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(2E,6E)-3,7,10-trimethylundeca-2,6-dienyl diphosphate + NADPH
diphosphate + ?
-
weak
-
-
?
(2E,6E)-3,7,11-trimethyldodeca-2,6-dienyl diphosphate + NADPH
diphosphate + ?
-
-
-
-
?
(2E,6E)-3,7,12-trimethyltrideca-2,6-dienyl diphosphate + NADPH
diphosphate + ?
-
weak
-
-
?
(2E,6E)-3,7-dimethyldodeca-2,6-dienyl diphosphate + NADPH
diphosphate + ?
-
-
-
-
?
(2E,6E)-3,7-dimethyltetradeca-2,6-dienyl diphosphate + NADPH
diphosphate + ?
-
weak
-
-
?
(2E,6E)-3,7-dimethyltrideca-2,6-dienyl diphosphate + NADPH
diphosphate + ?
-
weak
-
-
?
(2E,6E)-3,7-dimethylundeca-2,6-dienyl diphosphate + NADPH
diphosphate + ?
-
weak
-
-
?
(2E,6E)-farnesyl diphosphate + NADH + H+
squalene + diphosphate + NAD+
-
-
-
-
?
(2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + diphosphate + NADP+
-
-
-
-
?
(E,E)-7-desmethylfarnesyl diphosphate + NADPH
6,19-didesmethylsqualene + NADP+ + diphosphate
-
at 60% of the efficiency that farnesyl diphosphate is converted to squalene
in absence of farnesyl diphosphate, 6-desmethylsqualene is produced in presence of farnesyl diphosphate
?
10,11-dihydrofarnesyl diphosphate + NADPH
2,3,22,23-tetrahydrosqualene + NADP+ + diphosphate
-
at 60% of the efficiency that farnesyl diphosphate is converted to squalene
-
?
2 (2E,6E)-farnesyl diphosphate
diphosphate + presqualene diphosphate
2 (2E,6E)-farnesyl diphosphate + NAD(P)H + H+
squalene + 2 diphosphate + NAD(P)+
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
2 farnesyl diphosphate
presqualene diphosphate + diphosphate
2 farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
-
-
?
2-methylfarnesyl diphosphate + NADPH
11-methylsqualene + NADP+ + diphosphate
3-demethylfarnesyl diphosphate + NADPH
10-demethylsqualene + NADP+ + diphosphate
farnesyl diphosphate
12,13-cis-dehydrosqualene + diphosphate
farnesyl diphosphate + farnesyl diphosphate
diphosphate + presqualene diphosphate
farnesyl diphosphate + NAD(P)H
squalene + diphosphate + NAD(P)+
farnesyl diphosphate + NAD(P)H + H+
squalene + diphosphate + NAD(P)+
farnesyl diphosphate + NADPH + H+
squalene + diphosphate + NADP+
Thermosynechococcus vestitus
-
-
sole product
-
?
presqualene diphosphate + NAD(P)H
squalene + NAD(P)+ + diphosphate
presqualene diphosphate + NAD(P)H + H+
squalene + diphosphate + NAD(P)+
presqualene diphosphate + NADPH + H+
squalene + diphosphate + NADP+
additional information
?
-
2 (2E,6E)-farnesyl diphosphate
diphosphate + presqualene diphosphate
-
-
-
-
?
2 (2E,6E)-farnesyl diphosphate
diphosphate + presqualene diphosphate
first half-reaction
-
-
?
2 (2E,6E)-farnesyl diphosphate
diphosphate + presqualene diphosphate
first reaction
-
-
?
2 (2E,6E)-farnesyl diphosphate
diphosphate + presqualene diphosphate
first reaction
-
-
?
2 (2E,6E)-farnesyl diphosphate
diphosphate + presqualene diphosphate
-
-
-
?
2 (2E,6E)-farnesyl diphosphate + NAD(P)H + H+
squalene + 2 diphosphate + NAD(P)+
-
-
-
-
?
2 (2E,6E)-farnesyl diphosphate + NAD(P)H + H+
squalene + 2 diphosphate + NAD(P)+
-
overall reaction
-
-
?
2 (2E,6E)-farnesyl diphosphate + NAD(P)H + H+
squalene + 2 diphosphate + NAD(P)+
-
-
-
?
2 (2E,6E)-farnesyl diphosphate + NAD(P)H + H+
squalene + 2 diphosphate + NAD(P)+
overall reaction
-
-
?
2 (2E,6E)-farnesyl diphosphate + NAD(P)H + H+
squalene + 2 diphosphate + NAD(P)+
-
-
-
?
2 (2E,6E)-farnesyl diphosphate + NAD(P)H + H+
squalene + 2 diphosphate + NAD(P)+
overall reaction
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
overall reaction
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
overall reaction
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
the enzyme initially catalyzes the condensation of two molecules of farnesyl diphosphate (FPP) to form presqualene diphosphate (PSPP), and next converting PSPP to squalene in a reaction requiring NADPH and Mg2+
product analysis by GC-MS analysis
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
-
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
-
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
overall reaction
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
overall reaction, the enzyme catalyzes the two-step reductive head-to-head condensation of two molecules of farnesyl pyrophosphate to form squalene using presqualene diphosphate (PSPP) as an intermediate
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
overall reaction
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
overall reaction
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
specific for, the enzyme catalyzes a head-to-head condensation reaction (1'-2,3-linked) between two molecules of farnesyl diphosphate (C15) forms a cyclopropylcarbinyl intermediate, presqualene diphosphate. The subsequent conversion of presqualene diphosphate to squalene involves an extensive rearrangement of the carbon skeleton and an NADPH-dependent reduction reaction
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
overall reaction
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
squalene synthase catalyzes the first enzymatic step from the central isoprenoid pathway toward sterol and triterpenoid biosynthesis
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
farnesyl diphosphate forms hydrogen bonds with enzyme residues Arg49, Arg74, Ser48, and Val47 of conserved 77DTVED81 motif
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
farnesyl diphosphate forms hydrogen bonds with enzyme residues Asp81, Asp217, Glu80, and Gln206 of conserved 77DTVED81 and 213DYLED217 motifs
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
overall reaction
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
the enzyme catalyzes the first dedicated step in the biosynthesis of sterols and other triterpenoids
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
overall reaction
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
overall reaction
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
Thermosynechococcus vestitus
-
-
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
overall reaction
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
the enzyme is involved in celastrol biosynthesis
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
overall reaction
-
-
?
2 farnesyl diphosphate
presqualene diphosphate + diphosphate
-
-
-
-
?
2 farnesyl diphosphate
presqualene diphosphate + diphosphate
-
-
-
?
2 farnesyl diphosphate
presqualene diphosphate + diphosphate
-
-
-
-
?
2 farnesyl diphosphate
presqualene diphosphate + diphosphate
-
-
-
-
?
2 farnesyl diphosphate
presqualene diphosphate + diphosphate
-
-
-
-
?
2 farnesyl diphosphate
presqualene diphosphate + diphosphate
-
-
-
-
?
2 farnesyl diphosphate
presqualene diphosphate + diphosphate
-
-
-
-
?
2 farnesyl diphosphate
presqualene diphosphate + diphosphate
-
assay at pH 7.2, 30°C, 3 h
-
-
?
2 farnesyl diphosphate
presqualene diphosphate + diphosphate
Thermosynechococcus vestitus
-
-
in absence of NADPH, formation of presqualene diphosphate
-
?
2-methylfarnesyl diphosphate + NADPH
11-methylsqualene + NADP+ + diphosphate
-
-
-
?
2-methylfarnesyl diphosphate + NADPH
11-methylsqualene + NADP+ + diphosphate
-
-
-
?
3-demethylfarnesyl diphosphate + NADPH
10-demethylsqualene + NADP+ + diphosphate
-
-
-
?
3-demethylfarnesyl diphosphate + NADPH
10-demethylsqualene + NADP+ + diphosphate
-
-
-
?
farnesyl diphosphate
12,13-cis-dehydrosqualene + diphosphate
-
-
-
?
farnesyl diphosphate
12,13-cis-dehydrosqualene + diphosphate
-
in presence of Mn2+
12-cis-dehydrosqualene + diphosphate
?
farnesyl diphosphate
12,13-cis-dehydrosqualene + diphosphate
-
-
-
?
farnesyl diphosphate + farnesyl diphosphate
diphosphate + presqualene diphosphate
-
-
-
-
?
farnesyl diphosphate + farnesyl diphosphate
diphosphate + presqualene diphosphate
-
-
-
?
farnesyl diphosphate + farnesyl diphosphate
diphosphate + presqualene diphosphate
-
enzyme may be important during response to infection and inflammation
-
-
?
farnesyl diphosphate + farnesyl diphosphate
diphosphate + presqualene diphosphate
-
first pathway-specific enzyme in cholesterol biosynthesis
-
-
?
farnesyl diphosphate + farnesyl diphosphate
diphosphate + presqualene diphosphate
-
-
-
?
farnesyl diphosphate + farnesyl diphosphate
diphosphate + presqualene diphosphate
-
-
-
?
farnesyl diphosphate + farnesyl diphosphate
diphosphate + presqualene diphosphate
-
squalene is the first sterol intermediate in cholesterol biosynthesis
-
-
?
farnesyl diphosphate + farnesyl diphosphate
diphosphate + presqualene diphosphate
-
enzyme may be important during response to infection and inflammation
-
-
?
farnesyl diphosphate + farnesyl diphosphate
diphosphate + presqualene diphosphate
-
-
-
?
farnesyl diphosphate + farnesyl diphosphate
diphosphate + presqualene diphosphate
-
-
-
?
farnesyl diphosphate + farnesyl diphosphate
diphosphate + presqualene diphosphate
-
-
-
?
farnesyl diphosphate + farnesyl diphosphate
diphosphate + presqualene diphosphate
-
-
-
?
farnesyl diphosphate + farnesyl diphosphate
diphosphate + presqualene diphosphate
-
-
-
?
farnesyl diphosphate + farnesyl diphosphate
diphosphate + presqualene diphosphate
-
-
-
?
farnesyl diphosphate + farnesyl diphosphate
diphosphate + presqualene diphosphate
-
-
-
?
farnesyl diphosphate + farnesyl diphosphate
diphosphate + presqualene diphosphate
-
-
-
?
farnesyl diphosphate + farnesyl diphosphate
diphosphate + presqualene diphosphate
-
-
-
-
?
farnesyl diphosphate + farnesyl diphosphate
diphosphate + presqualene diphosphate
-
first pathway-specific enzyme in cholesterol biosynthesis
-
-
?
farnesyl diphosphate + farnesyl diphosphate
diphosphate + presqualene diphosphate
-
essential enzyme in cholesterol biosynthetic pathway
-
-
?
farnesyl diphosphate + NAD(P)H
squalene + diphosphate + NAD(P)+
-
-
-
?
farnesyl diphosphate + NAD(P)H
squalene + diphosphate + NAD(P)+
-
-
-
?
farnesyl diphosphate + NAD(P)H
squalene + diphosphate + NAD(P)+
-
-
-
?
farnesyl diphosphate + NAD(P)H
squalene + diphosphate + NAD(P)+
-
-
-
?
farnesyl diphosphate + NAD(P)H
squalene + diphosphate + NAD(P)+
-
-
-
?
farnesyl diphosphate + NAD(P)H
squalene + diphosphate + NAD(P)+
-
-
-
?
farnesyl diphosphate + NAD(P)H
squalene + diphosphate + NAD(P)+
-
-
-
?
farnesyl diphosphate + NAD(P)H
squalene + diphosphate + NAD(P)+
-
-
-
?
farnesyl diphosphate + NAD(P)H
squalene + diphosphate + NAD(P)+
-
-
-
?
farnesyl diphosphate + NAD(P)H
squalene + diphosphate + NAD(P)+
-
-
-
?
farnesyl diphosphate + NAD(P)H
squalene + diphosphate + NAD(P)+
-
-
-
?
farnesyl diphosphate + NAD(P)H
squalene + diphosphate + NAD(P)+
-
-
-
?
farnesyl diphosphate + NAD(P)H
squalene + diphosphate + NAD(P)+
-
-
presqualene diphosphate and squalene are produced in a ratio of 6:1
?
farnesyl diphosphate + NAD(P)H
squalene + diphosphate + NAD(P)+
-
-
-
?
farnesyl diphosphate + NAD(P)H + H+
squalene + diphosphate + NAD(P)+
-
-
-
-
?
farnesyl diphosphate + NAD(P)H + H+
squalene + diphosphate + NAD(P)+
-
-
-
-
?
presqualene diphosphate + NAD(P)H
squalene + NAD(P)+ + diphosphate
-
-
-
?
presqualene diphosphate + NAD(P)H
squalene + NAD(P)+ + diphosphate
-
in presence of reducing pyridine nucleotide, preferably NADPH, squalene is formed, in absence of reducing cofactor the rate of the condensation reaction is lower and all of the product accumulates as presqualene diphosphate
-
-
?
presqualene diphosphate + NAD(P)H
squalene + NAD(P)+ + diphosphate
-
-
-
?
presqualene diphosphate + NAD(P)H
squalene + NAD(P)+ + diphosphate
-
-
-
?
presqualene diphosphate + NAD(P)H
squalene + NAD(P)+ + diphosphate
-
-
-
?
presqualene diphosphate + NAD(P)H
squalene + NAD(P)+ + diphosphate
-
in presence of reducing pyridine nucleotide, preferably NADPH, squalene is formed, in absence of reducing cofactor the rate of the condensation reaction is lower and all of the product accumulates as presqualene diphosphate
-
?
