Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 5.4.99.7 - Lanosterol synthase and Organism(s) Rattus norvegicus and UniProt Accession P48450

for references in articles please use BRENDA:EC5.4.99.7
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     5 Isomerases
         5.4 Intramolecular transferases
             5.4.99 Transferring other groups
                5.4.99.7 Lanosterol synthase
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Rattus norvegicus
UNIPROT: P48450 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
atlas, oxidosqualene cyclase, lanosterol synthase, 2,3-oxidosqualene cyclase, erg7p, oxidosqualene-lanosterol cyclase, 2,3-oxidosqualene-lanosterol cyclase, 2,3-oxidosqualene:lanosterol cyclase, oxidosqualene:lanosterol cyclase, squalene 2,3-oxide-lanosterol cyclase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lanosterol synthase
-
2,3-Epoxysqualene lanosterol-cyclase
-
-
-
-
2,3-epoxysqualene--lanosterol cyclase
-
-
-
-
2,3-Epoxysqualene-lanosterol cyclase
-
-
-
-
2,3-Oxidosqualene cyclase
2,3-oxidosqualene cyclase-lanosterol synthase
-
-
2,3-Oxidosqualene sterol cyclase
-
-
-
-
2,3-Oxidosqualene-lanosterol cyclase
-
-
-
-
Cyclase, 2,3-oxidosqualene-lanosterol
-
-
-
-
Lanosterol 2,3-oxidosqualene cyclase
-
-
-
-
Oxidosqualene cyclase
-
-
-
-
Oxidosqualene--lanosterol cyclase
-
-
-
-
Oxidosqualene-lanosterol cyclase
-
-
-
-
oxidosqualene:lanosterol cyclase
-
-
Squalene 2,3-epoxide:lanosterol cyclase
-
-
-
-
Squalene 2,3-oxide-lanosterol cyclase
-
-
-
-
Squalene epoxidase-cyclase
-
-
-
-
Squalene-2,3-oxide-lanosterol cyclase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cyclization
-
-
-
-
isomerization
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
(S)-2,3-Epoxysqualene mutase (cyclizing, lanosterol-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9032-71-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-2,3-epoxysqualene
lanosterol
show the reaction diagram
-
-
-
?
2,3-oxidosqualene
lanosterol
show the reaction diagram
-
-
-
?
(3S)-Squalene epoxide
?
show the reaction diagram
-
-
-
-
?
(S)-2,3-oxidosqualene
lanosterol
show the reaction diagram
-
-
-
-
?
(S)-squalene-2,3-epoxide
Lanosterol
show the reaction diagram
2,3-monoepoxysqualene
lanosterol
show the reaction diagram
-
-
-
-
?
2,3:22,23-diepoxysqualene
24(S),25-epoxylanosterol
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-2,3-epoxysqualene
lanosterol
show the reaction diagram
-
-
-
?
2,3-monoepoxysqualene
lanosterol
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(4-Benzenesulfonyl-piperazin-1-yl)-(3,4,5,6-tetrahydro-2H-[1,4']bipyridinyl-4-yl)-methanone
-
IC50: 326 nM
(4aalpha,5alpha,6alpha,8abeta)-Decahydro-5,8a-dimethyl-2-(1,5,9-trimethyldecyl)-6-isoquinolinol
-
and simplified analogues
(6E)-10-Aza-10,11-dihydrosqualene-2,3-epoxide
(6Z)-10-aza-10,11-dihydrosqualene-2,3-epoxide
-
IC50: above 0.02 mM, at a protein concentration of 5 mg/ml
(Z)-3-[4-(4-bromobenzoyl)phenacylidene]quinuclidine
-
IC50: 124 nM, oral and selective inhibition of cholesterol biosynthesis derived from enzyme inhibition
1-(2-methyl-4-pyrimidinyl)-4-(1-(4-bromophenylsulfonyl)piperazin-4-ylcarbonyl)piperidine
-
76% inhibition at 0.001 mM, IC50: 398 nM
1-(2-oxazolinyl)-4-(1-(4-bromophenylsulfonyl)piperazin-4-ylcarbonyl)piperidine
-
87% inhibition at 0.001 mM
1-(2-pyrimidinyl)-4-(1-(4-bromophenylsulfonyl)piperazin-4-ylcarbonyl)piperidine
-
8% inhibition at 0.001 mM
1-(2-thiazolinyl)-4-(1-(4-bromophenylsulfonyl)piperazin-4-ylcarbonyl)piperidine
