Lanosterol synthase

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Lanosterol synthase
Lanosterol synthase

Existing structural data : 1W6J , 1W6K

Properties of human protein
Mass / length primary structure 732 amino acids
Secondary to quaternary structure Monomer, membrane protein (ER)
Identifier
Gene names LSS OSC
External IDs
Enzyme classification
EC, category 5.4.99.7 ,  isomerase
Response type Cycling
Substrate Squalene epoxide
Products Lanosterol
Occurrence
Parent taxon Eukaryotes
Orthologue
human House mouse
Entrez 4047 16987
Ensemble ENSG00000160285 ENSMUSG00000033105
UniProt P48449 Q8BLN5
Refseq (mRNA) NM_001001438 NM_146006
Refseq (protein) NP_001001438 NP_666118
Gene locus Chr 21: 46.19 - 46.23 Mb Chr 10: 76.53 - 76.56 Mb
PubMed search 4047 16987

The lanosterol synthase is the enzyme that in eukaryotes the cyclization to of squalene lanosterol catalyzed . This reaction is part of the cholesterol biosynthesis in animals, but also in plants, which convert the larger amount of squalene epoxide to cycloartenol . Lanosterol synthase is localized in the membrane of the endoplasmic reticulum .

The cycloartenol synthase in plants and Hopensynthase in some bacteria are homologues of lanosterol synthase, which are related to evolutionary biology with her.

The expression of lanosterol synthase is regulated by the concentration of HDAC3 in the nucleus.

Catalyzed reaction

(S) -Squalene-2,3-epoxy ⇒ Lanosterol

(S) -Squalene-2,3-epoxide is cyclized to lanosterol.

Individual evidence

  1. ↑ Homologues at OMA
  2. ↑ a b Swiss Institute of Bioinformatics (SIB): PROSITE documentation PDOC00825. Terpenes synthases. Retrieved August 12, 2011 .
  3. ↑ Ruf A, Müller F, D'Arcy B, et al. : The monotopic membrane protein human oxidosqualene cyclase is active as monomer . In: Biochem. Biophys. Res. Commun. . 315, No. 2, March 2004, pp. 247-54. doi : 10.1016 / j.bbrc.2004.01.052 . PMID 14766201 .
  4. ↑ Kolesnikova MD, Xiong Q, Lodeiro S, Hua L, Matsuda SP: Lanosterol biosynthesis in plants . In: Arch. Biochem. Biophys. . 447, No. 1, March 2006, pp. 87-95. doi : 10.1016 / j.abb.2005.12.010 . PMID 16445886 .
  5. ↑ Villagra A, Ulloa N, Zhang X, Yuan Z, Sotomayor E, Seto E: Histone deacetylase 3 down-regulates cholesterol synthesis through repression of lanosterol synthase gene expression . In: J. Biol. Chem. . 282, No. 49, December 2007, pp. 35457-70. doi : 10.1074 / jbc.M701719200 . PMID 17925399 .

Web links

Wikibooks: Biochemistry and Pathobiochemistry: Cholesterol Biosynthesis  - Learning and Teaching Materials