presqualene diphosphate + NAD(P)H
squalene + NAD(P)+ + diphosphate
-
in presence of reducing pyridine nucleotide, preferably NADPH, squalene is formed, in absence of reducing cofactor the rate of the condensation reaction is lower and all of the product accumulates as presqualene diphosphate
-
?
presqualene diphosphate + NAD(P)H
squalene + NAD(P)+ + diphosphate
-
presqualene diphosphate synthetase and squalene synthetase are copurified during isolation
-
?
presqualene diphosphate + NAD(P)H
squalene + NAD(P)+ + diphosphate
-
a single active site catalyzes both reactions
-
?
presqualene diphosphate + NAD(P)H
squalene + NAD(P)+ + diphosphate
-
one protein with 2 catalytic sites may be involved in synthesis of presqualene diphosphate and for its reduction to squalene
-
-
?
presqualene diphosphate + NAD(P)H
squalene + NAD(P)+ + diphosphate
-
the polymeric form of the enzyme also catalyzes the reduction of presqualene diphosphate by NADPH to squalene
-
-
?
presqualene diphosphate + NAD(P)H
squalene + NAD(P)+ + diphosphate
-
in presence of reducing pyridine nucleotide, preferably NADPH, squalene is formed, in absence of reducing cofactor the rate of the condensation reaction is lower and all of the product accumulates as presqualene diphosphate
-
?
presqualene diphosphate + NAD(P)H + H+
squalene + diphosphate + NAD(P)+
-
-
-
-
?
presqualene diphosphate + NAD(P)H + H+
squalene + diphosphate + NAD(P)+
-
-
-
?
presqualene diphosphate + NAD(P)H + H+
squalene + diphosphate + NAD(P)+
-
-
-
-
?
presqualene diphosphate + NAD(P)H + H+
squalene + diphosphate + NAD(P)+
-
-
-
-
?
presqualene diphosphate + NAD(P)H + H+
squalene + diphosphate + NAD(P)+
-
-
-
-
?
presqualene diphosphate + NAD(P)H + H+
squalene + diphosphate + NAD(P)+
second reaction
-
-
?
presqualene diphosphate + NAD(P)H + H+
squalene + diphosphate + NAD(P)+
second reaction
-
-
?
presqualene diphosphate + NAD(P)H + H+
squalene + diphosphate + NAD(P)+
-
-
-
-
?
presqualene diphosphate + NADPH + H+
squalene + diphosphate + NADP+
-
-
-
?
presqualene diphosphate + NADPH + H+
squalene + diphosphate + NADP+
-
-
-
-
?
presqualene diphosphate + NADPH + H+
squalene + diphosphate + NADP+
second half reaction
-
-
?
presqualene diphosphate + NADPH + H+
squalene + diphosphate + NADP+
-
-
-
-
?
presqualene diphosphate + NADPH + H+
squalene + diphosphate + NADP+
-
-
-
?
additional information
?
-
squalene and botryococcene are branched-chain, triterpene compounds that arise from the head-to-head condensation of two molecules of farnesyl diphosphate to yield 1'-1 and 1'-3 linkages, respectively. Different enzymes are responsible for botryococcene and squalene biosynthesis in the green alga Botryococcus braunii race B. The specificity for the 1'-1 and 1'-3 linkages is controlled by residues in the active sites that can mediate catalytic specificity. Identification of several amino acid positions contributing to the rearrangement of the cyclopropyl intermediate to squalene, The same positions do not appear to be sufficient to account for the cyclopropyl rearrangement to give botryococcene, oerview
-
-
?
additional information
?
-
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squalene and botryococcene are branched-chain, triterpene compounds that arise from the head-to-head condensation of two molecules of farnesyl diphosphate to yield 1'-1 and 1'-3 linkages, respectively. Different enzymes are responsible for botryococcene and squalene biosynthesis in the green alga Botryococcus braunii race B. The specificity for the 1'-1 and 1'-3 linkages is controlled by residues in the active sites that can mediate catalytic specificity. Identification of several amino acid positions contributing to the rearrangement of the cyclopropyl intermediate to squalene, The same positions do not appear to be sufficient to account for the cyclopropyl rearrangement to give botryococcene, oerview
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additional information
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analysis of substrate specificity, overview
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additional information
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analysis of substrate specificity, overview
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additional information
?
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the catalytic process involves two reactions: firstly, two FPP molecules are condensed to form presqualene diphosphate (PSPP), an intermediate with a cyclopropane C1'-C2-C3 ring structure, and secondly, PSPP undergoes a NADPH-dependent rearrangement and reduction to generate the end product squalene
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additional information
?
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the catalytic process involves two reactions: firstly, two FPP molecules are condensed to form presqualene diphosphate (PSPP), an intermediate with a cyclopropane C1'-C2-C3 ring structure, and secondly, PSPP undergoes a NADPH-dependent rearrangement and reduction to generate the end product squalene
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additional information
?
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catalytic mechanism, overview
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additional information
?
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catalytic mechanism, overview
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additional information
?
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enzyme is key regulator not only for phytosterol but also for triterpene biosynthesis
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additional information
?
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enzyme is key regulator not only for phytosterol but also for triterpene biosynthesis
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additional information
?
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specificity overview
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additional information
?
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none of the following analogues gives nonpolar products: 7,11-dimethyl-3-ethyl-2,6,10-dodecatrienyl diphosphate, 6,7,10,11-tetrahydrofarnesyl diphosphate, 4-methylthiofarnesyl diphosphate, 4-fluorofarnesyl diphosphate
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additional information
?
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specificity overview
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additional information
?
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specificity overview
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additional information
?
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none of the following analogues gives nonpolar products: 7,11-dimethyl-3-ethyl-2,6,10-dodecatrienyl diphosphate, 6,7,10,11-tetrahydrofarnesyl diphosphate, 4-methylthiofarnesyl diphosphate, 4-fluorofarnesyl diphosphate
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additional information
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reaction is completely regioselective
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additional information
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no substrate: 6,7-dihydrofarnesyl diphosphate, 3-desmethylfarnesyl diphosphate
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additional information
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not metabolized: (E)-6,7,10,11-tetrahydrofarnesyl diphosphate
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additional information
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specificity overview
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additional information
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replacement of 3-methyl of farnesyl diphosphate by an ethyl group or introduction of a methyl group at C-4 results in a complete loss of activity
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 (2E,6E)-farnesyl diphosphate
diphosphate + presqualene diphosphate
2 (2E,6E)-farnesyl diphosphate + NAD(P)H + H+
squalene + 2 diphosphate + NAD(P)+
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
2 farnesyl diphosphate
presqualene diphosphate + diphosphate
2 farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
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?
farnesyl diphosphate + farnesyl diphosphate
diphosphate + presqualene diphosphate
presqualene diphosphate + NAD(P)H + H+
squalene + diphosphate + NAD(P)+
presqualene diphosphate + NADPH + H+
squalene + diphosphate + NADP+
additional information
?
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2 (2E,6E)-farnesyl diphosphate
diphosphate + presqualene diphosphate
first half-reaction
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?
2 (2E,6E)-farnesyl diphosphate
diphosphate + presqualene diphosphate
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?
2 (2E,6E)-farnesyl diphosphate + NAD(P)H + H+
squalene + 2 diphosphate + NAD(P)+
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?
2 (2E,6E)-farnesyl diphosphate + NAD(P)H + H+
squalene + 2 diphosphate + NAD(P)+
-
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?
2 (2E,6E)-farnesyl diphosphate + NAD(P)H + H+
squalene + 2 diphosphate + NAD(P)+
-
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?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
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?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
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?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
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?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
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?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
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?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
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?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
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?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
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?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
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?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
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?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
overall reaction
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?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
overall reaction
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?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
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?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
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?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
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?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
squalene synthase catalyzes the first enzymatic step from the central isoprenoid pathway toward sterol and triterpenoid biosynthesis
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2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
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?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
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?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
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2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
the enzyme catalyzes the first dedicated step in the biosynthesis of sterols and other triterpenoids
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2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
overall reaction
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?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
overall reaction
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2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
Thermosynechococcus vestitus
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2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
the enzyme is involved in celastrol biosynthesis
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2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
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?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
overall reaction
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?
2 farnesyl diphosphate
presqualene diphosphate + diphosphate
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?
2 farnesyl diphosphate
presqualene diphosphate + diphosphate
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?
2 farnesyl diphosphate
presqualene diphosphate + diphosphate
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?
2 farnesyl diphosphate
presqualene diphosphate + diphosphate
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?
2 farnesyl diphosphate
presqualene diphosphate + diphosphate
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?
2 farnesyl diphosphate
presqualene diphosphate + diphosphate
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?
farnesyl diphosphate + farnesyl diphosphate
diphosphate + presqualene diphosphate
-
enzyme may be important during response to infection and inflammation
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farnesyl diphosphate + farnesyl diphosphate
diphosphate + presqualene diphosphate
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first pathway-specific enzyme in cholesterol biosynthesis
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?
farnesyl diphosphate + farnesyl diphosphate
diphosphate + presqualene diphosphate
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squalene is the first sterol intermediate in cholesterol biosynthesis
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farnesyl diphosphate + farnesyl diphosphate
diphosphate + presqualene diphosphate
-
enzyme may be important during response to infection and inflammation
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farnesyl diphosphate + farnesyl diphosphate
diphosphate + presqualene diphosphate
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farnesyl diphosphate + farnesyl diphosphate
diphosphate + presqualene diphosphate
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first pathway-specific enzyme in cholesterol biosynthesis
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farnesyl diphosphate + farnesyl diphosphate
diphosphate + presqualene diphosphate
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essential enzyme in cholesterol biosynthetic pathway
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presqualene diphosphate + NAD(P)H + H+
squalene + diphosphate + NAD(P)+
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presqualene diphosphate + NAD(P)H + H+
squalene + diphosphate + NAD(P)+
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?
presqualene diphosphate + NAD(P)H + H+
squalene + diphosphate + NAD(P)+
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?
presqualene diphosphate + NAD(P)H + H+
squalene + diphosphate + NAD(P)+
-
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?
presqualene diphosphate + NAD(P)H + H+
squalene + diphosphate + NAD(P)+
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presqualene diphosphate + NADPH + H+
squalene + diphosphate + NADP+
second half reaction
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presqualene diphosphate + NADPH + H+
squalene + diphosphate + NADP+
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?
presqualene diphosphate + NADPH + H+
squalene + diphosphate + NADP+
-
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?
additional information
?
-
squalene and botryococcene are branched-chain, triterpene compounds that arise from the head-to-head condensation of two molecules of farnesyl diphosphate to yield 1'-1 and 1'-3 linkages, respectively. Different enzymes are responsible for botryococcene and squalene biosynthesis in the green alga Botryococcus braunii race B. The specificity for the 1'-1 and 1'-3 linkages is controlled by residues in the active sites that can mediate catalytic specificity. Identification of several amino acid positions contributing to the rearrangement of the cyclopropyl intermediate to squalene, The same positions do not appear to be sufficient to account for the cyclopropyl rearrangement to give botryococcene, oerview
-
-
?
additional information
?
-
-
squalene and botryococcene are branched-chain, triterpene compounds that arise from the head-to-head condensation of two molecules of farnesyl diphosphate to yield 1'-1 and 1'-3 linkages, respectively. Different enzymes are responsible for botryococcene and squalene biosynthesis in the green alga Botryococcus braunii race B. The specificity for the 1'-1 and 1'-3 linkages is controlled by residues in the active sites that can mediate catalytic specificity. Identification of several amino acid positions contributing to the rearrangement of the cyclopropyl intermediate to squalene, The same positions do not appear to be sufficient to account for the cyclopropyl rearrangement to give botryococcene, oerview
-
-
?
additional information
?
-
the catalytic process involves two reactions: firstly, two FPP molecules are condensed to form presqualene diphosphate (PSPP), an intermediate with a cyclopropane C1'-C2-C3 ring structure, and secondly, PSPP undergoes a NADPH-dependent rearrangement and reduction to generate the end product squalene
-
-
?
additional information
?
-
-
the catalytic process involves two reactions: firstly, two FPP molecules are condensed to form presqualene diphosphate (PSPP), an intermediate with a cyclopropane C1'-C2-C3 ring structure, and secondly, PSPP undergoes a NADPH-dependent rearrangement and reduction to generate the end product squalene
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?
additional information
?
-
enzyme is key regulator not only for phytosterol but also for triterpene biosynthesis
-
-
?
additional information
?
