Squalene monooxygenase

Squalene epoxidase
Chemical reaction catalyzed by squalene epoxidase.
Identifiers
EC no.1.14.13.132
CAS no.9029-62-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
SQLE
Identifiers
AliasesSQLE, entrez:6713, squalene epoxidase
External IDsOMIM: 602019; MGI: 109296; HomoloGene: 2355; GeneCards: SQLE; OMA:SQLE - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_003129

NM_009270

RefSeq (protein)

NP_003120

NP_033296

Location (UCSC)Chr 8: 125 – 125.02 MbChr 15: 59.19 – 59.2 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Squalene monooxygenase (also called squalene epoxidase) is a eukaryotic enzyme that uses NADPH and diatomic oxygen to oxidize squalene to 2,3-oxidosqualene (squalene epoxide). Squalene epoxidase catalyzes the first oxygenation step in sterol biosynthesis and is thought to be one of the rate-limiting enzymes in this pathway.[5] In humans, squalene epoxidase is encoded by the SQLE gene.[6] Several eukaryote genomes lack a squalene monooxygenase encoding gene, but instead encode an alternative squalene epoxidase that performs the same task.[7]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000104549Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000022351Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ "Entrez Gene: SQLE squalene epoxidase".
  6. ^ Nagai M, Sakakibara J, Wakui K, Fukushima Y, Igarashi S, Tsuji S, Arakawa M, Ono T (Aug 1997). "Localization of the squalene epoxidase gene (SQLE) to human chromosome region 8q24.1". Genomics. 44 (1): 141–3. doi:10.1006/geno.1997.4825. PMID 9286711.
  7. ^ Pollier J, Vancaester E, Kuzhiumparambil U, Vickers CE, Vandepoele K, Goossens A, Fabris M (2019). "A widespread alternative squalene epoxidase participates in eukaryote steroid biosynthesis". Nature Microbiology. 4 (2): 226–233. doi:10.1038/s41564-018-0305-5. hdl:1854/LU-8587985. PMID 30478288. S2CID 53726187.