-
complete inhibition at 0.001 mM
1-(4-iodophenylsulfonyl)-4-(1-(4-pyridyl)piperidon-4-ylcarbonyl)piperazine
-
IC50: 82 nM
1-(4-pyrimidinyl)-4-(1-(4-bromophenylsulfonyl)piperazin-4-ylcarbonyl)piperidine
-
complete inhibition at 0.001 mM, IC50: 116 nM
19-aza-18,19,22,23-tetrahydrosqualene-2,3-epoxide
-
IC50: 0.0075 mM, protein concentration of 5 mg/ml
19-Aza-18,19,22,3-tetrahydrosqualene-2,3-epoxide
-
-
19-Azasqualene
-
-
19-Azasqualene-2,3-epoxide
-
-
2-Aza-2,3-dihydrosqualene
2-aza-2,3-dihydrosqualene alcohol
-
-
2-Aza-2,3-dihydrosqualene N-oxide
22,23-Epoxy-2-aza-2,3-dihydrosqualene
-
slight
22,23-epoxy-2-aza-2,3-dihydrosqualene-N-oxide
-
0.01 mM, 14% inhibition
3-[(4-chlorobenzoyl)-4-phenoxy]quinuclidin-3-ol
-
-
3-[(4-chlorobenzoyl)-4-phenoxy]quinuclidine
3-[2-(4-bromobenzophenone)ethynyl]quinuclidin-3-ol
-
-
3-[Methyl-(4,8,13,17,21-pentamethyl-docosa-4,8,12,16,20-pentaenyl)-amino]-propan-1-ol
-
0.01 mM, 2% inhibition
4-(4-bromobenzoyl)-1-(1-(4-pyridyl)piperidin-4-ylcarbonyl)piperazine
-
96% inhibition at 0.001 mM
4-(4-bromophenylmethyl)-1-(1-(4-pyridyl)piperidin-4-ylcarbonyl)piperazine
-
complete inhibition at 0.001 mM
azasqualene alcohol
-
0.01 mM, 13% inhibition
BIBB 515
-
-
cholesterol
-
an increased cholesterol level suppresses the expression of 2,3-oxidosqualene cyclase
diethyl-(4,8,13,17,21-pentamethyl-docosa-4,8,12,16,20-pentaenyl)-aminoxide
-
IC50: 1.5 mM
Diethyl-(4,8,13,17,21-pentamethyl-docosa-4,8,12,16,20-pentaenyl)-ammonium
-
IC50: 3.2 mM
Iminosqualene
-
-
KCl
-
0-0.1 M: activity decreases with increasing concentration of KCl in the presence of optimal concentrations of Triton X-100
N-(1-Oxododecyl)-4alpha,10-dimethyl-8-aza-trans-decal-3beta-ol
-
potent, competitive
N-[(1,5,9)-Trimethyl-decyl]-4alpha,10-dimethyl-8-aza-decal-3beta-ol
-
strong
N-[3-(1,1'-biphenyl-4-yloxy)propyl]-N,N-dimethylamine
-
IC50: 2500 nM
Squalene maleimide
-
-
Sulfur-substituted squalene oxide analogues
-
mechanism-based inhibition
-
Trimethyl-(4,8,13,17,21-pentamethyl-docosa-4,8,12,16,20-pentaenyl)-ammonium
-
IC50: 5.1 mM
[19-(3,3-Dimethyl-oxiranyl)-4,8,13,17-tetramethyl-nonadeca-4,8,12,16-tetraenyl]-dimethyl-amine
-
0.01 mM, 8% inhibition
[4-(4-Bromo-benzenesulfonyl)-piperazin-1-yl]-(3,4,5,6-tetrahydro-2H-[1,4']bipyridinyl-4-yl)-methanone
-
IC50: 228 nM
[5-(4-(4-chloro-benzoyl)-3-fluoro-phenoxy)-pentyl]-methyl-propyl-ammonium fumarate
-
IC50: 49 nM
{4-[4-(4,5-Dihydro-oxazol-2-yl)-benzylidene]-piperidin-1-yl}-(4-trifluoromethyl-phenyl)-methanone
-
IC50: 90 nM, complete inhibition at 0.001 nM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S105 protein from rat liver
-
required for optimal activity. The S105 protein acts internally within the microsomal membrane system facilitating the access of substrate to specific enzyme sites
-
Triton X-100
-
0.05-0.15%, activates solubilized enzyme up to 300%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.055
(3S)-squalene epoxide
-
-
0.015
2,3-epoxysqualene
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.008
S23515
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000326
(4-Benzenesulfonyl-piperazin-1-yl)-(3,4,5,6-tetrahydro-2H-[1,4']bipyridinyl-4-yl)-methanone
Rattus norvegicus
-
IC50: 326 nM
0.0048
(6E)-10-Aza-10,11-dihydrosqualene-2,3-epoxide
Rattus norvegicus
-
IC50: 0.0048 mM, at a protein concentration of 5 mg/ml
0.02
(6Z)-10-aza-10,11-dihydrosqualene-2,3-epoxide
Rattus norvegicus
-
IC50: above 0.02 mM, at a protein concentration of 5 mg/ml
0.000124