-
-
enzyme is key regulator not only for phytosterol but also for triterpene biosynthesis
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(1-[[(1R,5S)-7-chloro-5-(2-chlorophenyl)-1-(2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetyl]piperidin-4-yl)acetic acid
-
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(1-[[(3R,5S)-1-[3-(acetyloxy)-2,2-dimethylpropyl]-7-chloro-5-(2,3-dimethoxyphenyl)-2-oxo-1,2,3,5-tetrahydro-4,1-benzoxazepin-3-yl]acetyl]piperidin-4-yl)acetic acid
(1-[[(3R,5S)-7-chloro-5-(2,3-dimethoxyphenyl)-1-(3-hydroxy-2,2-dimethylpropyl)-2-oxo-1,2,3,5-tetrahydro-4,1-benzoxazepin-3-yl]acetyl]piperidin-4-yl)acetic acid
-
-
(1-[[(6S)-8-chloro-6-(2,3-dimethoxyphenyl)-1-(propan-2-yl)-6,10b-dihydro-1H,4H-[2]benzoxepino[4,5-c][1,2]oxazol-4-yl]acetyl]piperidin-4-yl)acetic acid
-
-
(1R,5S)-7-chloro-5-(2-methoxyphenyl)-1-(2-methylpropyl)-3-[2-oxo-2-(piperidin-1-yl)ethyl]-1,3,4,5-tetrahydro-2H-3-benzazepin-2-one
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-
(2E)-3-[(1R,5S)-3-(carboxymethyl)-7-chloro-5-(2-chlorophenyl)-2-oxo-2,3,4,5-tetrahydro-1H-3-benzazepin-1-yl]-2-methylprop-2-enoic acid
-
-
(3R)-3-[[3-(benzyloxy)phenyl]ethynyl]-1-azabicyclo[2.2.2]octan-3-ol
-
IC50: 1500 nM
(3S)-1-(3-((4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl)propanoyl)-3-piperidine carboxylic acid
-
-
(3S)-1-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetyl]-3-piperidinecarboxylic acid
-
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1,3-diallyl-2-[3-(isopropylamino)propoxy]-9H-carbazole
-
50% inhibition at 250 nM
1-(2-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]ethyl]-2H-1,2,3,4-tetrazol-5-yl)cyclopropanecarboxylic acid
-
-
1-(3-((4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl)propanoyl)-3-azetidine carboxylic acid
-
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1-allyl-2-(3-anilinopropoxy)-9H-carbazole
-
50% inhibition at above 0.001 mM nM
1-allyl-2-[3-(benzylamino)propoxy]-9H-carbazole
-
50% inhibition at 63 nM
1-allyl-2-[3-(benzylamino)propoxy]-9H-carbazole hydrochloride
-
50% inhibition at 150 nM
1-allyl-2-[3-(cyclohexylamino)propoxy]-9H-carbazole
-
50% inhibition at 310 nM
1-allyl-2-[3-(cyclopropylamino)propoxy]-9H-carbazole
-
50% inhibition at 230 nM
1-allyl-2-[3-(isobutylamino)propoxy]-9H-carbazole
-
50% inhibition at 400 nM
1-allyl-2-[3-(isopropylamino)propoxy]-9H-carbazole
1-allyl-2-[3-(isopropylamino)propoxy]-9H-xanthen-9-one
1-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetyl]-4-piperidinecarboxylic acid
-
-
1-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]ethyl]-1H-1,2,3-triazole-4-carboxylic acid
-
-
1-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]ethyl]-1H-pyrazole-4-carboxylic acid
-
-
1-[[(1R,5R)-7-chloro-5-(2,3-dimethoxyphenyl)-1-(2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetyl]piperidine-4-carboxylic acid
-
-
1-[[(1R,5S)-7-chloro-5-(2,3-dimethoxyphenyl)-1-(2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetyl]piperidine-4-carboxylic acid
-
-
1-[[(1R,5S)-7-chloro-5-(2-chlorophenyl)-1-(2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetyl]piperidine-4-carboxylic acid
-
-
1-[[(1R,5S)-7-chloro-5-(2-methoxyphenyl)-1-(2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetyl]piperidine-4-carboxylic acid
-
-
1-[[(1S,5S)-7-chloro-5-(2,3-dimethoxyphenyl)-1-(2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetyl]piperidine-4-carboxylic acid
-
-
1-[[(6S)-8-chloro-6-(2,3-dimethoxyphenyl)-1-(propan-2-yl)-6,10b-dihydro-1H,4H-[2]benzoxepino[4,5-c][1,2]oxazol-4-yl]acetyl]piperidine-4-carboxylic acid
-
-
11,12-di-O-methylcarnosol
-
11,12-diacetyl-carnosol
-
2-(1-(3-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]propanoyl)-3-azetidinyl)acetic acid
-
-
2-(1-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetyl]-4-piperidinyl)acetic acid
-
-
2-(1-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]ethyl]-1H-1,2,3-triazol-4-yl)acetic acid
-
-
2-(1-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]ethyl]-1H-1,2,3-triazol-5-yl)acetic acid
-
-
2-(1-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]ethyl]-1H-pyrazol-3-yl)acetic acid
-
-
2-(1-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]ethyl]-1H-pyrazol-4-yl)acetic acid
-
-
2-(1-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]ethyl]-1H-pyrazol-5-yl)acetic acid
-
-
2-(1-[2-[(4S,6R)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetyl]-4-piperidinyl)acetic acid
-
-
2-(1-[2-[8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetyl]-4-piperidinyl)acetic acid
-
-
2-(1-[3-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]propanoyl]-4-piperidinyl)acetic acid
-
-
2-(2-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl)ethyl]-2H-1,2,3,4-tetrazol-5-yl]-2-methylpropanoic acid
-
-
2-(2-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl)ethyl]-2H-1,2,3,4-tetrazol-5-yl]acetic acid
-
-
2-(2-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]ethyl]-1H-1,2,3,4-tetrazol-5-yl)acetic acid
-
-
2-(4-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetyl]-1-piperazinyl)acetic acid
-
-
2-(4-[3-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]propanoyl]-2-oxo-1-piperazinyl)acetic acid
-
-
2-(trans-4-stilbenyl)-4-methyl-morpholin-2-ol
-
2-([2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetyl]amino)acetic acid
-
-
2-[(1-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]ethyl]-1H-1,2,3-triazol-4-yl)methoxy]-2-ethylbutanoic acid
-
-
2-[(1-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]ethyl]-1H-1,2,3-triazol-4-yl)methoxy]-2-methylpropanoic acid
-
-
2-[(1-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]ethyl]-1H-1,2,3-triazol-4-yl)methoxy]acetic acid
-
-
2-[(1-[3-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]propanoyl]-4-piperidinyl)methoxy]acetic acid
-
-
2-[(1-[3-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]propanoyl]-4-piperidinyl)oxy]acetic acid
-
-
2-[(2-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]ethyl]-2H-1,2,3,4-tetrazol-5-yl)methoxy]-2-methylpropanoic acid
-
-
2-[(6S)-8-chloro-6-(2,3-dimethoxyphenyl)-1-(propan-2-yl)-6,10b-dihydro-1H,4H-[2]benzoxepino[4,5-c][1,2]oxazol-4-yl]-1-[(3R)-3-hydroxypyrrolidin-1-yl]ethanone
-
-
2-[1,8-dichloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetic acid
-
-
2-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]ethyl]-2H-1,2,3,4-tetrazol-5-carboxylic acid
-
-
2-[3-(isopropylamino)propoxy]-1-ethyl-9H-carbazole
-
50% inhibition at 460 nM
2-[3-(isopropylamino)propoxy]-9H-carbazole
2-[8-chloro-6-(1-naphthyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetic acid
-
-
2-[8-chloro-6-(2,3-dichlorobenzoyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetic acid
-
-
2-[8-chloro-6-(2,3-dihydro-1,4-benzodioxin-5-yl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetic acid
-
-
2-[8-chloro-6-(2,3-dimethoxyphenyl)-1-(4-morpholinylmethyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetic acid
-
-
2-[8-chloro-6-(2,3-dimethoxyphenyl)-1-[(dimethylamino)methyl]-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetic acid
-
-
2-[8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetic acid
-
-
2-[[(2Z)-2-(1-azabicyclo(2.2.2)oct-3-ylidene)-2-fluoroethyl]oxy]-9H-carbazole
-
i.e. YM-53601, 50% inhibition at 90 nM
3-(2-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]ethyl]-2H-1,2,3,4-tetrazol-5-yl)propanoic acid
-
-
3-(4-quinolin-6-ylphenyl)quinuclidin-3-ol
3-(biphenyl-4-yl)-2,3-dehydroquinuclidine
-
50% inhibition at 243 nM
3-(biphenyl-4-yl)-3-hydroxyquinuclidine
-
50% inhibition at 13 nM
3-(biphenyl-4-yl)-4'[(t-butyldimethylsilyl)oxy]-3-hydroxyquinuclidine
-
50% inhibition above 0.001 mM
3-(biphenyl-4-yl-4'-hydroxy)-2,3-dehydroquinuclidine
-
50% inhibition at 96 nM
3-(biphenyl-4-ylmethyl)-1-azabicyclo[2.2.2]oct-2-ene
-
IC50: 730 nM
3-(trans-4-stilbenyl)octahydropyridino[2,1-c][1,4]oxazin-3-ol
-
3-([2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetyl]amino)benzoic acid
-
-
3-([2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetyl]amino)propionic acid
-
-
3-C-carboxy-2,4-dideoxy-2-dodec-11-en-1-ylpentaric acid
-
-
3-C-carboxy-2,4-dideoxy-2-dodecylpentaric acid
-
-
3-[(1-[3-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]propanoyl]-4-piperidinyl)oxy]propanoic acid
-
-
3-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6Hpyrrolo[1,2-a][4,1]benzoxazepin-4-yl]propionic acid
-
-
3-[[4-(benzyloxy)phenyl]ethynyl]-1-azabicyclo[2.2.2]oct-2-ene
-
IC50: 830 nM
4-methyl-2-(3',5'-di-tert-butyl-4'-hydroxy-4-biphenyl)-3,4-dihydro-2H-1,4-benzothiazine-2-ol
-
4-methyl-2-(4'-hydroxybiphenyl)-3,4-dihydro-2H-1,4-benzothiazin-2-ol
-
4-methyl-2-(4'-trifluromethyl-4-biphenyl)-3,4-dihydro-2H-1,4-benzothiazine-2-ol
-
4-methyl-2-phenyl-3,4-dihydro-2H-benzothiazin-2-ol
-
4-methyl-2-phenyl-3,4-dihydro-2H-benzoxazin-2-ol
-
4-[3-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]propanoyl]-2-morpholine carboxylic acid
-
-
6-([[(1R,5S)-7-chloro-5-(2-chlorophenyl)-1-(2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetyl]amino)hexanoic acid
-
-
Ammonium analogues
-
overview
-
BMS 187745
-
decrease of cholesterol or LDL
BPH-701
about 60% inhibition at 0.005 mM
celastrol
binds to the enzyme in a noncompetitive manner, but does not bind covalently. Celastrol also inhibits growth of the highly virulent Aspergillus fumigatus by inhibiting flavin-dependent monooxygenase siderophore A , it may be a promising multi-target lead for antifungal development
CHQHNSMYC
an ennea-peptide, slight inhibition
CKTENMQSC
an ennea-peptide
CLGVHSSSC
an ennea-peptide
CLSPHSMFC
an ennea-peptide
CP-294838
a benzoxazepinone IC50 130 nM
CP-295697
a bisphosphonate, IC50: 20 nM
CQMHQLSSC
an ennea-peptide
CSGMKTTGC
an ennea-peptide
CSTLKVATC
an ennea-peptide
CSTPWHQWC
an ennea-peptide
CTVNWYPLC
an ennea-peptide
cynarin
by the combination of three different computational approaches and biological assays, cynarin is selected as a potential squalene synthase inhibitor
ethyl 4-(1-azabicyclo[2.2.2]oct-2-en-3-yl)benzoate
-
IC50: 50 nM
ethyl [(1R,5S)-7-chloro-5-(2-chlorophenyl)-1-(2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetate
-
-
Farnesyl methylenediphosphonate
a substrate analogue, potent enzyme inhibition
Guanidinium chloride
loss of 86% activity at 0.3M GdmCl, 50% at 0.2 M
methyl 2-[8-chloro-6-(2,3-dimethoxyphenyl)-4H,6Hpyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetate
-
-
N-isopropyl-biphenyloxypropylamine
-
50% inhibition at 93 nM
N-[[(3R,5S)-7-chloro-5-(2,3-dimethoxyphenyl)-1-(2,2-dimethylpropyl)-2-oxo-1,2,3,5-tetrahydro-4,1-benzoxazepin-3-yl]acetyl]-L-aspartic acid
-
-
NADP+
-
inhibitor of squalene synthesis
SPHS
a tetrapeptide, slight inhibition
Urea
loss of 81% activity at 2 M, 50% at 1 M
[(1R,5R)-7-chloro-1-(2-methylpropyl)-2-oxo-5-phenyl-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetic acid
-
-
[(1R,5S)-1-benzyl-7-chloro-5-(2-chlorophenyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetic acid
-
-
[(1R,5S)-5-(2-bromophenyl)-7-chloro-1-(2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetic acid
-
-
[(1R,5S)-5-(2-chlorophenyl)-1-(2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetic acid
-
-
[(1R,5S)-5-(2-chlorophenyl)-7-fluoro-1-(2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetic acid
-
-
[(1R,5S)-5-(2-chlorophenyl)-7-methyl-1-(2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetic acid
-
-
[(1R,5S)-7-chloro-5-(2,3-dimethoxyphenyl)-1-(2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetic acid
-
-
[(1R,5S)-7-chloro-5-(2-chlorophenyl)-1-(2-hydroxy-2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetic acid
-
-
[(1R,5S)-7-chloro-5-(2-chlorophenyl)-1-(2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetic acid
-
-
[(1R,5S)-7-chloro-5-(2-methoxyphenyl)-1-(2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetic acid
-
-
[(4R,6R)-8-chloro-6-(2,3-dimethoxyphenyl)-1-(propan-2-yl)-6,10b-dihydro-1H,4H-[2]benzoxepino[4,5-c][1,2]oxazol-4-yl]acetic acid
-
-
[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-1-(propan-2-yl)-6,10b-dihydro-1H,4H-[2]benzoxepino[4,5-c][1,2]oxazol-4-yl]acetic acid
-
-
[(4S,6R)-8-chloro-6-(2,3-dimethoxyphenyl)-1-(propan-2-yl)-6,10b-dihydro-1H,4H-[2]benzoxepino[4,5-c][1,2]oxazol-4-yl]acetic acid
-
-
[(4S,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-1-(propan-2-yl)-6,10b-dihydro-1H,4H-[2]benzoxepino[4,5-c][1,2]oxazol-4-yl]acetic acid
-
-
[(6S)-8-chloro-6-(2,3-dimethoxyphenyl)-1-(propan-2-yl)-6,10b-dihydro-1H,4H-[2]benzoxepino[4,5-c][1,2]oxazol-4-yl]acetic acid
-
-
(1-[[(3R,5S)-1-[3-(acetyloxy)-2,2-dimethylpropyl]-7-chloro-5-(2,3-dimethoxyphenyl)-2-oxo-1,2,3,5-tetrahydro-4,1-benzoxazepin-3-yl]acetyl]piperidin-4-yl)acetic acid
-
i.e. lapaquistat acetate or TAK-475
(1-[[(3R,5S)-1-[3-(acetyloxy)-2,2-dimethylpropyl]-7-chloro-5-(2,3-dimethoxyphenyl)-2-oxo-1,2,3,5-tetrahydro-4,1-benzoxazepin-3-yl]acetyl]piperidin-4-yl)acetic acid
-
i.e. lapaquistat acetate or TAK-475
1-allyl-2-[3-(isopropylamino)propoxy]-9H-carbazole
-
50% inhibition at 32 nM
1-allyl-2-[3-(isopropylamino)propoxy]-9H-carbazole
-
50% inhibition at 66 nM
1-allyl-2-[3-(isopropylamino)propoxy]-9H-xanthen-9-one
-
50% inhibition at 120 nM
1-allyl-2-[3-(isopropylamino)propoxy]-9H-xanthen-9-one
-
50% inhibition at 120 nM
2-[3-(isopropylamino)propoxy]-9H-carbazole
-
50% inhibition at 810 nM
2-[3-(isopropylamino)propoxy]-9H-carbazole
-
50% inhibition at 110 nM
3-(4-quinolin-6-ylphenyl)quinuclidin-3-ol
-
i.e. RPR107393, 50% inhibition at 57 nM
3-(4-quinolin-6-ylphenyl)quinuclidin-3-ol
-
i.e. RPR107393, 50% inhibition at 68 nM
BMS-188494
-
-
BMS-188494
-
decrease of cholesterol or LDL
BMS-188494
-
no induction of myotoxicity
BPH-652
potent inhibitor
BPH-652
a phosphonosulfonate, binding structure
EP2302
-
-
EP2302
-
decrease of cholesterol or LDL
EP2302
-
decrease of cholesterol and triglyceride biosynthesis
