| Entry |
|
|---|
| Name |
squalene synthase;
farnesyltransferase;
presqualene-diphosphate synthase;
presqualene synthase;
squalene synthetase;
farnesyl-diphosphate farnesyltransferase;
SQS |
|---|
| Class |
Transferases;
Transferring alkyl or aryl groups, other than methyl groups;
Transferring alkyl or aryl groups, other than methyl groups (only
sub-subclass identified to date)
 |
|---|
| Sysname |
farnesyl-diphosphate:farnesyl-diphosphate farnesyltransferase |
|---|
| Reaction(IUBMB) |
(1) (1a) 2 farnesyl diphosphate = diphosphate + presqualene
diphosphate [RN:R00702];
(2) (1b) presqualene diphosphate + NAD(P)H + H+ = squalene +
diphosphate + NAD(P)+ [RN:R02872] |
|---|
| Reaction(KEGG) |
R00702 R02872;
(other) R06223
 |
|---|
| Substrate |
farnesyl diphosphate [CPD:C00448];
presqualene diphosphate [CPD:C03428];
NADH [CPD:C00004];
NADPH [CPD:C00005];
H+ [CPD:C00080] |
|---|
| Product |
diphosphate [CPD:C00013];
presqualene diphosphate [CPD:C03428];
squalene [CPD:C00751];
NAD+ [CPD:C00003];
NADP+ [CPD:C00006] |
|---|
| Inhibitor |
alpha-Phosphono sulfonate triacid [CPD:C05355] |
|---|
| Comment |
This microsomal enzyme catalyses the first committed step in the
biosynthesis of sterols. The enzyme from yeast requires either Mg2+
or Mn2+ for activity. In the absence of NAD(P)H, presqualene
diphosphate (PSPP) is accumulated. When NAD(P)H is present,
presqualene diphosphate does not dissociate from the enzyme during
the synthesis of squalene from farnesyl diphosphate (FPP) [8]. High
concentrations of FPP inhibit the production of squalene but not of
PSPP [8]. |
|---|
| 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: K00801 farnesyl-diphosphate farnesyltransferase |
|---|
| Genes |
HSA: 2222(FDFT1)
PTR: 740684(FDFT1)
MCC: 696396(FDFT1)
MMU: 14137(Fdft1)
RNO: 29580(Fdft1)
CFA: 477362(FDFT1)
BTA: 281767(FDFT1)
ECB: 100060929
MDO: 100029000
OAA: 100082427
GGA: 422038(FDFT1)
TGU: 100217567
XTR: 100216201
DRE: 571911(fdft1)
BFO: BRAFLDRAFT_198742
SPU: 586013
TAD: TRIADDRAFT_27912
ATH: AT4G34640(SQS1) AT4G34650(SQS2)
POP: POPTR_818128 POPTR_833037
RCU: RCOM_1450010
VVI: 100265798(GSVIVT00035946001)
OSA: 4334492(Os03g0805100) 4342663(Os07g0200700)
SBI: SORBI_01g004550(SORBIDRAFT_01g004550)
ZMA: 100191601 541614(sqs1)
PPP: PHYPADRAFT_59853
CRE: CHLREDRAFT_99438
OLU: OSTLU_31144
CME: CMG178C
SCE: YHR190W(ERG9)
AGO: AGOS_AFR444C
KLA: KLLA0D08866g
LTH: KLTH0F06886g
DHA: DEHA0D03245g
PIC: PICST_83429(ERG9)
PPA: PAS_chr3_0317
VPO: Kpol_541p19
LEL: LELG_02428
ZRO: ZYRO0A00924g
CTP: CTRG_01858
CDU: CD36_22740(ERG9)
CGR: CAGL0M07095g
YLI: YALI0A10076g
SPO: SPBC646.05c(erg9)
NCR: NCU06054
PAN: PODANSg2377
MGR: MGG_09239
FGR: FG09381.1
AFM: AFUA_7G01220
AOR: AO090010000204
ANG: An12g01890
AFV: AFLA_117780
PCS: Pc21g13930
NFI: NFIA_113940
CIM: CIMG_08115
URE: UREG_04164
SSL: SS1G_02527
BFU: BC1G_01273
CNE: CNC05660
CNB: CNBC1530
MPR: MPER_11859
UMA: UM04374.1
MGL: MGL_3284
MBR: MONBRDRAFT_38891
DDI: DDB_0231376(fdfT)
TET: TTHERM_00382150
TBR: Tb927.8.7120
TCR: 507897.20 508369.20
LMA: LmjF31.2940
LIF: LinJ31.3660
LBZ: LbrM31_V2.3310
PTI: PHATRDRAFT_13160
TPS: THAPSDRAFT_268488
AVN: Avin_20770
TTU: TERTU_3241
MCA: MCA0813(sqs)
NOC: Noc_1321
AEH: Mlg_2690
HHA: Hhal_2280
TAU: Tola_2974
AFE: Lferr_1784
AFR: AFE_2125
REU: Reut_A3084
RME: Rmet_5617
CTI: RALTA_B0216
BMA: BMAA1840
BMV: BMASAVP1_0843
BML: BMA10229_1133
BMN: BMA10247_A2107
BPS: BPSS0232
BPM: BURPS1710b_A1762(sqs)
BPL: BURPS1106A_A0327
BPD: BURPS668_A0418
BTE: BTH_II2156
BVI: Bcep1808_4828