(Z)-3-[4-(4-bromobenzoyl)phenacylidene]quinuclidine
Rattus norvegicus
-
IC50: 124 nM, oral and selective inhibition of cholesterol biosynthesis derived from enzyme inhibition
0.000398
1-(2-methyl-4-pyrimidinyl)-4-(1-(4-bromophenylsulfonyl)piperazin-4-ylcarbonyl)piperidine
Rattus norvegicus
-
76% inhibition at 0.001 mM, IC50: 398 nM
0.000082
1-(4-iodophenylsulfonyl)-4-(1-(4-pyridyl)piperidon-4-ylcarbonyl)piperazine
Rattus norvegicus
-
IC50: 82 nM
0.000116
1-(4-pyrimidinyl)-4-(1-(4-bromophenylsulfonyl)piperazin-4-ylcarbonyl)piperidine
Rattus norvegicus
-
complete inhibition at 0.001 mM, IC50: 116 nM
0.0075
19-aza-18,19,22,23-tetrahydrosqualene-2,3-epoxide
Rattus norvegicus
-
IC50: 0.0075 mM, protein concentration of 5 mg/ml
7.5
2-Aza-2,3-dihydrosqualene
Rattus norvegicus
-
IC50: 7.5 mM
3.7
2-Aza-2,3-dihydrosqualene N-oxide
Rattus norvegicus
-
IC50: 3.7 mM
0.00016
3-[(4-chlorobenzoyl)-4-phenoxy]quinuclidine
Rattus norvegicus
-
IC50: 160 nM
1.5
diethyl-(4,8,13,17,21-pentamethyl-docosa-4,8,12,16,20-pentaenyl)-aminoxide
Rattus norvegicus
-
IC50: 1.5 mM
3.2
Diethyl-(4,8,13,17,21-pentamethyl-docosa-4,8,12,16,20-pentaenyl)-ammonium
Rattus norvegicus
-
IC50: 3.2 mM
0.0025
N-[3-(1,1'-biphenyl-4-yloxy)propyl]-N,N-dimethylamine
Rattus norvegicus
-
IC50: 2500 nM
5.1
Trimethyl-(4,8,13,17,21-pentamethyl-docosa-4,8,12,16,20-pentaenyl)-ammonium
Rattus norvegicus
-
IC50: 5.1 mM
0.000228
[4-(4-Bromo-benzenesulfonyl)-piperazin-1-yl]-(3,4,5,6-tetrahydro-2H-[1,4']bipyridinyl-4-yl)-methanone
Rattus norvegicus
-
IC50: 228 nM
0.000049
[5-(4-(4-chloro-benzoyl)-3-fluoro-phenoxy)-pentyl]-methyl-propyl-ammonium fumarate
Rattus norvegicus
-
IC50: 49 nM
0.00009
{4-[4-(4,5-Dihydro-oxazol-2-yl)-benzylidene]-piperidin-1-yl}-(4-trifluoromethyl-phenyl)-methanone
Rattus norvegicus
-
IC50: 90 nM, complete inhibition at 0.001 nM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0000429
cataractous Shumiya cataract rat
0.000046
normal Shumiya cataract rat
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Shumiya cataract rat
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
in corneal epithelial layer, stromal layer, and endothelial layer
Manually annotated by BRENDA team
-
in lens epithelial layer and shallow cortex layer
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
the enzyme belongs to the terpene cyclase/mutase superfamily of enzymes
physiological function
-
relationship of lanosterol synthase with eye diseases
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LSS_RAT
733
0
83301
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65000
-
x * 65000, SDS-PAGE
75000
-
2 * 75000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 65000, SDS-PAGE
dimer
-
2 * 75000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D139N
reduced activity
D139N/G189A/Q481R
induces cataracts in rats, produces only 39% of the lanosterol produced by wild-type
H469-C472del
deletion allele, inactive
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Saccharomyces cerevisiae
expression in Saccharomyces cerevisiae
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
since the Shumiya cataract rat model represents a new example of hereditary cholesterol deficiency-associated cataracts, it should be useful in the development of therapeutic and/or preventive measures for cataracts
medicine
-
S23515 can exert hypolipidemic effects in addition to its hypotensive activities
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Willett, J.D.; Sharpless, K.B.; Lord, K.E.; van Tamelen, E.E.; Clayton, R.B.