EP2306
-
decrease of cholesterol or LDL
EP2306
-
decrease of cholesterol and triglyceride biosynthesis
ER-27856
-
-
ER-27856
-
decrease of cholesterol biosynthesis
ER-27856
-
decrease of cholesterol biosynthesis
ER-28448
-
decrease of cholesterol biosynthesis
ER-28448
-
decrease of cholesterol biosynthesis
farnesyl diphosphate
-
no inhibition of presqualene diphosphate synthase reaction; substrate inhibitor of squalene synthase reaction
farnesyl diphosphate
-
substrate inhibitor of squalene synthase reaction
lapaquistat
-
lipid-lowering effect
lapaquistat
-
lipid-lowering effect
lapaquistat
-
decrease of cholesterol or LDL
lapaquistat
-
lipid-lowering effect
lapaquistat
-
lipid-lowering effect
RPR107393
-
reduction in plasma cholesterol concentrations
RPR107393
-
reduction of plasman cholesterol concentrations
RPR107393
-
inhibition of cholesterol biosynthesis and reduced plasma total cholesterol levels
squalestatin
-
hypolipidemic effects but potential toxicity because of high levels of urinary dicarboxylic acid
squalestatin
-
hypolipidemic effects but potential toxicity because of high levels of urinary dicarboxylic acid
TAK-475
-
-
YM-53601
-
decrease of non-high-density lipoprotein cholesterol
YM-53601
-
reduction of non-high-density lipoprotein cholesterol concentrations
YM-53601
-
decrease of non-high-density lipoprotein cholesterol
YM-53601
-
reduction of non-high-density lipoprotein cholesterol concentrations
YM-53601
-
decrease of non-high-density lipoprotein cholesterol
zaragozic acid
potent inhibitor
zaragozic acid
-
hypolipidemic effects but potential toxicity because of high levels of urinary dicarboxylic acid
zaragozic acid
IC50 0.7 nM
zaragozic acid
-
competitive to farnesyl diphosphate
zaragozic acid
competitive type of inhibition
zaragozic acid
-
hypolipidemic effects but potential toxicity because of high levels of urinary dicarboxylic acid
zaragozic acid
-
decrease in plasma cholesterol
zaragozic acid A
-
0.04 mM
zaragozic acid A
-
enzyme binding induces a local conformational change in the substrate binding site, and its C-6 acyl group also extends over to the cofactor binding cavity, enzyme-inhibitor binding structure and thermodynamics, detailed overview
zaragozic acid A
is a potent inhibitor of mammalian SSN and also a competitive inhibitor of recombinant Leishmania donovani SSN, 50% inhibition at 100 nM
zaragozic acid A
-
inhibition of squalene synthase. Administration also significantly increases the rate of degradation of hepatic low density lipoprotein receptor protein, and increases proprotein convertase subtilisin/kexin type 9 mRNA and protein levels in concert with an increase in hepatic low density lipoprotein receptor mRNA levels, low density lipoprotein turnover, and decreases in serum cholesterol levels
zaragozic acid A
Thermosynechococcus vestitus
-
pH 7.2, 37°C
additional information
-
identification and optimization of tetrahydro-2H-3-benzazepin-2-ones as squalene synthase inhibitors, overview
-
additional information
-
4H,6H-[2]benzoxepino[4,5-c][1,2]oxazoles as squalene synthase inhibitors, design, synthesis, structure-activity relationship, and pharmacological profiles, overview
-
additional information
discovering peptide inhibitors of human squalene synthase through screening the phage-displayed cyclic peptide c7c library, molecular modelling and ADMET predictions of the selected peptides, using the crystal structure PDB 1EZF, a homo-trimer protein complex (with inhibitors CP-320473, CP-458003 and CP-424677), as the target, overview. The inhibitory peptides have potentials to develop cholesterol-lowering therapeutics. The ligand-protein interaction analysis also reveals that the inner hydrophobic pocketis a critical site of human enzyme for inhibition. No binding of peptide CPWWYGPWC. Cytotoxicity effects of different inhibitors, and protein-ligand interaction analysis, overview
-
additional information
-
discovering peptide inhibitors of human squalene synthase through screening the phage-displayed cyclic peptide c7c library, molecular modelling and ADMET predictions of the selected peptides, using the crystal structure PDB 1EZF, a homo-trimer protein complex (with inhibitors CP-320473, CP-458003 and CP-424677), as the target, overview. The inhibitory peptides have potentials to develop cholesterol-lowering therapeutics. The ligand-protein interaction analysis also reveals that the inner hydrophobic pocketis a critical site of human enzyme for inhibition. No binding of peptide CPWWYGPWC. Cytotoxicity effects of different inhibitors, and protein-ligand interaction analysis, overview
-
additional information
evaluation of the structure of substrate/inhibitor-binding sites via homology modeling, overview. Supplementation of any type of detergent inhibits the enzyme activity during purification
-
additional information
-
evaluation of the structure of substrate/inhibitor-binding sites via homology modeling, overview. Supplementation of any type of detergent inhibits the enzyme activity during purification
-
additional information
-
peroxisomal squalene synthase is inhibited by sonication, microsomal enzyme not
-
additional information
-
design, synthesis, and identification of highly potent benzhydrol derivatives as squalene synthase inhibitors, design of tricyclic pyrrolobenzoxazepine derivatives, overview
-
additional information
overexpression of the enzyme's C-terminal domain containing a hinge domain from fungi, not from animals or plants, leads to growth inhibition of wild-type yeast
-
additional information
-
overexpression of the enzyme's C-terminal domain containing a hinge domain from fungi, not from animals or plants, leads to growth inhibition of wild-type yeast
-
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0.0014
(1-[[(1R,5S)-7-chloro-5-(2-chlorophenyl)-1-(2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetyl]piperidin-4-yl)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.000213
(1-[[(3R,5S)-1-[3-(acetyloxy)-2,2-dimethylpropyl]-7-chloro-5-(2,3-dimethoxyphenyl)-2-oxo-1,2,3,5-tetrahydro-4,1-benzoxazepin-3-yl]acetyl]piperidin-4-yl)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00026
(1-[[(3R,5S)-7-chloro-5-(2,3-dimethoxyphenyl)-1-(3-hydroxy-2,2-dimethylpropyl)-2-oxo-1,2,3,5-tetrahydro-4,1-benzoxazepin-3-yl]acetyl]piperidin-4-yl)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.000131
(1-[[(6S)-8-chloro-6-(2,3-dimethoxyphenyl)-1-(propan-2-yl)-6,10b-dihydro-1H,4H-[2]benzoxepino[4,5-c][1,2]oxazol-4-yl]acetyl]piperidin-4-yl)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00037
(1R,5S)-7-chloro-5-(2-methoxyphenyl)-1-(2-methylpropyl)-3-[2-oxo-2-(piperidin-1-yl)ethyl]-1,3,4,5-tetrahydro-2H-3-benzazepin-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0055
(2E)-3-[(1R,5S)-3-(carboxymethyl)-7-chloro-5-(2-chlorophenyl)-2-oxo-2,3,4,5-tetrahydro-1H-3-benzazepin-1-yl]-2-methylprop-2-enoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0015
(3R)-3-[[3-(benzyloxy)phenyl]ethynyl]-1-azabicyclo[2.2.2]octan-3-ol
Trypanosoma cruzi
-
IC50: 1500 nM
0.0000014
(3S)-1-(3-((4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl)propanoyl)-3-piperidine carboxylic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.0000023
(3S)-1-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetyl]-3-piperidinecarboxylic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.0000017
1-(2-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]ethyl]-2H-1,2,3,4-tetrazol-5-yl)cyclopropanecarboxylic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.0000022
1-(3-((4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl)propanoyl)-3-azetidine carboxylic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.0000034
1-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetyl]-4-piperidinecarboxylic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.00000059
1-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]ethyl]-1H-1,2,3-triazole-4-carboxylic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.0000021
1-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]ethyl]-1H-pyrazole-4-carboxylic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.00022
1-[[(1R,5R)-7-chloro-5-(2,3-dimethoxyphenyl)-1-(2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetyl]piperidine-4-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00045
1-[[(1R,5S)-7-chloro-5-(2,3-dimethoxyphenyl)-1-(2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetyl]piperidine-4-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00093
1-[[(1R,5S)-7-chloro-5-(2-chlorophenyl)-1-(2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetyl]piperidine-4-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0005
1-[[(1R,5S)-7-chloro-5-(2-methoxyphenyl)-1-(2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetyl]piperidine-4-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.02
1-[[(1S,5S)-7-chloro-5-(2,3-dimethoxyphenyl)-1-(2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetyl]piperidine-4-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.000112
1-[[(6S)-8-chloro-6-(2,3-dimethoxyphenyl)-1-(propan-2-yl)-6,10b-dihydro-1H,4H-[2]benzoxepino[4,5-c][1,2]oxazol-4-yl]acetyl]piperidine-4-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0184
11,12-di-O-methylcarnosol
Rattus norvegicus
pH 7.4, 37°C
0.378
11,12-diacetyl-carnosol
Rattus norvegicus
pH 7.4, 37°C
0.000007
2-(1-(3-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]propanoyl)-3-azetidinyl)acetic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.0000013
2-(1-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetyl]-4-piperidinyl)acetic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.00000051
2-(1-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]ethyl]-1H-1,2,3-triazol-4-yl)acetic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.00000081
2-(1-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]ethyl]-1H-1,2,3-triazol-5-yl)acetic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.0000013
2-(1-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]ethyl]-1H-pyrazol-3-yl)acetic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.0000031
2-(1-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]ethyl]-1H-pyrazol-4-yl)acetic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.0000016
2-(1-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]ethyl]-1H-pyrazol-5-yl)acetic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.0006
2-(1-[2-[(4S,6R)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetyl]-4-piperidinyl)acetic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.0000027
2-(1-[2-[8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetyl]-4-piperidinyl)acetic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.0000024
2-(1-[3-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]propanoyl]-4-piperidinyl)acetic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.0000011
2-(2-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl)ethyl]-2H-1,2,3,4-tetrazol-5-yl]-2-methylpropanoic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.0000011
2-(2-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl)ethyl]-2H-1,2,3,4-tetrazol-5-yl]acetic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.0000011
2-(2-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]ethyl]-1H-1,2,3,4-tetrazol-5-yl)acetic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.0000043
2-(4-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetyl]-1-piperazinyl)acetic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.0000022
2-(4-[3-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]propanoyl]-2-oxo-1-piperazinyl)acetic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.007
2-(trans-4-stilbenyl)-4-methyl-morpholin-2-ol
Rattus norvegicus
pH and temperature not specified in the publication
0.0000023
2-([2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetyl]amino)acetic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.0000017
2-[(1-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]ethyl]-1H-1,2,3-triazol-4-yl)methoxy]-2-ethylbutanoic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.00000069
2-[(1-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]ethyl]-1H-1,2,3-triazol-4-yl)methoxy]-2-methylpropanoic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.00000068
2-[(1-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]ethyl]-1H-1,2,3-triazol-4-yl)methoxy]acetic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.0000009
2-[(1-[3-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]propanoyl]-4-piperidinyl)methoxy]acetic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.0000008
2-[(1-[3-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]propanoyl]-4-piperidinyl)oxy]acetic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.0000025
2-[(2-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]ethyl]-2H-1,2,3,4-tetrazol-5-yl)methoxy]-2-methylpropanoic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.000162
2-[(6S)-8-chloro-6-(2,3-dimethoxyphenyl)-1-(propan-2-yl)-6,10b-dihydro-1H,4H-[2]benzoxepino[4,5-c][1,2]oxazol-4-yl]-1-[(3R)-3-hydroxypyrrolidin-1-yl]ethanone
Homo sapiens
-
pH and temperature not specified in the publication
0.0000016
2-[1,8-dichloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.00000089
2-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]ethyl]-2H-1,2,3,4-tetrazol-5-carboxylic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.0006
2-[8-chloro-6-(1-naphthyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.000052
2-[8-chloro-6-(2,3-dichlorobenzoyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.00044
2-[8-chloro-6-(2,3-dihydro-1,4-benzodioxin-5-yl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.0000076
