KEGG   ENZYME: 1.14.13.132Help
Entry
EC 1.14.13.132              Enzyme                                 

Name
squalene monooxygenase;
squalene epoxidase;
squalene-2,3-epoxide cyclase;
squalene 2,3-oxidocyclase;
squalene hydroxylase;
squalene oxydocyclase;
squalene-2,3-epoxidase
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy
Sysname
squalene,NADPH:oxygen oxidoreductase (2,3-epoxidizing)
Reaction(IUBMB)
squalene + NADPH + H+ + O2 = (3S)-2,3-epoxy-2,3-dihydrosqualene + NADP+ + H2O [RN:R02874]
Reaction(KEGG)
R02874;
(other) R02873
Show
Substrate
squalene [CPD:C00751];
NADPH [CPD:C00005];
H+ [CPD:C00080];
O2 [CPD:C00007]
Product
(3S)-2,3-epoxy-2,3-dihydrosqualene [CPD:C01054];
NADP+ [CPD:C00006];
H2O [CPD:C00001]
Comment
A flavoprotein (FAD). This enzyme, together with EC 5.4.99.7 lanosterol synthase, was formerly known as squalene oxidocyclase. The electron donor, NADPH, is coupled via EC 1.6.2.4, NADPH---hemoprotein reductase [5,7].
History
EC 1.14.13.132 created 1961 as EC 1.99.1.13, transferred 1965 to EC 1.14.1.3, part transferred 1972 to EC 1.14.99.7, transferred 2011 to EC 1.14.13.132
Pathway
Steroid biosynthesis
Sesquiterpenoid and triterpenoid biosynthesis
Metabolic pathways
Biosynthesis of secondary metabolites
Orthology
K00511  
squalene monooxygenase
Genes
HSA: 
6713(SQLE)
PTR: 
464383(SQLE)
PPS: 
100976805(SQLE)
GGO: 
101129462(SQLE)
PON: 
NLE: 
100585992(SQLE)
MCC: 
706764(SQLE)
MCF: 
102118907(SQLE)
CJC: 
100410163(SQLE)
MMU: 
20775(Sqle)
RNO: 
29230(Sqle)
CGE: 
NGI: 
103743909(Sqle)
HGL: 
101709317(Sqle)
OCU: 
100356021(SQLE)
TUP: 
102473783(SQLE)
CFA: 
608021(SQLE)
AML: 
100465589(SQLE)
UMR: 
103661624(SQLE)
FCA: 
101086537(SQLE)
PTG: 
102948681(SQLE)
BTA: 
526535(SQLE)
BOM: 
102264644(SQLE)
PHD: 
102342379(SQLE)
CHX: 
102187506(SQLE)
OAS: 
100125351(SQLE)
SSC: 
100113409(SQLE)
CFR: 
102518096(SQLE)
BACU: 
103015244(SQLE)
LVE: 
103088551(SQLE)
ECB: 
100067615(SQLE)
MYB: 
MYD: 
102766276(SQLE)
PALE: 
102894920(SQLE)
MDO: 
100032247(SQLE)
SHR: 
100918180(SQLE)
OAA: 
100076751(SQLE)
GGA: 
420335(SQLE)
MGP: 
100546703(SQLE)
APLA: 
101802617(SQLE)
TGU: 
100225604(SQLE)
FAB: 
101806873(SQLE)
PHI: 
102109574(SQLE)
FPG: 
101920264(SQLE)
FCH: 
102054050(SQLE)
CLV: 
102090054(SQLE)
ASN: 
102368291(SQLE)
AMJ: 
102563308(SQLE)
PSS: 
102444614(SQLE)
CMY: 
102929627(SQLE)
ACS: 
100557553(sqle)
PBI: 
XTR: 
100491400(sqle)
DRE: 
799528(sqlea)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
CMK: 
103187848(sqle)
BFO: 
SPU: 
LGI: 
TAD: 
AQU: 
ATH: 
AT1G58440(XF1) AT2G22830(SQE2) AT4G37760(SQE3) AT5G24140(SQP2) AT5G24150(SQP1) AT5G24160(SQE6)
ALY: 
CRB: 
EUS: 
CIT: 
CIC: 
TCC: 
GMX: 
PVU: 
MTR: 
CAM: 
FVE: 
PPER: 
PMUM: 
MDM: 
CSV: 
CMO: 
RCU: 
POP: 
VVI: 
SLY: 
SOT: 
OSA: 
DOSA: 
Os03t0231700-01(Os03g0231700) Os03t0231800-02(Os03g0231800)
OBR: 
BDI: 
SBI: 
SORBI_01g042050(SORBIDRAFT_01g042050)
ZMA: 
100274333 100285558(pco148653)
