| Entry |
|
| 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 O2 as oxidant and incorporation or
reduction of oxygen. The oxygen incorporated need not be derived
from O2;
Miscellaneous
 |
| Sysname |
squalene,hydrogen-donor:oxygen oxidoreductase (2,3-epoxidizing) |
| Reaction(IUBMB) |
squalene + AH2 + O2 = (S)-squalene-2,3-epoxide + A + H2O [RN:R02873] |
| Reaction(KEGG) |
R02873;
(other) R02874
 |
| Substrate |
squalene [CPD:C00751];
AH2 [CPD:C00030];
O2 [CPD:C00007] |
| Product |
(S)-squalene-2,3-epoxide [CPD:C01054];
A [CPD:C00028];
H2O [CPD:C00001] |
| Cofactor |
FAD [CPD:C00016] |
| Comment |
A flavoprotein (FAD). This enzyme, together with EC 5.4.99.7
lanosterol synthase, was formerly known as squalene oxidocyclase. |
| Pathway |
PATH: ec00100 Steroid biosynthesis
PATH: ec01062 Biosynthesis of terpenoids and steroids
PATH: ec01066 Biosynthesis of alkaloids derived from terpenoid and
polyketide
PATH: ec01070 Biosynthesis of plant hormones
PATH: ec01100 Metabolic pathways |
| Orthology |
KO: K00511 squalene monooxygenase |
| Genes |
HSA: 6713(SQLE)
PTR: 464383(SQLE)
MCC: 706764(SQLE)
MMU: 20775(Sqle)
RNO: 29230(Sqle)
CFA: 608021(SQLE)
BTA: 526535(SQLE)
SSC: 100113409(SQLE)
ECB: 100067615(SQLE)
MDO: 100032247(SQLE)
OAA: 100076751
TGU: 100225604
DRE: 799528
BFO: BRAFLDRAFT_288182
SPU: 584086 591651
TAD: TRIADDRAFT_63342
ATH: AT1G58440(XF1) AT4G37760(SQE3) AT5G24140(SQP2)
POP: POPTR_411973 POPTR_831444 POPTR_832433
RCU: RCOM_0859900 RCOM_1585750
VVI: 100254037(GSVIVT00015002001) 100260031(GSVIVT00038547001)
100262930(GSVIVT00012453001) 100265235(GSVIVT00038545001)
OSA: 4332152(Os03g0231700) 4332153(Os03g0231800)
SBI: SORBI_01g042050(SORBIDRAFT_01g042050)
ZMA: 100274333 100285558(pco148653)
PPP: PHYPADRAFT_224792
OLU: OSTLU_88065
CME: CMH256C
SCE: YGR175C(ERG1)
AGO: AGOS_AAL141C
KLA: KLLA0F15224g
LTH: KLTH0B03784g
PIC: PICST_75910(ERG1)
PPA: PAS_chr3_0124
VPO: Kpol_2002p90
LEL: LELG_00710
ZRO: ZYRO0B10912g
CTP: CTRG_05483
CDU: CD36_08100
CGR: CAGL0D05940g
YLI: YALI0E15730g
SPO: SPBC713.12(erg1)
NCR: NCU08280
PAN: PODANSg7130
MGR: MGG_06139
FGR: FG06215.1
AFM: AFUA_5G07780
AOR: AO090701000685
ANG: An03g03770
AFV: AFLA_061500
PCS: Pc22g15550
NFI: NFIA_079490
CIM: CIMG_06149
URE: UREG_04240
SSL: SS1G_13084
BFU: BC1G_14066
CNE: CND06110
CNB: CNBD0290
LBC: LACBIDRAFT_190855
MPR: MPER_07144 MPER_15678
UMA: UM02398.1
MGL: MGL_0127
DDI: DDB_0234143(sqle)
TBR: Tb11.02.0780
TCR: 509589.20
LMA: LmjF13.1620
LIF: LinJ13.1560
LBZ: LbrM13_V2.1480
 |
Reference Authors Title
Journal Organism
|
1 [PMID:5918046]
Cory EJ, Russey WE, Ortiz de Montellano PR.
2,3-oxidosqualene, an intermediate in the biological synthesis of
sterols from squalene.
J. Am. Chem. Soc. 88 (1966) 4750-1.
Rattus norvegicus [GN:rno] |
Reference Authors Title Journal Organism
|
2 [PMID:13438881]
TCHEN TT, BLOCH K.
On the conversion of squalene to lanosterol in vitro.
J. Biol. Chem. 226 (1957) 921-30.
Rattus norvegicus [GN:rno] |
Reference Authors Title
Journal
|
3 [PMID:5918048]
Van Tamelen EE, Willett JD, Clayton RB, Lord KE.
Enzymic conversion of squalene 2,3-oxide to lanosterol and
cholesterol.
J. Am. Chem. Soc. 88 (1966) 4752-4. |
Reference Authors Title Journal Organism
|
4 [PMID:5438357]
Yamamoto S, Bloch K.
Studies on squalene epoxidase of rat liver.
J. Biol. Chem. 245 (1970) 1670-4.
Rattus norvegicus [GN:rno] |
| Other DBs |
ExplorEnz - The Enzyme Database: 1.14.99.7
IUBMB Enzyme Nomenclature: 1.14.99.7
ExPASy - ENZYME nomenclature database: 1.14.99.7
BRENDA, the Enzyme Database: 1.14.99.7
CAS: 9029-62-3 |