2-[8-chloro-6-(2,3-dimethoxyphenyl)-1-(4-morpholinylmethyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.00054
2-[8-chloro-6-(2,3-dimethoxyphenyl)-1-[(dimethylamino)methyl]-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.0000033
2-[8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.00000085
3-(2-[2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]ethyl]-2H-1,2,3,4-tetrazol-5-yl)propanoic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.00073
3-(biphenyl-4-ylmethyl)-1-azabicyclo[2.2.2]oct-2-ene
Trypanosoma cruzi
-
IC50: 730 nM
0.042
3-(trans-4-stilbenyl)octahydropyridino[2,1-c][1,4]oxazin-3-ol
Rattus norvegicus
pH and temperature not specified in the publication
0.000004
3-([2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetyl]amino)benzoic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.0000029
3-([2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetyl]amino)propionic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.0000014
3-[(1-[3-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]propanoyl]-4-piperidinyl)oxy]propanoic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.0000031
3-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6Hpyrrolo[1,2-a][4,1]benzoxazepin-4-yl]propionic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.00083
3-[[4-(benzyloxy)phenyl]ethynyl]-1-azabicyclo[2.2.2]oct-2-ene
Trypanosoma cruzi
-
IC50: 830 nM
0.0065
4-methyl-2-(3',5'-di-tert-butyl-4'-hydroxy-4-biphenyl)-3,4-dihydro-2H-1,4-benzothiazine-2-ol
Rattus norvegicus
pH and temperature not specified in the publication
0.0085
4-methyl-2-(4'-hydroxybiphenyl)-3,4-dihydro-2H-1,4-benzothiazin-2-ol
Rattus norvegicus
pH and temperature not specified in the publication
0.014
4-methyl-2-(4'-trifluromethyl-4-biphenyl)-3,4-dihydro-2H-1,4-benzothiazine-2-ol
Rattus norvegicus
pH and temperature not specified in the publication
0.028
4-methyl-2-phenyl-3,4-dihydro-2H-benzothiazin-2-ol
Rattus norvegicus
pH and temperature not specified in the publication
0.05
4-methyl-2-phenyl-3,4-dihydro-2H-benzoxazin-2-ol
Rattus norvegicus
pH and temperature not specified in the publication
0.0000016
4-[3-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]propanoyl]-2-morpholine carboxylic acid
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.0024
6-([[(1R,5S)-7-chloro-5-(2-chlorophenyl)-1-(2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetyl]amino)hexanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
1.336
7alpha-ethoxyrosmanol
Rattus norvegicus
pH 7.4, 37°C
0.543
7alpha-methoxyrosmanol
Rattus norvegicus
pH 7.4, 37°C
0.0176
carnosol
Rattus norvegicus
pH 7.4, 37°C
1.524
carnosol quinone
Rattus norvegicus
pH 7.4, 37°C
0.00083
celastrol
Aspergillus flavus
pH 7.4, temperature not specified in the publication
0.0001
chlorogenic acid
Sus scrofa
-
pH 7.4, 37°C
0.087
CKTE
Homo sapiens
pH and temperature not specified in the publication
0.064
CLSPHSMFC
Homo sapiens
pH and temperature not specified in the publication
0.00013
CP-294838
Homo sapiens
a benzoxazepinone IC50 130 nM
0.00002
CP-295697
Homo sapiens
a bisphosphonate, IC50: 20 nM
0.00000084
E5700
Trypanosoma cruzi
-
IC50: 0.84 nM
0.00000352
ER119884
Trypanosoma cruzi
-
IC50: 3.52 nM
0.00005
ethyl 4-(1-azabicyclo[2.2.2]oct-2-en-3-yl)benzoate
Trypanosoma cruzi
-
IC50: 50 nM
0.02
ethyl [(1R,5S)-7-chloro-5-(2-chlorophenyl)-1-(2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetate
Homo sapiens
-
pH and temperature not specified in the publication
0.0692
galdosol
Rattus norvegicus
pH 7.4, 37°C
0.0903
isorosmanol
Rattus norvegicus
pH 7.4, 37°C
0.00022
methyl 2-[8-chloro-6-(2,3-dimethoxyphenyl)-4H,6Hpyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetate
Rattus norvegicus
-
pH 7.2-7.5, 37°C
0.0969
rosmadial
Rattus norvegicus
pH 7.4, 37°C
0.0802
rosmanol
Rattus norvegicus
pH 7.4, 37°C
0.0269
rosmaquinone
Rattus norvegicus
pH 7.4, 37°C
0.076
SMFC
Homo sapiens
pH and temperature not specified in the publication
0.09
WHQW
Homo sapiens
pH and temperature not specified in the publication
0.0000007
zaragozic acid
Homo sapiens
IC50 0.7 nM
0.0000955
zaragozic acid A
Thermosynechococcus vestitus
-
pH 7.2, 37°C
0.0153
[(1R,5R)-7-chloro-1-(2-methylpropyl)-2-oxo-5-phenyl-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.02
[(1R,5S)-1-benzyl-7-chloro-5-(2-chlorophenyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0022
[(1R,5S)-5-(2-bromophenyl)-7-chloro-1-(2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.02
[(1R,5S)-5-(2-chlorophenyl)-1-(2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.02
[(1R,5S)-5-(2-chlorophenyl)-7-fluoro-1-(2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.02
[(1R,5S)-5-(2-chlorophenyl)-7-methyl-1-(2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0012
[(1R,5S)-7-chloro-5-(2,3-dimethoxyphenyl)-1-(2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.02
[(1R,5S)-7-chloro-5-(2-chlorophenyl)-1-(2-hydroxy-2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0033
[(1R,5S)-7-chloro-5-(2-chlorophenyl)-1-(2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0019
[(1R,5S)-7-chloro-5-(2-methoxyphenyl)-1-(2-methylpropyl)-2-oxo-1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00142
[(4R,6R)-8-chloro-6-(2,3-dimethoxyphenyl)-1-(propan-2-yl)-6,10b-dihydro-1H,4H-[2]benzoxepino[4,5-c][1,2]oxazol-4-yl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.000056
[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-1-(propan-2-yl)-6,10b-dihydro-1H,4H-[2]benzoxepino[4,5-c][1,2]oxazol-4-yl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.000169
[(4S,6R)-8-chloro-6-(2,3-dimethoxyphenyl)-1-(propan-2-yl)-6,10b-dihydro-1H,4H-[2]benzoxepino[4,5-c][1,2]oxazol-4-yl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0055
[(4S,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-1-(propan-2-yl)-6,10b-dihydro-1H,4H-[2]benzoxepino[4,5-c][1,2]oxazol-4-yl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.000223
[(6S)-8-chloro-6-(2,3-dimethoxyphenyl)-1-(propan-2-yl)-6,10b-dihydro-1H,4H-[2]benzoxepino[4,5-c][1,2]oxazol-4-yl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
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evolution
phylogenetic analysis of SQS enzymes in plants shows highly similar conserved pattern including 77DTVED81 and 213DYLED217 motifs, which are rich in aspartic acids involved in FPP binding
evolution
phylogenetic analysis of SQS enzymes in plants shows highly similar conserved pattern including 77DTVED81 and 213DYLED217 motifs, which are rich in aspartic acids involved in FPP binding
evolution
the enzyme belongs to the isoprenoid biosynthesis enzymes class 1 superfamily
evolution
-
the enzyme belongs to the isoprenoid biosynthesis enzymes class 1 superfamily
-
malfunction
-
Inhibition of squalene synthase leads directly to a reduction in cholesterol biosynthesis and thus to a fall in plasma cholesterol levels. Plasma LDL-cholesterol and triglycerides are lowered by squalene synthase inhibitors
malfunction
-
modifications in region IV prevents SQS from undergoing the second half-reaction, indicating that this region may reasonably constitute a functional NADPH binding site
malfunction
enzyme overexpression in transgenic Withania somnifera plants affects the shoot elongation and multiplication, phenotype, overview
malfunction
the SQS inhibitors YM-53601 and zaragozic acid A decrease hepatitis C virus RNA, protein, and progeny production in HCV-infected cells without affecting cell viability, using the HCV JFH-1 strain and human hepatoma Huh-7.5.1-derived cells. siRNA-mediated knockdown of SQS leads to significantly reduced HCV production, confirming the enzyme acts as an antiviral target. A metabolic labeling study demonstrates that enzyme inhibitor YM-53601 suppresses the biosynthesis of cholesterol and cholesteryl esters at antiviral concentrations
metabolism
-
key enzyme in the isoprenoid pathway
metabolism
-
part of cholesterol biosynthesis pathway
metabolism
-
part of cholesterol biosynthesis pathway
metabolism
-
part of cholesterol biosynthesis pathway
metabolism
-
part of cholesterol biosynthesis pathway
metabolism
-
part of cholesterol biosynthesis pathway
metabolism
-
part of cholesterol biosynthesis pathway
metabolism
-
part of cholesterol synthesis pathway
metabolism
-
part of cholesterol synthesis pathway
metabolism
-
part of cholesterol synthesis pathway
metabolism
-
part of cholesterol synthesis pathway
metabolism
-
part of cholesterol synthesis pathway
metabolism
-
part of cholesterol synthesis pathway
metabolism
-
part of cholesterol synthesis pathway
metabolism
-
part of cholesterol synthesis pathway
metabolism
-
part of cholesterol synthesis pathway
metabolism
-
squalene synthase catalyzes the committed step of sterol synthesis
metabolism
-
squalene synthase catalyzes the conversion of farnesyl pyrophosphate into squalene by reductive condensation. This is a crucial step in cholesterol biosynthesis, squalene serves as the exclusive precursor for cholesterol
metabolism
squalene synthase catalyzes the first enzymatic step of the central isoprenoid pathway in sterol and triterpenoid biosynthesis
metabolism
squalene synthase is a key enzyme in the regulation of isoprenoid biosynthesis and is important in the withanolides biosynthesis pathway, overview
metabolism
-
squalene synthase is a key enzyme involved in antifungal steroidal glycoalkaloids biosynthesis. Steroidal glycoalkaloids are a family of nitrogenous secondary metabolites acting as phytoalexins, e.g. gamma-solamargine and its aglycone solasodine from Solanum nigrum inhibiting hyphae formation of Fusarium oxysporum
metabolism
squalene synthase is a major enzyme in the sterol biosynthetic pathway
metabolism
squalene synthase is the key enzyme of saponin biosynthesis pathway
metabolism
enzyme SQS operates at a branch point of the withanolide biosynthetic pathway regulating the metabolic flux and catalyzes the first committed step leading to the synthesis of different withanolides
metabolism
four major steps - substrate binding, condensation, intermediate formation and translocation - of the ordered sequential mechanisms involved in the 1'-1 isoprenoid biosynthetic pathway
metabolism
-
squalene synthase catalyzes the first committed step in sterol biosynthesis
metabolism
squalene synthase catalyzes the first committed step in sterol biosynthesis
metabolism
squalene synthase catalyzes the first committed step in sterol biosynthesis
metabolism
squalene synthase catalyzes the first committed step in sterol biosynthesis, role of squalene synthase in the ergosterol biosynthetic pathway of budding yeast, overview
metabolism
Thermosynechococcus vestitus
-
squalene synthase catalyzes the first step of sterol/hopanoid biosynthesis in the organism
metabolism
squalene synthase catalyzes the first step of sterol/hopanoid biosynthesis in the organism
metabolism
squalene synthase catalyzes the first step of sterol/hopanoid biosynthesis in the organism
metabolism
the enzyme catalyzes the first dedicated step in the biosynthesis of sterols and other triterpenoids
metabolism
the enzyme catalyzes the first dedicated step in the biosynthesis of sterols and other triterpenoids
metabolism
the enzyme is a key enzyme in the isoprenoid biosynthesis
metabolism
-
the enzyme is involved in squalene synthesis and sterol metabolism
metabolism
-
squalene synthase catalyzes the first enzymatic step from the central isoprenoid pathway toward sterol and triterpenoid biosynthesis
metabolism
the enzyme catalyzes a key steps in the biosynthesis of cyclic terpenoids
metabolism
the enzyme is involved in celastrol biosynthesis
metabolism
-
the enzyme is a key enzyme in the isoprenoid biosynthesis
-
metabolism
-
squalene synthase is a major enzyme in the sterol biosynthetic pathway
-
physiological function
-
essential role in embryonic development
physiological function
-
influence on regulation of cholesterol metabolism
physiological function
-
influence on regulation of cholesterol metabolism
physiological function
-
influence on regulation of cholesterol metabolism
physiological function
-
influence on regulation of cholesterol metabolism
physiological function
-
influence on regulation of cholesterol metabolism
physiological function
-
influence on regulation of cholesterol metabolism
physiological function
-
influence on regulation of cholesterol metabolism
physiological function
-
influence on regulation of cholesterol metabolism
physiological function
squalene synthase catalyses an unusual head-to-head reductive dimerization of two molecules of farnesyl-pyrophosphate in a two-step reaction to form squalene
physiological function
squalene synthase functions as a key regulator in channeling the carbon flux into both the primary and secondary metabolite branches, and squalene synthase may play a regulatory role in directing triterpene intermediates and sterol pathways
physiological function
enzyme SQS plays an important role in regulating isoprenoid biosynthesis in eukaryotes
physiological function
SQS play an important regulatory role in phytosterol biosynthetic pathway
physiological function
Thermosynechococcus vestitus
-
squalene is biosynthesized via the head-to-head condensation of two molecules of farnesyl diphosphate, which is catalyzed by the single enzyme squalene synthase. Squalene is a precursor of thousands of bioactive triterpenoids
physiological function
squalene is biosynthesized via the head-to-head condensation of two molecules of farnesyl diphosphate, which is catalyzed by the single enzyme squalene synthase. Squalene is a precursor of thousands of bioactive triterpenoids
physiological function
squalene synthase is the rate-limiting enzyme located at the downstream of cholesterol synthesis pathway
physiological function