BUR: Bcep18194_B1749
BCM: Bcenmc03_3255
BCJ: BCAM1397A
BAM: Bamb_3686
BAC: BamMC406_4159
BMU: Bmul_4328
BMJ: BMULJ_04178(fdfT)
BXE: Bxe_B0485
BPH: Bphy_5450
BPY: Bphyt_4026
BGL: bglu_2g21520
PNU: Pnuc_0189
NEU: NE1958(fdfT)
NET: Neut_0403
GBE: GbCGDNIH1_1980
OIH: OB0469
GYM: GYMC10_3503
SSP: SSP1103
LSP: Bsph_2162
ESI: Exig_2456
PJD: Pjdr2_5389
HOR: Hore_15920
BHY: BHWA1_01292
SUS: Acid_1266
FSU: Fisuc_3119
AMU: Amuc_0365
GAU: GAU_0461
EMI: Emin_0169
SYN: sll0513
TEL: tll1096
MAR: MAE_33550
CYT: cce_1843
CYP: PCC8801_0502
CYC: PCC7424_1894
CYN: Cyan7425_4822
CYH: Cyan8802_0519
GVI: glr4058
ANA: alr1805
NPU: Npun_R2917
AVA: Ava_4808
TER: Tery_2043
AMR: AM1_3670
HSL: OE2014F(fdfT)
HMA: rrnAC1477(fdfT)
HWA: HQ2353A(fdfT)
HLA: Hlac_1206
HUT: Huta_0934
HMU: Hmuk_0902
 |
|---|
| Structures |
PDB: 1D8D 1D8E 1EZF 1KZO 1KZP |
|---|
Reference
Authors
Title
Journal
Organism
|
1 [PMID:3805037]
Kuswik-Rabiega G, Rilling HC.
Squalene synthetase. Solubilization and partial purification of
squalene synthetase, copurification of presqualene pyrophosphate and
squalene synthetase activities.
J. Biol. Chem. 262 (1987) 1505-9.
Saccharomyces cerevisiae [GN:sce] |
|---|
Reference
Authors
Title
Journal
Organism
|
2 [PMID:1527001]
Ericsson J, Appelkvist EL, Thelin A, Chojnacki T, Dallner G.
Isoprenoid biosynthesis in rat liver peroxisomes. Characterization
of cis-prenyltransferase and squalene synthetase.
J. Biol. Chem. 267 (1992) 18708-14.
Rattus norvegicus [GN:rno] |
|---|
Reference
Authors
Title
Journal
Organism
|
3 [PMID:11111077]
Tansey TR, Shechter I.
Structure and regulation of mammalian squalene synthase.
Biochim. Biophys. Acta. 1529 (2000) 49-62.
Rattus norvegicus [GN:rno], Homo sapiens [GN:hsa], Arabidopsis
thaliana [GN:ath], Saccharomyces cerevisiae [GN:sce], Neurospora
crassa [GN:dncr] |
|---|
Reference
Authors
Title
Journal
Organism
|
4 [PMID:8239656]
LoGrasso PV, Soltis DA, Boettcher BR.
Overexpression, purification, and kinetic characterization of a
carboxyl-terminal-truncated yeast squalene synthetase.
Arch. Biochem. Biophys. 307 (1993) 193-9.
Saccharomyces cerevisiae [GN:sce] |
|---|
Reference
Authors
Title
Journal
Organism
|
5 [PMID:1569107]
Shechter I, Klinger E, Rucker ML, Engstrom RG, Spirito JA, Islam MA,
Boettcher BR, Weinstein DB.
Solubilization, purification, and characterization of a truncated
form of rat hepatic squalene synthetase.
J. Biol. Chem. 267 (1992) 8628-35.
Rattus norvegicus [GN:rno] |
|---|
Reference
Authors
Title
Journal
Organism
|
6 [PMID:26684]
Agnew WS, Popjak G.
Squalene synthetase. Stoichiometry and kinetics of presqualene
pyrophosphate and squalene synthesis by yeast microsomes.
J. Biol. Chem. 253 (1978) 4566-73.
Homo sapiens [GN:hsa] |
|---|
Reference
Authors
Title
Journal
Organism
|
7 [PMID:10896663]
Pandit J, Danley DE, Schulte GK, Mazzalupo S, Pauly TA, Hayward CM,
Hamanaka ES, Thompson JF, Harwood HJ Jr.
Crystal structure of human squalene synthase. A key enzyme in
cholesterol biosynthesis.
J. Biol. Chem. 275 (2000) 30610-7.
Homo sapiens [GN:hsa] |
|---|
Reference
Authors
Title
Journal
|
8 [PMID:10677224]
Radisky ES, Poulter CD.
Squalene synthase: steady-state, pre-steady-state, and
isotope-trapping studies.
Biochemistry. 39 (2000) 1748-60. |
|---|
| Other DBs |
ExplorEnz - The Enzyme Database: 2.5.1.21
IUBMB Enzyme Nomenclature: 2.5.1.21
ExPASy - ENZYME nomenclature database: 2.5.1.21
BRENDA, the Enzyme Database: 2.5.1.21
CAS: 9077-14-9 |
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