SITA: 
PDA: 
ATR: 
s00065p00032730(AMTR_s00065p00032730)
SMO: 
PPP: 
VCN: 
OLU: 
OTA: 
BPG: 
MIS: 
MPP: 
CSL: 
CVR: 
CME: 
GSL: 
SCE: 
YGR175C(ERG1)
AGO: 
ERC: 
KLA: 
LTH: 
VPO: 
ZRO: 
CGR: 
NCS: 
NCAS_0A06930(NCAS0A06930)
NDI: 
NDAI_0D01990(NDAI0D01990)
TPF: 
TPHA_0E03160(TPHA0E03160)
TBL: 
TBLA_0C05980(TBLA0C05980) TBLA_0H02130(TBLA0H02130)
TDL: 
TDEL_0E04440(TDEL0E04440)
KAF: 
KAFR_0D01720(KAFR0D01720)
PPA: 
DHA: 
PIC: 
PGU: 
SPAA: 
LEL: 
CAL: 
CaO19.406(ERG1) CaO19.8036(ERG1)
CTP: 
COT: 
CDU: 
CTEN: 
YLI: 
CLU: 
NCR: 
SMP: 
PAN: 
TTT: 
MTM: 
CTHR: 
MGR: 
TMN: 
FGR: 
NHE: 
TRE: 
MAW: 
MAJ: 
CMT: 
VAL: 
ELA: 
SSL: 
BFU: 
MBE: 
AFM: 
AOR: 
AOR_1_1218114(AO090701000685)
ANG: 
ANI_1_450034(An03g03770)
AFV: 
ACT: 
NFI: 
PCS: 
CIM: 
CPW: 
PBL: 
URE: 
ABE: 
TVE: 
AJE: 
PNO: 
PTE: 
BZE: 
BSC: 
BOR: 
ZTR: 
PFJ: 
BCOM: 
TML: 
SPO: 
CNE: 
CNB: 
CGI: 
TMS: 
DSQ: 
PCO: 
SHS: 
PSQ: 
ADL: 
FME: 
GTR: 
LBC: 
MPR: 
MRR: 
CCI: 
SCM: 
ABP: 
AGABI1DRAFT69774(AGABI1DRAFT_69774)
ABV: 
AGABI2DRAFT205454(AGABI2DRAFT_205454)
CPUT: 
SLA: 
UMA: 
PFP: 
MGL: 
PGR: 
MLR: 
WSE: 
DDI: 
DPP: 
DFA: 
DFA_07098(sqle)
ACAN: 
TBR: 
TCR: 
LMA: 
LIF: 
LDO: 
LMI: 
LBZ: 
NGR: 
MAH: 
CCX: 
SUR: 
FTE: 
 » show all
Taxonomy
Reference
1  [PMID:5918046]
  Authors
Cory EJ, Russey WE, Ortiz de Montellano PR.
  Title
2,3-oxidosqualene, an intermediate in the biological synthesis of sterols from squalene.
  Journal
J. Am. Chem. Soc. 88 (1966) 4750-1.
Reference
2  [PMID:13438881]
  Authors
TCHEN TT, BLOCH K.
  Title
On the conversion of squalene to lanosterol in vitro.
  Journal
J. Biol. Chem. 226 (1957) 921-30.
Reference
3  [PMID:5918048]
  Authors
Van Tamelen EE, Willett JD, Clayton RB, Lord KE.
  Title
Enzymic conversion of squalene 2,3-oxide to lanosterol and cholesterol.
  Journal
J. Am. Chem. Soc. 88 (1966) 4752-4.
Reference
4  [PMID:5438357]
  Authors
Yamamoto S, Bloch K.
  Title
Studies on squalene epoxidase of rat liver.
  Journal
J. Biol. Chem. 245 (1970) 1670-4.
Reference
5  [PMID:234459]
  Authors
Ono T, Bloch K
  Title
Solubilization and partial characterization of rat liver squalene epoxidase.
  Journal
J. Biol. Chem. 250 (1975) 1571-9.
Reference
6  [PMID:8358382]
  Authors
Satoh T, Horie M, Watanabe H, Tsuchiya Y, Kamei T
  Title
Enzymatic properties of squalene epoxidase from Saccharomyces cerevisiae.
  Journal
Biol. Pharm. Bull. 16 (1993) 349-52.
Reference
7  [PMID:12467639]
  Authors
Chugh A, Ray A, Gupta JB
  Title
Squalene epoxidase as hypocholesterolemic drug target revisited.
  Journal
Prog. Lipid. Res. 42 (2003) 37-50.
Reference
8  [PMID:17852349]
  Authors
He F, Zhu Y, He M, Zhang Y
  Title
Molecular cloning and characterization of the gene encoding squalene epoxidase in Panax notoginseng.
  Journal
DNA. Seq. 19 (2008) 270-3.
  Sequence
[up:Q1PID4]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9029-62-3

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