the catalytic domain performs the head-to-head dimerization of two molecules of farnesyl diphosphate to form squalene, a 30 carbon isoprenoid oxidized by squalene monooxygenase (Erg1) and cyclized by lanosterol synthase
physiological function
-
the enzyme is involved in squalene synthesis and sterol metabolism
physiological function
the enzyme squalene synthase catalyzes the first committed step in sterol biosynthesis by condensing two molecules of farnesyl diphosphate into squalene in two reaction steps
physiological function
the enzyme squalene synthase catalyzes the first committed step in sterol biosynthesis by condensing two molecules of farnesyl diphosphate into squalene in two reaction steps
physiological function
squalene and botryococcene are branched-chain, triterpene compounds that arise from the head-tohead condensation of two molecules of farnesyl diphosphate to yield 1'-1 and 1'-3 linkages, respectively
physiological function
-
squalene synthase catalyses an unusual head-to-head reductive dimerization of two molecules of farnesyl-pyrophosphate in a two-step reaction to form squalene
-
additional information
-
enzyme overexpression leads a significant 4fold enhancement in squalene synthase activity and 2.5fold enhancement in withanolide A content, transformed cell suspension cultures also produce withaferin A, which is absent in the non-transformed cell cultures
additional information
methyl jasmonate, abscisic acid, and ethephon induce the accumulation of BfSS1 mRNA, overexpression of the BfSS1 gene in the sense orientation in Bupleurum falcatum increases the mRNA accumulation of downstream genes such as squalene epoxidase and cycloartenol synthase but decreases the mRNA levels of beta-amyrin synthase, a triterpene synthase mRNA. Methyljasmonate treatment of transgenic roots overexpressing BfSS1 in the sense orientation fails to stimulate beta-amyrin synthase mRNA accumulation but still enhances saikosaponin and phytosterol production
additional information
-
methyl jasmonate, abscisic acid, and ethephon induce the accumulation of BfSS1 mRNA, overexpression of the BfSS1 gene in the sense orientation in Bupleurum falcatum increases the mRNA accumulation of downstream genes such as squalene epoxidase and cycloartenol synthase but decreases the mRNA levels of beta-amyrin synthase, a triterpene synthase mRNA. Methyljasmonate treatment of transgenic roots overexpressing BfSS1 in the sense orientation fails to stimulate beta-amyrin synthase mRNA accumulation but still enhances saikosaponin and phytosterol production
additional information
the catalytic site is composed of the large central cavity formed by antiparallel alpha helices with two aspartate rich regions (DXXXD) on opposite walls, these residues are considered to play roles in binding of prenyl phosphates by binding Mg2+ ions
additional information
-
the catalytic site is composed of the large central cavity formed by antiparallel alpha helices with two aspartate rich regions (DXXXD) on opposite walls, these residues are considered to play roles in binding of prenyl phosphates by binding Mg2+ ions
additional information
the substrate binding site is present at the core region of the enzyme structure. The predicted active site involves Phe 204, Leu 205, Gln 206, Thr 208, Asn 209, Ala 293, and Leu 297. The aspartate side chains are involved in binding multiple Mg2+ ions that stabilize binding of diphosphate groups in the substrate.
additional information
-
the substrate binding site is present at the core region of the enzyme structure. The predicted active site involves Phe 204, Leu 205, Gln 206, Thr 208, Asn 209, Ala 293, and Leu 297. The aspartate side chains are involved in binding multiple Mg2+ ions that stabilize binding of diphosphate groups in the substrate.
additional information
determination and analysis of human SQS and its mutants in complex with several substrate analogues and intermediates coordinated with Mg2+ or Mn2+, SQS active analysis, overview
additional information
-
determination and analysis of human SQS and its mutants in complex with several substrate analogues and intermediates coordinated with Mg2+ or Mn2+, SQS active analysis, overview
additional information
functional analyses of the enzyme's two DXXD(E)D motifs and the highly conserved aromatic amino acid residues, kinetic analysis and reaction mechanism, overview. The potential active-site residues 58DXX61E62D (S1 site) and 213DXX216D217D (S2 site) are assumed to be involved in the binding of the substrate farnesyl diphosphate through the Mg2+ ion. The S1 site and the two basic residues R55 and K212 are responsible for the binding of farnesyl diphosphate
additional information
-
functional analyses of the enzyme's two DXXD(E)D motifs and the highly conserved aromatic amino acid residues, kinetic analysis and reaction mechanism, overview. The potential active-site residues 58DXX61E62D (S1 site) and 213DXX216D217D (S2 site) are assumed to be involved in the binding of the substrate farnesyl diphosphate through the Mg2+ ion. The S1 site and the two basic residues R55 and K212 are responsible for the binding of farnesyl diphosphate
additional information
homology modelling of SQS enzyme of Withania somnifera for the prediction of three-dimensional structure, molecular docking study of considered substrates, overview
additional information
-
homology modelling of SQS enzyme of Withania somnifera for the prediction of three-dimensional structure, molecular docking study of considered substrates, overview
additional information
molecular docking study, overview
additional information
molecular docking study, overview
additional information
-
squalene does not accumulate significantly in CrSQS-overexpressing cells, although conversion of farnesyl diphosphate to squalene is enhanced by overexpression of enzyme CrSQS
additional information
structure homology modelling using the crystal structure of human squalene synthase, PDB ID 1EZFB, as template, overview
additional information
-
structure homology modelling using the crystal structure of human squalene synthase, PDB ID 1EZFB, as template, overview
additional information
the hinge domain plays an essential functional role, such as assembly of ergosterol multi-enzymecomplexes in fungi
additional information
-
the hinge domain plays an essential functional role, such as assembly of ergosterol multi-enzymecomplexes in fungi
additional information
proposed catalytic cascades for the enzyme-mediated biosynthesis of squalene and botryococcene, and molecular modeling of Botryococcus braunii botryococcene and squalene synthase enzymes, overview. Substrate docking and molecular modeling
additional information
-
proposed catalytic cascades for the enzyme-mediated biosynthesis of squalene and botryococcene, and molecular modeling of Botryococcus braunii botryococcene and squalene synthase enzymes, overview. Substrate docking and molecular modeling
additional information
-
structure homology modelling using the crystal structure of human squalene synthase, PDB ID 1EZFB, as template, overview
-
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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
N171A/G207Q
site-directed mutagenesis
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
K45R
-
mutation with influence on total cholesterol and non-HDL-C levels
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
Q33R/D34N/S38N
the mutations do not affect the enzyme activity
Y73A
site-directed mutagenesis, structure comparison with bound metals and reaction intermediate PSPP compared to the wild-type enzyme
D280E
enzymic activity slightly above wild-type activity
D280P
enzymic activity about 74% of wild-type activity
D280Q
enzymic activity about 50% of wild-type activity
F285L
no enzymic activity
K45R
-
mutation with influence on total cholesterol and non-HDL-C levels
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
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
K45R
-
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
K45R
-
mutation with influence on total cholesterol and non-HDL-C levels
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
-
site-directed mutagenesis, the engineered enzyme E186K mutant mMaSQSDELTAC17 shows a 3.4fold improvement in catalytic efficiency (kcat/Km) compared to the control
-
K45R
-
mutation with influence on total cholesterol and non-HDL-C levels
K45R
-
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
-
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
-
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
-
heterologous expression of antigenic enzyme from Candida tropicalis in Pichia pastoris can be exploited for large-scale production
additional information
-
heterologous expression of antigenic enzyme from Candida tropicalis in Pichia pastoris can be exploited for large-scale production
-
additional information
-
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
-
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
-
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
-
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
-
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
siRNA-mediated knockdown of SQS in hepatoma cells
additional information
-
siRNA-mediated knockdown of SQS in hepatoma cells
additional information
various mutations clustered around the residues that are important for NADPH binding effectively convert SQS into a dehydrosqualene synthase, 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
construction of a soluble functional transmembrane domain-deleted (385-409 aa) MoSQS mutant (MoSQSDELTATM)
additional information
-
construction of a soluble functional transmembrane domain-deleted (385-409 aa) MoSQS mutant (MoSQSDELTATM)
additional information
-
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
-
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
-
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
-
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
-
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
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Kuswik-Rabiega, G.; Rilling, H.C.
Squalene synthetase. Solubilization and partial purification of squalene synthetase, copurification of presqualene pyrophosphate and squalene synthetase activities
J. Biol. Chem.
262
1505-1509
1987
Saccharomyces cerevisiae
brenda
Agnew, W.S.
Squalene synthetase
Methods Enzymol.
110
359-373
1985
Saccharomyces cerevisiae
brenda
Nishino, T.; Katsuki, H.
Formation of 12-cis-dehydrosqualene catalyzed by squalene synthetase
Methods Enzymol.
110
373-375
1985
Saccharomyces cerevisiae
brenda
Qureshi, A.A.; Beytia, E.D.; Porter, J.W.
Squalene synthetase. I. Dissociation and reassociation of enzyme complex
Biochem. Biophys. Res. Commun.
48
1123-1128
1972
Saccharomyces cerevisiae
brenda
Sasiak, K.; Rilling, H.C.
Purification to homogeneity and some properties of squalene synthetase
Arch. Biochem. Biophys.
260
622-627
1988
Saccharomyces cerevisiae
brenda
Washburn, W.N.; Kow, R.
Investigations of substrate specificity of squalene synthase
Tetrahedron Lett.
18
1555-1558
1977
Saccharomyces cerevisiae
-
brenda
Poulter, C.D.; Capson, T.L.; Thompson, M.D.; Bard, R.S.
Squalene synthetase. Inhibition by ammonium analogues of carbocationic intermediates in the conversion of presqualene diphosphate to squalene
J. Am. Chem. Soc.
111
3734-3739
1989
Saccharomyces cerevisiae
-
brenda
Ortiz de Montellano, P.R.; Wei, J.S.; Vinson, W.A.; Castillo, R.; Boparai, A.S.
Substrate selectivity of squalene synthetase
Biochemistry
16
2680-2685
1977
Saccharomyces cerevisiae, Rattus norvegicus
brenda
McKenzie, T.L.; Jiang, G.; Straubhaar, J.R.; Conrad, D.G.; Shechter, I.
Molecular cloning, expression, and characterization of the cDNA for the rat hepatic squalene synthase
J. Biol. Chem.
267
21368-21374
1992
Rattus norvegicus
brenda
Belingheri, L.; Beyer, P.; Kleinig, H.; Gleizes, M.
Solubilization and partial purification of squalene synthase from daffodil microsomal membranes
FEBS Lett.
292
34-36
1991
Narcissus pseudonarcissus
brenda
Koyama, T.; Ogura, K.; Seto, S.
Substrate specificity of squalene synthetase
Biochim. Biophys. Acta
617
218-224
1980
Sus scrofa
brenda
Takatsuji, H.; Nishino, T.; Izui, K.; Katsuki, H.
Formation of dehydrosqualene catalyzed by squalene synthetase in Saccharomyces cerevisiae
J. Biochem.
91
911-921
1982
Saccharomyces cerevisiae, Sus scrofa
brenda
Zhang, D.; Jennnings, S.M.; Robinson, G.W.; Poulter, C.D.
Yeast squalene synthase: expression, purification, and characterization of soluble recombinant enzyme [published erratum appears in Arch Biochem Biophys 1993 Sep;305(2):622]
Arch. Biochem. Biophys.
304
133-143
1993
Saccharomyces cerevisiae
brenda
LoGrasso, P.V.; Soltis, D.A.; Boettcher, B.R.
Overexpression, purification, and kinetic characterization of a carboxyl-terminal-truncated yeast squalene synthetase
Arch. Biochem. Biophys.
307
193-199
1993
Saccharomyces cerevisiae
brenda
Ericsson, J.; Appelkvist, E.L.; Thelin, A.; Chojnacki, T.; Dallner, G.
Isoprenoid biosynthesis in rat liver peroxisomes. Characterization of cis-prenyltransferase and squalene synthetase
J. Biol. Chem.
267
18708-18714
1992
Rattus norvegicus
brenda
Hanley, K.; Chappell, J.
Solubilization, partial purification, and immunodetection of squalene synthetase from tobacco cell suspension cultures
Plant Physiol.
98
215-220
1992
Nicotiana tabacum
brenda
Shechter, I.; Klinger, E.; Rucker, M.L.; Engstrom, R.G.; Spirito, J.A.; Islam, M.A.; Boettcher, B.R.; Weinstein, D.B.
Solubilization, purification, and characterization of a truncated form of rat hepatic squalene synthetase
J. Biol. Chem.
267
8628-8635
1992
Rattus norvegicus
brenda
Shechter, I.; Bloch, K.
