 is specially expressed in HEK AD-293 and N2A cells, but not in MIN6 cells. Adenovirus transfection inhibits apoptosis through scavenging excess reactive oxygen species, and recombinant DHCR24 adenoviruse induces neuron-specific DHCR24 expression
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme mRNA expression level is significantly increased in protein disulfide isomerase A3 siRNA-treated neurons
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the mRNA expression of the enzyme is significantly decreased in the cortical neurons treated with 0.00001 mM 1,25-dihydroxyvitamin D3
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bae, S.H.; Paik, Y.K.
Cholesterol biosynthesis from lanosterol: development of a novel assay method and characterization of rat liver microsomal lanosterol DELTA24-reductase
Biochem. J.
326
609-616
1997
Rattus norvegicus
Filipovic, I.; Buddecke, E.
Calmodulin antagonists suppress cholesterol synthesis by inhibiting sterol DELTA24 reductase
Lipids
22
261-265
1987
Homo sapiens, Rattus norvegicus
Cho, S.Y.; Kim, J.H.; Paik, Y.K.
Cholesterol biosynthesis from lanosterol: differential inhibition of sterol DELTA8-isomerase and other lanosterol-converting enzymes by tamoxifen
Mol. Cells
8
233-239
1998
Rattus norvegicus
Fernandez, C.; Suarez, Y.; Ferruelo, A.J.; Gomez-Coronado, D.; Lasuncion, M.A.
Inhibition of cholesterol biosynthesis by DELTA22-unsaturated phytosterols via competitive inhibition of sterol DELTA24-reductase in mammalian cells
Biochem. J.
366
109-119
2002
Homo sapiens, Rattus norvegicus
Lu, X.; Jia, D.; Zhao, C.; Wang, W.; Liu, T.; Chen, S.; Quan, X.; Sun, D.; Gao, B.
Recombinant adenovirus-mediated overexpression of 3beta-hydroxysteroid-DELTA24 reductase
Neural Regen. Res.
9
504-512
2014
Homo sapiens (Q15392), Homo sapiens, Rattus norvegicus (Q5BQE6)
Yavuz, U.; Alaylioglu, M.; Senguel, B.; Karras, S.N.; Gezen-Ak, D.; Dursun, E.
Protein disulfide isomerase A3 might be involved in the regulation of 24-dehydrocholesterol reductase via vitamin D equilibrium in primary cortical neurons
In Vitro Cell. Dev. Biol. Anim.
57
704-714
2021
Rattus norvegicus
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