2.5.1.21: squalene synthase
This is an abbreviated version!
For detailed information about squalene synthase, go to the full flat file.
Word Map on EC 2.5.1.21
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2.5.1.21
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farnesylation
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cholesterol
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prenylation
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sterol
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ftase
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mevalonate
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geranylgeranylation
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isoprenoids
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leukemia
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geranylgeranyltransferase
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pyrophosphate
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tipifarnib
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hmg-coa
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statin
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h-ras
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peptidomimetic
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epoxidase
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prenyltransferase
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dolichols
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rhob
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isoprenylation
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triterpene
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farnesol
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3-hydroxy-3-methylglutaryl
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lamins
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ergosterol
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cholesterol-lowering
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hmgcr
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prelamin
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p21ras
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lovastatin
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hutchinson-gilford
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lanosterol
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manumycin
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triterpenoids
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synthesis
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progerin
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farnesylpyrophosphate
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cis-prenyltransferase
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drug development
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oxidosqualene
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ras-transformed
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medicine
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ras-dependent
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nonsterols
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ras-mediated
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withanolides
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srebp-2
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ganoderic
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agriculture
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geranylgeraniol
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industry
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cycloartenol
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non-thiol
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2,3-oxidosqualene
- 2.5.1.21
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farnesylation
- cholesterol
-
prenylation
- sterol
- ftase
- mevalonate
-
geranylgeranylation
-
isoprenoids
- leukemia
-
geranylgeranyltransferase
- pyrophosphate
- tipifarnib
- hmg-coa
- statin
- h-ras
-
peptidomimetic
-
epoxidase
- prenyltransferase
- dolichols
- rhob
-
isoprenylation
-
triterpene
- farnesol
-
3-hydroxy-3-methylglutaryl
- lamins
- ergosterol
-
cholesterol-lowering
- hmgcr
-
prelamin
-
p21ras
- lovastatin
-
hutchinson-gilford
- lanosterol
- manumycin
-
triterpenoids
- synthesis
-
progerin
-
farnesylpyrophosphate
- cis-prenyltransferase
- drug development
- oxidosqualene
-
ras-transformed
- medicine
-
ras-dependent
-
nonsterols
-
ras-mediated
-
withanolides
- srebp-2
-
ganoderic
- agriculture
- geranylgeraniol
- industry
- cycloartenol
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non-thiol
- 2,3-oxidosqualene
Reaction
2 (2E,6E)-farnesyl diphosphate
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Synonyms
BbSS, BSS, CrSQS, dt-ySQase, Erg9, EtSS, farnesyl-diphosphate farnesyltransferase, farnesyl-diphosphate:farnesyldiphosphate farnesyltransferase, farnesyldiphosphate farnesyltransferase 1, farnesyldiphosphate:farnesyldiphosphate farnesyltransferase, farnesyltransferase, FDFT1, hSQS, presqualene synthase, presqualene-diphosphate synthase, SgSQS, SQase, SQS, SQS1, SQS2, squalene synthase, squalene synthase 1, squalene synthase 2, squalene synthetase, SS1, SSase, SSN, synthase, squalene, TkSQS1, TkSQS2
ECTree
2.5.1.21 squalene synthaseAdvanced search results
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results (Engineering
Engineering on EC 2.5.1.21 - squalene synthase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A177N
site-directed mutagenesis, mutant substrate specificity and activity compared to the wild-type
A177N/Q213G
site-directed mutagenesis, mutant substrate specificity and activity compared to the wild-type, the mutant has lost the first reaction step but retains a greater level of the second reaction step for the conversion of presqualene diphosphate to squalene
D220A
site-directed mutagenesis, mutant substrate specificity and activity compared to the wild-type
D224A
site-directed mutagenesis, mutant substrate specificity and activity compared to the wild-type
D79A