Solubilization and purification of trans-farnesyl pyrophosphate-squalene synthetase
J. Biol. Chem.
246
7690-7696
1971
Saccharomyces cerevisiae
brenda
Agnew, W.S.; Popjak, G.
Squalene synthetase. Stoichiometry and kinetics of presqualene pyrophosphate and squalene synthesis by yeast microsomes
J. Biol. Chem.
253
4566-4573
1978
Saccharomyces cerevisiae
brenda
Agnew, W.S.; Popjak, G.
Squalene synthetase. Solubilization from yeast microsomes of a phospholipid-requiring enzyme
J. Biol. Chem.
253
4574-4583
1978
Saccharomyces cerevisiae
brenda
Dugan, R.E.; Porter, J.W.
Hog liver squalene synthetase: the partial purification of the particulate enzyme and kinetic analysis of the reaction
Arch. Biochem. Biophys.
152
28-35
1972
Sus scrofa
brenda
Devarenne, T.P.; Shin, D.H.; Back, K.; Yin, S.; Chappell, J.
Molecular characterization of tobacco squalene synthase and regulation in response to fungal elicitor
Arch. Biochem. Biophys.
349
205-215
1998
Nicotiana tabacum
brenda
Thompson, J.F.; Danley, D.E.; Mazzalupo, S.; Milos, P.M.; Lira, M.E.; Harwood, H.J., Jr.
Truncation of human squalene synthase yields active, crystallizable protein
Arch. Biochem. Biophys.
350
283-290
1998
Homo sapiens (P37268), Homo sapiens
brenda
Okada, S.; Devarenne, T.P.; Chappell, J.
Molecular characterization of squalene synthase from the green microalga Botryococcus braunii, race B
Arch. Biochem. Biophys.
373
307-317
2000
Botryococcus braunii (Q9SDW9), Botryococcus braunii
brenda
Soltis, D.A.; McMahon, G.; Caplan, S.L.; Dudas, D.A.; Chamberlin, H.A.; Vattay, A.; Dottavio, D.; Rucker, M.L.; Engstrom, R.G.; et al.
Expression, purification, and characterization of the human squalene synthase: use of yeast and baculoviral systems
Arch. Biochem. Biophys.
316
713-723
1995
Homo sapiens
brenda
Devarenne, T.P.; Ghosh, A.; Chappell, J.
Regulation of squalene synthase, a key enzyme of sterol biosynthesis, in tobacco
Plant Physiol.
129
1095-1106
2002
Nicotiana tabacum
brenda
Mookhtiar, K.A.; Kalinowski, S.S.; Zhang, D.; Poulter, C.D.
Yeast squalene synthase. A mechanism for addition of substrates and activation by NADPH
J. Biol. Chem.
269
11201-11207
1994
Saccharomyces cerevisiae
brenda
Gu, P.; Ishii, Y.; Spencer, T.A.; Shechter, I.
Function-structure studies and identification of three enzyme domains involved in the catalytic activity in rat hepatic squalene synthase
J. Biol. Chem.
273
12515-12525
1998
Rattus norvegicus
brenda
Hayashi, H.; Hirota, A.; Hiraoka, N.; Ikeshiro, Y.
Molecular cloning and characterization of two cDNAs for Glycyrrhiza glabra squalene synthase
Biol. Pharm. Bull.
22
947-950
1999
Glycyrrhiza glabra
brenda
Tansey, T.R.; Shechter, I.
Structure and regulation of mammalian squalene synthase
Biochim. Biophys. Acta
1529
49-62
2000
Saccharomyces cerevisiae, Homo sapiens, Rattus norvegicus
brenda
Pandit, J.; Danley, D.E.; Schulte, G.K.; Mazzalupo, S.; Pauly, T.A.; Hayward, C.M.; Hamanaka, E.S.; Thompson, J.F.; Harwood, H.J., Jr.
Crystal structure of human squalene synthase. A key enzyme in cholesterol biosynthesis
J. Biol. Chem.
275
30610-30617
2000
Homo sapiens (P37268), Homo sapiens
brenda
Nakashima, T.; Inoue, T.; Oka, A.; Nishino, T.; Osumi, T.; Hata, S.
Cloning, expression, and characterization of cDNAs encoding Arabidopsis thaliana squalene synthase
Proc. Natl. Acad. Sci. USA
92
2328-2332
1995
Arabidopsis thaliana
brenda
Kroon, P.A.; Threlfall, D.R.
Squalene synthase from cell suspension cultures of Tabernaemontana divaricata
Phytochemistry
45
1157-1163
1997
Tabernaemontana divaricata
-
brenda
Zhang, D.l.; Poulter, C.D.
Biosynthesis of non-head-to-tail isoprenoids. Synthesis of 1'-1 and 1'-3 structures by recombinant yeast squalene synthase
J. Am. Chem. Soc.
117
1641-1642
1995
Saccharomyces cerevisiae
brenda
Akamine, S.; Nakamori, K.; Chechetka, S.A.; Banba, M.; Umehara, Y.; Kouchi, H.; Izui, K.; Hata, S.
cDNA cloning, mRNA expression, and mutational analysis of the squalene synthase gene of Lotus japonicus
Biochim. Biophys. Acta
1626
97-101
2003
Lotus japonicus (Q84LE3), Lotus japonicus
brenda
Ishihara, T.; Kakuta, H.; Moritani, H.; Ugawa, T.; Yanagisawa, I.
Synthesis and biological evaluation of novel propylamine derivatives as orally active squalene synthase inhibitors
Bioorg. Med. Chem.
12
5899-5908
2004
Homo sapiens, Rattus norvegicus
brenda
Orenes Lorente, S.; Gomez, R.; Jimenez, C.; Cammerer, S.; Yardley, V.; de Luca-Fradley, K.; Croft, S.L.; Ruiz Perez, L.M.; Urbina, J.; Gonzalez Pacanowska, D.; Gilbert, I.H.
Biphenylquinuclidines as inhibitors of squalene synthase and growth of parasitic protozoa
Bioorg. Med. Chem.
13
3519-3529
2005
Leishmania major
brenda
Seo, J.W.; Jeong, J.H.; Shin, C.G.; Lo, S.C.; Han, S.S.; Yu, K.W.; Harada, E.; Han, J.Y.; Choi, Y.E.
Overexpression of squalene synthase in Eleutherococcus senticosus increases phytosterol and triterpene accumulation
Phytochemistry
66
869-877
2005
Panax ginseng (O48666), Panax ginseng
brenda
Lee, M.H.; Jeong, J.H.; Seo, J.W.; Shin, C.G.; Kim, Y.S.; In, J.G.; Yang, D.C.; Yi, J.S.; Choi, Y.E.
Enhanced triterpene and phytosterol biosynthesis in Panax ginseng overexpressing squalene synthase gene
Plant Cell Physiol.
45
976-984
2004
Panax ginseng (O48666), Panax ginseng
brenda
Sealey-Cardona, M.; Cammerer, S.; Jones, S.; Ruiz-Perez, L.M.; Brun, R.; Gilbert, I.H.; Urbina, J.A.; Gonzalez-Pacanowska, D.
Kinetic characterization of squalene synthase from Trypanosoma cruzi: selective inhibition by quinuclidine derivatives
Antimicrob. Agents Chemother.
51
2123-2129
2007
Trypanosoma cruzi
brenda
Charlton-Menys, V.; Durrington, P.N.
Squalene synthase inhibitors: clinical pharmacology and cholesterol-lowering potential
Drugs
67
11-16
2007
Homo sapiens
brenda
Brusselmans, K.; Timmermans, L.; Van de Sande, T.; Van Veldhoven, P.P.; Guan, G.; Shechter, I.; Claessens, F.; Verhoeven, G.; Swinnen, J.V.
Squalene synthase, a determinant of raft-associated cholesterol and modulator of cancer cell proliferation
J. Biol. Chem.
282
18777-18785
2007
Homo sapiens
brenda
Okazaki, H.; Tazoe, F.; Okazaki, S.; Isoo, N.; Tsukamoto, K.; Sekiya, M.; Yahagi, N.; Iizuka, Y.; Ohashi, K.; Kitamine, T.; Tozawa, R.; Inaba, T.; Yagyu, H.; Okazaki, M.; Shimano, H.; Shibata, N.; Arai, H.; Nagai, R.Z.; Kadowaki, T.; Osuga, J.; Ishibashi, S.
Increased cholesterol biosynthesis and hypercholesterolemia in mice overexpressing squalene synthase in the liver
J. Lipid Res.
47
1950-1958
2006
Mus musculus
brenda
Bedi, M.; Niesen, M.; Lopez, D.
Inhibition of squalene synthase upregulates PCSK9 expression in rat liver
Arch. Biochem. Biophys.
470
116-119
2008
Rattus norvegicus
brenda
Paradise, E.M.; Kirby, J.; Chan, R.; Keasling, J.D.
Redirection of flux through the FPP branch-point in Saccharomyces cerevisiae by down-regulating squalene synthase
Biotechnol. Bioeng.
100
371-378
2008
Saccharomyces cerevisiae
brenda
Do, R.; Pare, G.; Montpetit, A.; Hudson, T.J.; Gaudet, D.; Engert, J.C.
K45R variant of squalene synthase increases total cholesterol levels in two study samples from a French Canadian population
Hum. Mutat.
29
689-694
2008
Homo sapiens
brenda
Lee, S.; Poulter, C.D.
Cloning, solubilization, and characterization of squalene synthase from Thermosynechococcus elongatus BP-1
J. Bacteriol.
190
3808-3816
2008
Thermosynechococcus vestitus
brenda
Huang, Z.; Jiang, K.; Pi, Y.; Hou, R.; Liao, Z.; Cao, Y.; Han, X.; Wang, Q.; Sun, X.; Tang, K.
Molecular cloning and characterization of the yew gene encoding squalene synthase from Taxus cuspidata
J. Biochem. Mol. Biol.
40
625-635
2007
Taxus cuspidata (A9NJG0), Taxus cuspidata
brenda
Zhao, M.W.; Liang, W.Q.; Zhang, D.B.; Wang, N.; Wang, C.G.; Pan, Y.J.
Cloning and characterization of squalene synthase (SQS) gene from Ganoderma lucidum
J. Microbiol. Biotechnol.
17
1106-1112
2007
Ganoderma lucidum (A0SJQ5), Ganoderma lucidum
brenda
Choi, S.W.; Hur, N.Y.; Ahn, S.C.; Kim, D.S.; Lee, J.K.; Kim, D.O.; Park, S.K.; Kim, B.Y.; Baik, M.Y.
Isolation and structural determination of squalene synthase inhibitor from Prunus mume fruit
J. Microbiol. Biotechnol.
17
1970-1975
2007
Sus scrofa
brenda
Busquets, A.; Keim, V.; Closa, M.; del Arco, A.; Boronat, A.; Arro, M.; Ferrer, A.
Arabidopsis thaliana contains a single gene encoding squalene synthase
Plant Mol. Biol.
67
25-36
2008
Arabidopsis thaliana (O23118), Arabidopsis thaliana (P53799), Arabidopsis thaliana
brenda
Seiki, S.; Frishman, W.H.
Pharmacologic inhibition of squalene synthase and other downstream enzymes of the cholesterol synthesis pathway: a new therapeutic approach to treatment of hypercholesterolemia
Cardiol. Rev.
17
70-76
2009
Callithrix sp., Canis lupus familiaris, Cavia porcellus, Cricetus cricetus, Homo sapiens, Macaca sp., Mus musculus, Oryctolagus cuniculus, Rattus norvegicus
brenda
Do, R.; Kiss, R.S.; Gaudet, D.; Engert, J.C.
Squalene synthase: a critical enzyme in the cholesterol biosynthesis pathway
Clin. Genet.
75
19-29
2009
Cavia porcellus, Oryctolagus cuniculus, Homo sapiens, Macaca mulatta, Mus musculus, Rattus norvegicus
brenda
Pan, J.J.; Bugni, T.S.; Poulter, C.D.
Recombinant squalene synthase. synthesis of cyclopentyl non-head-to-tail triterpenes
J. Org. Chem.
74
7562-7565
2009
Saccharomyces cerevisiae
brenda
Uchida, H.; Yamashita, H.; Kajikawa, M.; Ohyama, K.; Nakayachi, O.; Sugiyama, R.; Yamato, K.T.; Muranaka, T.; Fukuzawa, H.; Takemura, M.; Ohyama, K.
Cloning and characterization of a squalene synthase gene from a petroleum plant, Euphorbia tirucalli L
Planta
229
1243-1252
2009
Euphorbia tirucalli (B9WZW7), Euphorbia tirucalli
brenda
Calo, F.; Bondke, A.; Richardson, J.; White, A.; Barrett, A.
Total synthesis and determination of the absolute stereochemistry of the squalene synthase inhibitors CJ-13,981 and CJ-13,982
Tetrahedron Lett.
50
3388-3390
2009
Homo sapiens
-
brenda
Griebenow, N.; Flessner, T.; Buchmueller, A.; Raabe, M.; Bischoff, H.; Kolkhof, P.
Identification and optimization of tetrahydro-2H-3-benzazepin-2-ones as squalene synthase inhibitors
Bioorg. Med. Chem. Lett.
21
2554-2558
2011
Homo sapiens
brenda
Griebenow, N.; Buchmueller, A.; Kolkhof, P.; Schamberger, J.; Bischoff, H.
Identification of 4H,6H-[2]benzoxepino[4,5-c][1,2]oxazoles as novel squalene synthase inhibitors
Bioorg. Med. Chem. Lett.