Squalene-2,3-oxide, an intermediate in the enzymatic conversion of squalene to lanosterol and cholesterol
J. Biol. Chem.
242
4182-4191
1967
Rattus norvegicus
Manually annotated by BRENDA team
Saat, Y.A.; Bloch, K.E.
Effect of a supernatant protein on microsomal squalene epoxidase and 2,3-oxidosqualene-lanosterol cyclase
J. Biol. Chem.
251
5155-5160
1976
Rattus norvegicus
Manually annotated by BRENDA team
Taton, M.; Benveniste, P.; Rahier, A.
N-[(1,5,9)-Trimethyl-decyl]-4alpha,10-dimethyl-8-aza-trans-decal-3beta-ol a novel potent inhibitor of 2,3-oxidosqualene cycloartenol and lanosterol cyclases
Biochem. Biophys. Res. Commun.
138
764-770
1986
Rattus norvegicus
Manually annotated by BRENDA team
Cattel, L.; Ceruti, M.; Balliano, G.; Viola, F.; Grosa, G.; Rocco, F.; Brusa, P.
2,3-Oxidosqualene cyclase: from azasqualenes to new site-directed inhibitors
Lipids
30
235-246
1995
Saccharomyces cerevisiae, Candida albicans, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Viola, F.; Brusa, P.; Balliano, G.; Ceruti, M.; Boutaud, O.; Schuber, F.; Cattel, L.
Inhibition of 2,3-oxidosqualene cyclase and sterol biosynthesis by 10- and 19-azasqualene derivatives
Biochem. Pharmacol.
50
787-796
1995
Saccharomyces cerevisiae, Candida albicans, Homo sapiens, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Jolidon, S.; Polak, A.M.; Guerry, P.; Hartman, P.G.
Inhibitors of 2,3-oxidosqualene lanosterol-cyclase as potential antifungal agents
Biochem. Soc. Trans.
18
47-48
1990
Candida albicans, Rattus norvegicus
Manually annotated by BRENDA team
Kusano, M.; Abe, I.; Sankawa, U.; Ebizuka, Y.
Purification and some properties of squalene 2,3-epoxide: lanosterol cyclase from rat liver
Chem. Pharm. Bull.
39
239-241
1991
Rattus norvegicus
Manually annotated by BRENDA team
Wannamaker, M.W.; Waid, P.P.; van Sickle, W.A.; McCarthy, J.R.; Wilson, P.K.; Schatzman, G.L.; Moore, W.R.
N-(1-Oxododecyl)-4alpha,10-dimethyl-8-aza-trans-decal-3beta-ol: a potent competitive inhibitor of 2,3-oxidosqualene cyclase
J. Med. Chem.
35
3581-3583
1992
Rattus norvegicus
Manually annotated by BRENDA team
Barth, M.M.; Binet, J.L.; Thomas, D.M.; de Fornel, D.C.; Samreth, S.; Schuber, F.J.; Renaut, P.P.
Structural and stereoelectronic requirements for the inhibition of mammalian oxidosqualene cyclase by substituted isoquinoline derivatives
J. Med. Chem.
39
2302-2312
1996
Rattus norvegicus
Manually annotated by BRENDA team
Stach, D.; Zheng, Y.F.; Perez, A.L.; Oehlschlager, A.C.; Abe, I.; Prestwich, G.D.; Hartman, P.G.