site-directed mutagenesis, mutant substrate specificity and activity compared to the wild-type
D83A
site-directed mutagenesis, mutant substrate specificity and activity compared to the wild-type
E223A
site-directed mutagenesis, mutant substrate specificity and activity compared to the wild-type
E82A
site-directed mutagenesis, mutant substrate specificity and activity compared to the wild-type
G207Q
site-directed mutagenesis, mutant substrate specificity and activity compared to the wild-type
N171A
site-directed mutagenesis, mutant substrate specificity and activity compared to the wild-type
Q213G
site-directed mutagenesis, mutant substrate specificity and activity compared to the wild-type
Q213N
site-directed mutagenesis, mutant substrate specificity and activity compared to the wild-type
R219A
site-directed mutagenesis, mutant substrate specificity and activity compared to the wild-type
R76A
site-directed mutagenesis, mutant substrate specificity and activity compared to the wild-type
V176N
site-directed mutagenesis, mutant substrate specificity and activity compared to the wild-type
V176N/A177N
site-directed mutagenesis, mutant substrate specificity and activity compared to the wild-type
Y172A
site-directed mutagenesis, mutant substrate specificity and activity compared to the wild-type
Y172F
site-directed mutagenesis, mutant substrate specificity and activity compared to the wild-type
F288A
site-directed mutagenesis, structure comparison with bound metals and reaction intermediate PSPP compared to the wild-type enzyme
F288L
site-directed mutagenesis, structure comparison with bound metals and reaction intermediate PSPP compared to the wild-type enzyme
K45R
Y73A
site-directed mutagenesis, structure comparison with bound metals and reaction intermediate PSPP compared to the wild-type enzyme
D58E
site-directed mutagenesis of the DXXED motif (S1 site), almost inactive mutant
D58L
site-directed mutagenesis of the DXXED motif (S1 site), almost inactive mutant
D58N
site-directed mutagenesis of the DXXED motif (S1 site), almost inactive mutant
D62E
site-directed mutagenesis of the DXXED motif (S1 site), the mutant shows 85% reduced activity compared to the wild-type
D62L
site-directed mutagenesis of the DXXED motif (S1 site), almost inactive mutant
D62N
site-directed mutagenesis of the DXXED motif (S1 site), almost inactive mutant
E61D
site-directed mutagenesis of the DXXED motif (S1 site), almost inactive mutant
E61L
site-directed mutagenesis of the DXXED motif (S1 site), almost inactive mutant
E61Q
site-directed mutagenesis of the DXXED motif (S1 site), almost inactive mutant
R55H
site-directed mutagenesis of the DXXED motif (S1 site), almost inactive mutant
R55I
site-directed mutagenesis of the DXXED motif (S1 site), inactive mutant
R55K
site-directed mutagenesis of the DXXED motif (S1 site), the mutant shows 96% reduced activity compared to the wild-type
E186K
K45R
synthesis
overexpression of enzyme in Eleutherococcus senticosus, results in enzyme activity up to 3fold higher than wild-type and increase in phytosterols beta-sitosterol and stigmasterol as well as in triterpene saponin levels
additional information
K45R
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single nuceotide polymorphism. Mutation is associated with increased total cholesterol and non-high-density lipoprotein cholesterol. Mutation also influences low-density lipolrotein cholesterol and triglycerides
E186K
site-directed mutagenesis, the engineered enzyme E186K mutant mMaSQSDELTAC17 shows a 3.4fold improvement in catalytic efficiency (kcat/Km) compared to the control
E186K
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site-directed mutagenesis, the engineered enzyme E186K mutant mMaSQSDELTAC17 shows a 3.4fold improvement in catalytic efficiency (kcat/Km) compared to the control
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K45R
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mutation with influence on total cholesterol and non-HDL-C levels
additional information
O23118
expression as fusion protein after replacement of the 69 C-terminal residues of SQS2 by the111 C-terminal residues of the Schizosaccharomyces pombe. Like wild-type, the fusion protein has no catalytic activity
additional information
expression as fusion protein after replacement of the 69 C-terminal residues of SQS2 by the111 C-terminal residues of the Schizosaccharomyces pombe. Like wild-type, the fusion protein has no catalytic activity
additional information
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expression as fusion protein after replacement of the 69 C-terminal residues of SQS2 by the111 C-terminal residues of the Schizosaccharomyces pombe. Like wild-type, the fusion protein has no catalytic activity
additional information
expression in sense and antisense orientation, phenotypes, overview
additional information
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expression in sense and antisense orientation, phenotypes, overview
additional information
heterologous expression of antigenic enzyme from Candida tropicalis in Pichia pastoris can be exploited for large-scale production
additional information
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heterologous expression of antigenic enzyme from Candida tropicalis in Pichia pastoris can be exploited for large-scale production
additional information
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heterologous expression of antigenic enzyme from Candida tropicalis in Pichia pastoris can be exploited for large-scale production
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additional information
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CrSQS-overexpression increases the rate of conversion of 14C-labeled farnesylpyrophosphate into squalene but does not lead to overaccumulation of squalene. Addition of terbinafine causes the accumulation of squalene and suppression of cell survival. In CrSQE-knockdown lines, the expression level of CrSQE is reduced by 59-76% of that in wild-type cells, and significant levels of squalene accumulate without any growth inhibition. In co-transformation lines with CrSQS-overexpression and squalene epoxidase CrSQE-knockdown, the level of squalene is not increased significantly compared with that in solitary CrSQE knockdown lines