21
3648-3653
2011
Homo sapiens
brenda
Ichikawa, M.; Ohtsuka, M.; Ohki, H.; Haginoya, N.; Itoh, M.; Sugita, K.; Usui, H.; Suzuki, M.; Terayama, K.; Kanda, A.
Discovery of novel tricyclic compounds as squalene synthase inhibitors
Bioorg. Med. Chem.
20
3072-3093
2012
Rattus norvegicus
brenda
Sun, Y.; Zhao, Y.; Wang, L.; Lou, H.X.; Cheng, A.X.
Cloning and expression analysis of squalene synthase, a key enzyme involved in antifungal steroidal glycoalkaloids biosynthesis from Solanum nigrum
Drug Discov. Ther.
6
242-248
2012
Solanum nigrum
brenda
Bhargava, P.; Kumar, K.; Chaudhaery, S.S.; Saxena, A.K.; Roy, U.
Cloning, overexpression and characterization of Leishmania donovani squalene synthase
FEMS Microbiol. Lett.
311
82-92
2010
Leishmania donovani (Q257D4), Leishmania donovani, Leishmania donovani MHOM/IN/80/Dd8 (Q257D4)
brenda
Liu, C.I.; Jeng, W.Y.; Chang, W.J.; Ko, T.P.; Wang, A.H.
Binding modes of zaragozic acid A to human squalene synthase and staphylococcal dehydrosqualene synthase
J. Biol. Chem.
287
18750-18757
2012
Homo sapiens
brenda
Grover, A.; Samuel, G.; Bisaria, V.S.; Sundar, D.
Enhanced withanolide production by overexpression of squalene synthase in Withania somnifera
J. Biosci. Bioeng.
115
680-685
2013
Withania somnifera
brenda
Gupta, N.; Sharma, P.; Santosh Kumar, R.J.; Vishwakarma, R.K.; Khan, B.M.
Functional characterization and differential expression studies of squalene synthase from Withania somnifera
Mol. Biol. Rep.
39
8803-8812
2012
Withania somnifera (H9L9T8), Withania somnifera
brenda
Kalra, S.; Kumar, S.; Lakhanpal, N.; Kaur, J.; Singh, K.
Characterization of Squalene synthase Gene from Chlorophytum borivilianum (Sant. and Fernand.)
Mol. Biotechnol.
54
944-953
2013
Chlorophytum borivilianum (I6Z427), Chlorophytum borivilianum
brenda
Kim, Y.S.; Cho, J.H.; Park, S.; Han, J.Y.; Back, K.; Choi, Y.E.
Gene regulation patterns in triterpene biosynthetic pathway driven by overexpression of squalene synthase and methyl jasmonate elicitation in Bupleurum falcatum
Planta
233
343-355
2011
Bupleurum falcatum (Q32R64), Bupleurum falcatum
brenda
Ginzberg, I.; Thippeswamy, M.; Fogelman, E.; Demirel, U.; Mweetwa, A.M.; Tokuhisa, J.; Veilleux, R.E.
Induction of potato steroidal glycoalkaloid biosynthetic pathway by overexpression of cDNA encoding primary metabolism HMG-CoA reductase and squalene synthase
Planta
235
1341-1353
2012
Solanum tuberosum (Q9XJ31), Solanum tuberosum, Solanum tuberosum Desiree (Q9XJ31)
brenda
Liu, C.I.; Jeng, W.Y.; Chang, W.J.; Shih, M.F.; Ko, T.P.; Wang, A.H.
Structural insights into the catalytic mechanism of human squalene synthase
Acta Crystallogr. Sect. D
70
231-241
2014
Homo sapiens (P37268), Homo sapiens
brenda
Shiuan, D.; Chen, Y.H.; Lin, H.K.; Huang, K.J.; Tai, D.F.; Chang, D.K.
Discovering peptide inhibitors of human squalene synthase through screening the phage-displayed cyclic peptide c7c library
Appl. Biochem. Biotechnol.
179
597-609
2016
Homo sapiens (P37268), Homo sapiens
brenda
Linscott, K.B.; Niehaus, T.D.; Zhuang, X.; Bell, S.A.; Chappell, J.
Mapping a kingdom-specific functional domain of squalene synthase
Biochim. Biophys. Acta
1861
1049-1057
2016
Arabidopsis thaliana, Homo sapiens (P37268), Saccharomyces cerevisiae (P53866), Saccharomyces cerevisiae, Botryococcus braunii (Q9SDW9)
brenda
Ohtake, K.; Saito, N.; Shibuya, S.; Kobayashi, W.; Amano, R.; Hirai, T.; Sasaki, S.; Nakano, C.; Hoshino, T.
Biochemical characterization of the water-soluble squalene synthase from Methylococcus capsulatus and the functional analyses of its two DXXD(E)D motifs and the highly conserved aromatic amino acid residues
FEBS J.
281
5479-5497
2014
Methylococcus capsulatus (Q60AN4), Methylococcus capsulatus
brenda
Furubayashi, M.; Li, L.; Katabami, A.; Saito, K.; Umeno, D.
Directed evolution of squalene synthase for dehydrosqualene biosynthesis
FEBS Lett.
588
3375-3381
2014
Thermosynechococcus vestitus, Homo sapiens (P37268), Homo sapiens, Saccharomyces cerevisiae (P53866), Saccharomyces cerevisiae
brenda
Katabami, A.; Li, L.; Iwasaki, M.; Furubayashi, M.; Saito, K.; Umeno, D.
Production of squalene by squalene synthases and their truncated mutants in Escherichia coli
J. Biosci. Bioeng.
119
165-171
2015
Thermosynechococcus vestitus, Homo sapiens (P37268), Homo sapiens
brenda
Huang, D.; Yao, Y.; Zhang, H.; Mei, Z.; Wang, R.; Feng, L.; Liu, B.
Directed optimization of a newly identified squalene synthase from Mortierella alpine based on sequence truncation and site-directed mutagenesis
J. Ind. Microbiol. Biotechnol.
42
1341-1352
2015
Mortierella alpina (A0A0K2F2K4), Mortierella alpina, Mortierella alpina ATCC 32222 (A0A0K2F2K4)
brenda
Hong, W.K.; Heo, S.Y.; Park, H.M.; Kim, C.H.; Sohn, J.H.; Kondo, A.; Seo, J.W.
Characterization of a squalene synthase from the thraustochytrid microalga Aurantiochytrium sp. KRS101
J. Microbiol. Biotechnol.
23
759-765
2013
Aurantiochytrium sp. KRS101 (U3KZM8)
brenda
Saito, K.; Shirasago, Y.; Suzuki, T.; Aizaki, H.; Hanada, K.; Wakita, T.; Nishijima, M.; Fukasawa, M.
Targeting cellular squalene synthase, an enzyme essential for cholesterol biosynthesis, is a potential antiviral strategy against hepatitis C virus
J. Virol.
89
2220-2232
2015
Homo sapiens (P37268), Homo sapiens
brenda
Sanchita, S.; Singh, G.; Sharma, A.
In silico study of binding motifs in squalene synthase enzyme of secondary metabolic pathway of Solanaceae [corrected]
Mol. Biol. Rep.
41
7201-7208
2014
Withania somnifera (H9L9T8), Withania somnifera
brenda
Patel, N.; Patel, P.; Kendurkar, S.; Thulasiram, H.; Khan, B.
Overexpression of squalene synthase in Withania somnifera leads to enhanced withanolide biosynthesis
Plant Cell Tissue Organ Cult.
122
409-420
2015
Withania somnifera (H9L9T8)
-
brenda
Kajikawa, M.; Kinohira, S.; Ando, A.; Shimoyama, M.; Kato, M.; Fukuzawa, H.
Accumulation of squalene in a microalga Chlamydomonas reinhardtii by genetic modification of squalene synthase and squalene epoxidase genes
PLoS ONE
10
e0120446
2015
Chlamydomonas reinhardtii
brenda
Zha, L.; Liu, S.; Su, P.; Yuan, Y.; Huang, L.
Cloning, prokaryotic expression and functional analysis of squalene synthase (SQS) in Magnolia officinalis
Protein Expr. Purif.
120
28-34
2016
Magnolia officinalis (A0A140DJS0), Magnolia officinalis
brenda
Lee, P.Y.; Yong, V.C.; Rosli, R.; Gam, L.H.; Chong, P.P.
Cloning, expression and purification of squalene synthase from Candida tropicalis in Pichia pastoris
Protein Expr. Purif.
94
15-21
2014
Candida tropicalis (C5M7M6), Candida tropicalis, Candida tropicalis ATCC MYA-3404 (C5M7M6)
brenda
Filiz, E.; Ozyigit, I.; Vatansever, R.
Comparative analyses of squalene synthase (SQS) proteins in poplar and pine by using bioinformatics tools
Tree Genet. Genomes
12
32
2016
Populus trichocarpa (B9HRH0), Pinus massoniana (W6D7A6)
-
brenda
Bell, S.A.; Niehaus, T.D.; Nybo, S.E.; Chappell, J.
Structure-function mapping of key determinants for hydrocarbon biosynthesis by squalene and squalene synthase-like enzymes from the green alga Botryococcus braunii race B
Biochemistry
53
7570-7581
2014
Botryococcus braunii (Q9SDW9), Botryococcus braunii
brenda
Zhao, H.; Tang, Q.; Mo, C.; Bai, L.; Tu, D.; Ma, X.
Cloning and characterization of squalene synthase and cycloartenol synthase from Siraitia grosvenorii
Acta Pharm. Sin. B
7
215-222
2017
Siraitia grosvenorii (K7NBW9), Siraitia grosvenorii
brenda
Song, J.; Shang, N.; Baig, N.; Yao, J.; Shin, C.; Kim, B.K.; Li, Q.; Malwal, S.R.; Oldfield, E.; Feng, X.; Guo, R.T.
Aspergillus flavus squalene synthase as an antifungal target Expression, activity, and inhibition
Biochem. Biophys. Res. Commun.
512
517-523
2019
Aspergillus flavus (A0A2P2GY60), Aspergillus flavus, Aspergillus flavus AF70 (A0A2P2GY60)
brenda
Su, H.; Liu, Y.; Xiao, Y.; Tan, Y.; Gu, Y.; Liang, B.; Huang, H.; Wu, Y.
Molecular and biochemical characterization of squalene synthase from Siraitia grosvenorii
Biotechnol. Lett.
39
1009-1018
2017
Siraitia grosvenorii (A0A192YD12), Siraitia grosvenorii
brenda
Liu, G.; Fu, J.
Squalene synthase cloning and functional identification in wintersweet plant (Chimonanthus zhejiangensis)
Bot. Stud.
59
30
2018
Chimonanthus grammatus, Chimonanthus zhejiangensis (A0A3G3C7U6), Chimonanthus zhejiangensis, Chimonanthus salicifolius (A0A3G3C7V3)
brenda
Katselou, M.G.; Matralis, A.N.; Kourounakis, A.P.
Developing potential agents against atherosclerosis Design, synthesis and pharmacological evaluation of novel dual inhibitors of oxidative stress and squalene synthase activity
Eur. J. Med. Chem.
138
748-760
2017
Rattus norvegicus (Q02769)
brenda
Rong, Q.; Jiang, D.; Chen, Y.; Shen, Y.; Yuan, Q.; Lin, H.; Zha, L.; Zhang, Y.; Huang, L.
Molecular cloning and functional analysis of squalene synthase 2(SQS2) in Salvia miltiorrhiza Bunge
Front. Plant Sci.
7
1274
2016
Salvia miltiorrhiza (M4H1H3), Salvia miltiorrhiza
brenda
Jiang, D.; Rong, Q.; Chen, Y.; Yuan, Q.; Shen, Y.; Guo, J.; Yang, Y.; Zha, L.; Wu, H.; Huang, L.; Liu, C.
Molecular cloning and functional analysis of squalene synthase (SS) in Panax notoginseng
Int. J. Biol. Macromol.
95
658-666
2017
Panax notoginseng
brenda
Pattanaik, B.; Englund, E.; Nolte, N.; Lindberg, P.
Introduction of a green algal squalene synthase enhances squalene accumulation in a strain of Synechocystis sp. PCC 6803
Metab. Eng. Commun.
10
e00125
2020
Botryococcus braunii (Q9SDW9), Botryococcus braunii
brenda
Chen, Y.; Chen, X.; Luo, G.; Zhang, X.; Lu, F.; Qiao, L.; He, W.; Li, G.; Zhang, Y.
Discovery of potential inhibitors of squalene synthase from traditional Chinese medicine based on virtual screening and in vitro evaluation of lipid-lowering effect
Molecules
23
1040
2018
Homo sapiens (P37268)
brenda
Zhang, B.; Liu, Y.; Chen, M.; Feng, J.; Ma, Z.; Zhang, X.; Zhu, C.
Cloning, expression analysis and functional characterization of squalene synthase (SQS) from Tripterygium wilfordii
Molecules
23
269
2018
Tripterygium wilfordii (A0A142IKD0), Tripterygium wilfordii
brenda
Macias-Alonso, M.; Andres, L.S.; Cordova-Guerrero, I.; Estolano-Cobian, A.; Diaz-Rubio, L.; Marrero, J.G.
Inhibition of squalene synthase of rat liver by abietane diterpenes derivatives
Nat. Prod. Res.
35
2972-2976
2019
Rattus norvegicus (Q02769)
brenda
Unland, K.; Puetter, K.M.; Vorwerk, K.; van Deenen, N.; Twyman, R.M.; Pruefer, D.; Schulze Gronover, C.
Functional characterization of squalene synthase and squalene epoxidase in Taraxacum koksaghyz
Plant Direct
2
e00063
2018
Taraxacum kok-saghyz (A0A3G1SVP2)
brenda