Synthesis and inhibition studies of sulfur-substituted squalene oxide analogues as mechanism-based inhibitors of 2,3-oxidosqualene-lanosterol cyclase
J. Med. Chem.
40
201-209
1997
Candida albicans, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Moore, W.R.; Schatzman, G.L.
Purification of 2,3-oxidosqualene cyclase from rat liver
J. Biol. Chem.
267
22003-22006
1992
Rattus norvegicus
Manually annotated by BRENDA team
Abe, I.; Prestwich, G.D.
Molecular cloning, characterization, and functional expression of rat oxidosqualene cyclase cDNA
Proc. Natl. Acad. Sci. USA
92
9274-9278
1995
Rattus norvegicus
Manually annotated by BRENDA team
Astruc, M.; Tabacik, C.; Descomps, B.; Crastes de Paulet, A.
Squalene epoxidase and oxidosqualene lanosterol-cyclase activities in cholesterogenic and non-cholesterogenic tissues
Biochim. Biophys. Acta
487
204-211
1977
Rattus norvegicus
Manually annotated by BRENDA team
Cattel, L.; Ceruti, M.
Inhibitors of 2,3-oxidosqualene cyclase as tools for studying the mechanism and function of the enzyme
Crit. Rev. Biochem. Mol. Biol.
33
353-373
1998
Saccharomyces cerevisiae, Candida albicans, Canis lupus familiaris, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Brown, G.R.; Hollinshead, D.M.; Stokes, E.S.; Clarke, D.S.; Eakin, M.A.; Foubister, A.J.; Glossop, S.C.; Griffiths, D.; Johnson, M.C.; McTaggart, F.; Mirrlees, D.J.; Smith, G.J.; Wood, R.
Quinuclidine inhibitors of 2,3-oxidosqualene cyclase-lanosterol synthase: optimization from lipid profiles
J. Med. Chem.
42
1306-1311
1999
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Brown, G.R.; Hollinshead, D.M.; Stokes, E.S.; Waterson, D.; Clarke, D.S.; Foubister, A.J.; Glossop, S.C.; McTaggart, F.; Mirrlees, D.J.; Smith, G.J.; Wood, R.
A novel series of 4-piperidinopyridine and 4-piperidinopyrimidine inhibitors of 2,3-oxidosqualene cyclase-lanosterol synthase
J. Med. Chem.
43
4964-4972
2000
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Hinshaw, J.C.; Suh, D.Y.; Garnier, P.; Buckner, F.S.; Eastman, R.T.; Matsuda, S.P.; Joubert, B.M.; Coppens, I.; Joiner, K.A.; Merali, S.; Nash, T.E.; Prestwich, G.D.
Oxidosqualene cyclase inhibitors as antimicrobial agents
J. Med. Chem.
46
4240-4243
2003
Pneumocystis carinii, Rattus norvegicus, Trypanosoma brucei, Trypanosoma cruzi
Manually annotated by BRENDA team
Venteclef, N.; Guillard, R.; Issandou, M.
The imidazoline-like drug S23515 affects lipid metabolism in hepatocyte by inhibiting the oxidosqualene: lanosterol cyclase activity
Biochem. Pharmacol.
69
1041-1048
2005
Macaca fascicularis, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Mori, M.; Li, G.; Abe, I.; Nakayama, J.; Guo, Z.; Sawashita, J.; Ugawa, T.; Nishizono, S.; Serikawa, T.; Higuchi, K.; Shumiya, S.
Lanosterol synthase mutations cause cholesterol deficiency-associated cataracts in the Shumiya cataract rat
J. Clin. Invest.
116
395-404
2006
Rattus norvegicus (P48450)
Manually annotated by BRENDA team
Dang, H.; Liu, Y.; Pang, W.; Wang, N.; Shyy, J.Y.; Zhu, Y.
Suppression of 2,3-oxidosqualene cyclase by high-fat diet contributes to liver X receptor-alpha -mediated improvement of hepatic lipid profile
J. Biol. Chem.
284
6218-6226
2009
Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Kang, L.; Shen, X.; Yang, M.; Zhang, G.; Zhang, J.; Qin, B.; Yang, L.; Hu, N.; Guan, H.
Distribution of lanosterol synthase and lanosterol in cornea, lens and retina tissue of rats
Zhonghua Shiyan Yanke Zazhi
35
201-206
2017
Rattus norvegicus
-
Manually annotated by BRENDA team