Enzyme

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     5. Isomerases
        5.4 Intramolecular transferases
            5.4.99 Transferring other groups
ID:5.4.99.7
Description:Lanosterol synthase.
Alternative Name: Squalene-2,3-oxide-lanosterol cyclase.
Oxidosqualene--lanosterol cyclase.
2,3-epoxysqualene--lanosterol cyclase.
Prosite: PDOC00825;
PDB:
PDBScop
1W6K 8030915; 8030916; 8043294; 8043295;
1W6J 8030915; 8030916; 8043294; 8043295;
3SQC 8026013; 8026015; 8038392; 8038394; 8026013; 8026015; 8038392; 8038394; 8026013; 8026015; 8038392; 8038394;
1UMP 8026013; 8026015; 8038392; 8038394; 8026013; 8026015; 8038392; 8038394; 8026013; 8026015; 8038392; 8038394;
1O79 8026013; 8026015; 8038392; 8038394; 8026013; 8026015; 8038392; 8038394; 8026013; 8026015; 8038392; 8038394;
 » show all

Cath: 1.50.10.20; 2.40.50.310;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 5.4.99.7
BRENDA Enzyme Link: BRENDA 5.4.99.7
KEGG Enzyme Link: KEGG5.4.99.7
BioCyc Enzyme Link: BioCyc 5.4.99.7
ExPASy Enzyme Link: ExPASy5.4.99.7
EC2PDB Enzyme Link: EC2PDB 5.4.99.7
ExplorEnz Enzyme Link: ExplorEnz 5.4.99.7
PRIAM enzyme-specific profiles Link: PRIAM 5.4.99.7
IntEnz Enzyme Link: IntEnz 5.4.99.7
MEDLINE Enzyme Link: MEDLINE 5.4.99.7
MSA:

5.4.99.7;

Phylogenetic Tree:

5.4.99.7;

Uniprot:
M-CSA:
RHEA:14621 (S)-2,3-epoxysqualene = lanosterol
RULE(radius=1) ([*:1]-[C;H0;+0:2](-[*:3]-[*:4]-[CH;+0:5]=[C;H0;+0:6](-[*:7])-[*:8])=[CH;+0:9]-[*:10]-[*:11]-[CH;+0:12]=[C;H0;+0:13](-[CH3;+0:14])-[*:15]-[*:16]-[CH;+0:17]=[C;H0;+0:18](-[*:19])-[*:20].[*:21]-[C;H0;+0:22]1(-[*:23])-[*:24]-[O;H0;+0:25]-1)>>[*:1]-[C;H0;+0:2]12-[*:3]-[*:4]-[CH;+0:5](-[CH;+0:6](-[*:7])-[*:8])-[C;H0;+0:9]-1(-[CH3;+0:14])-[*:10]-[*:11]-[C;H0;+0:12]1=[C;H0;+0:13]-2-[*:15]-[*:16]-[CH;+0:17](-[C;H0;+0:22](-[*:21])(-[*:23])-[*:24]-[OH;+0:25])-[C;H0;+0:18]-1(-[*:19])-[*:20]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Molecular cloning of the human gene encoding lanosterol synthase from a liver cDNA library.Baker CH, Matsuda SP, Liu DR, Corey EJ1995 Aug 47639730
Molecular cloning, characterization, and functional expression of rat oxidosqualene cyclase cDNA.Abe I, Prestwich GD1995 Sep 267568116
A soluble 2,3-oxidosqualene sterol cyclase.Dean PD, Ortiz de Montellano PR, Bloch K, Corey EJ1967 Jun 256027261
Some properties of the microsomal 2,3-oxidosqualene sterol cyclase.Yamamoto S, Lin K, Bloch K1969 May5257956
Effects of a supernatant protein activator on microsomal squalene-2,3-oxide-lanosterol cyclase.Caras IW, Bloch K1979 Dec 10500676
A comprehensive machine-readable view of the mammalian cholesterol biosynthesis pathway.Mazein A, Watterson S, Hsieh WY, Griffiths WJ, Ghazal P2013 Jul 123583456
Catalytic mechanism and product specificity of oxidosqualene-lanosterol cyclase: a QM/MM study.Tian BX, Eriksson LA2012 Nov 2923130825
Site-saturated mutagenesis of histidine 234 of Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase demonstrates dual functions in cyclization and rearrangement reactions.Wu TK, Liu YT, Chang CH, Yu MT, Wang HJ2006 May 1716683806
Tryptophan 232 within oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae influences rearrangement and deprotonation but not cyclization reactions.Wu TK, Yu MT, Liu YT, Chang CH, Wang HJ, Diau EW2006 Mar 3016562881
The monotopic membrane protein human oxidosqualene cyclase is active as monomer.Ruf A, Müller F, D'Arcy B, Stihle M, Kusznir E, Handschin C, Morand OH, Thoma R2004 Mar 514766201
Purification, tandem mass characterization, and inhibition studies of oxidosqualene-lanosterol cyclase enzyme from bovine liver.Wu TK, Huang CY, Ko CY, Chang CH, Chen YJ, Liao HK2004 Jan 114678783