additional information
overexpression in Euphorbia tirucalli transgenic callus lines, increased amount of phytosterol
additional information
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overexpression in Euphorbia tirucalli transgenic callus lines, increased amount of phytosterol
additional information
functional complementation Ganoderma lucida squalene synthase in a squalene synthase-deficient strain of Saccharomyces cerevisiae
additional information
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functional complementation Ganoderma lucida squalene synthase in a squalene synthase-deficient strain of Saccharomyces cerevisiae
additional information
deletion of 30 N-terminal amino acids without effect to activity, additional deletion of 81 to 97 C-terminal amino acids abolishes activity, deletion of only 47 C-terminal amino acids retains activity
additional information
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deletion of 30 N-terminal amino acids without effect to activity, additional deletion of 81 to 97 C-terminal amino acids abolishes activity, deletion of only 47 C-terminal amino acids retains activity
additional information
significant truncation of squalene synthase at the C-terminus retains partial cellular activity. Construction of a squalene-producing strain as a convenient platform for gene discovery and the construction of the pathway toward natural and non-natural hopanoids/steroids. Using farnesyl diphosphate as the starting material, squalene is produced by the exogenously expressed squalene synthase, SQS, in Escherichia coli. The production of squalene can be enhanced by overexpressing the rate-limiting steps, enzyme isopentenyl-diphosphate DELTA-isomerase, Idi EC 5.3.3.2, or/and adding an alternative supply route, i.e. the MEV pathway, overview
additional information
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significant truncation of squalene synthase at the C-terminus retains partial cellular activity. Construction of a squalene-producing strain as a convenient platform for gene discovery and the construction of the pathway toward natural and non-natural hopanoids/steroids. Using farnesyl diphosphate as the starting material, squalene is produced by the exogenously expressed squalene synthase, SQS, in Escherichia coli. The production of squalene can be enhanced by overexpressing the rate-limiting steps, enzyme isopentenyl-diphosphate DELTA-isomerase, Idi EC 5.3.3.2, or/and adding an alternative supply route, i.e. the MEV pathway, overview
additional information
various mutations clustered around the residues that are important for NADPH binding effectively convert SQS into a dehydrosqualene synthase, overview
additional information
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various mutations clustered around the residues that are important for NADPH binding effectively convert SQS into a dehydrosqualene synthase, overview
additional information
construction of a soluble functional transmembrane domain-deleted (385-409 aa) MoSQS mutant (MoSQSDELTATM)
additional information
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construction of a soluble functional transmembrane domain-deleted (385-409 aa) MoSQS mutant (MoSQSDELTATM)
additional information
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point mutations in conserved regions A, B, C indicate that Tyr171, Asp219, Asp223 are essential for activity and Phe288 may be involved in second step of catalysis
additional information
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downregulation of expression by replacing its native promoter with the methionine-repressible MET3 promoter. Under certain culture conditions amorphadiene production increases fivefold upon ERG9 repression. With increasing flux to amorphadiene, squalene and ergosterol production each decrease. The levels of these three metabolites are dependent not only upon the level of ERG9 repression, but also the timing of its repression relative to the induction of amorphadiene synthase and genes responsible for enhancing flux to farnesyl diphosphate
additional information
construction of a mutant containing three synonymous mutations G1125A, T1128C, T1176C and one nonsynonymous mutation G856A, which corresponds to Gly286Ser exchange, by gene replacement. Various mutations clustered around the residues that are important for NADPH binding effectively convert SQS into a dehydrosqualene synthase, overview
additional information
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construction of a mutant containing three synonymous mutations G1125A, T1128C, T1176C and one nonsynonymous mutation G856A, which corresponds to Gly286Ser exchange, by gene replacement. Various mutations clustered around the residues that are important for NADPH binding effectively convert SQS into a dehydrosqualene synthase, overview
additional information
Thermosynechococcus vestitus
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significant truncation of squalene synthase at the C-terminus retains partial cellular activity. Construction of a squalene-producing strain as a convenient platform for gene discovery and the construction of the pathway toward natural and non-natural hopanoids/steroids. Using farnesyl diphosphate as the starting material, squalene is produced by the exogenously expressed squalene synthase, SQS, in Escherichia coli. The production of squalene can be enhanced by overexpressing the rate-limiting steps, enzyme isopentenyl-diphosphate DELTA-isomerase, Idi EC 5.3.3.2, or/and adding an alternative supply route, i.e. the MEV pathway, overview
additional information
Thermosynechococcus vestitus
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various mutations clustered around the residues that are important for NADPH binding effectively convert SQS into a dehydrosqualene synthase, overview
additional information
total withanolide content of enzyme overexpressing plants, WsSQS T0 transformed plants, and tissue distribution, overview
