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Information on EC 2.5.1.21 - squalene synthase
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2.5.1.21 squalene synthaseIUBMB Comments
This microsomal enzyme catalyses the first committed step in the biosynthesis of sterols. The enzyme from yeast requires either Mg2+ or Mn2+ for activity. In the absence of NAD(P)H, presqualene diphosphate (PSPP) is accumulated. When NAD(P)H is present, presqualene diphosphate does not dissociate from the enzyme during the synthesis of squalene from farnesyl diphosphate (FPP) . High concentrations of FPP inhibit the production of squalene but not of PSPP .
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Word Map
- 2.5.1.21
-
farnesylation
- cholesterol
- sterol
-
prenylation
- ftase
-
isoprenoids
- mevalonate
-
geranylgeranylation
-
geranylgeranyltransferase
- pyrophosphate
- leukemia
- tipifarnib
- hmg-coa
- statin
-
epoxidase
-
peptidomimetic
- prenyltransferase
- h-ras
- farnesol
-
prelamin
- manumycin
- lanosterol
- lovastatin
-
p21ras
- lamins
-
triterpenoids
-
farnesylpyrophosphate
- dolichols
- rhob
-
hutchinson-gilford
-
3-hydroxy-3-methylglutaryl
-
isoprenylation
-
myelodysplastic
-
cholesterol-lowering
- ergosterol
-
triterpene
-
ras-dependent
-
ras-transformed
- geranylgeraniol
- cycloartenol
- cis-prenyltransferase
- 2,3-oxidosqualene
-
nonsterols
-
non-thiol
- oxidosqualene
- synthesis
-
progerin
-
ganoderic
- industry
-
ras-mediated
- phytosterols
- drug development
- srebp-2
- medicine
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
BbSS, CrSQS, dt-ySQase, Erg9, EtSS, farnesyl-diphosphate farnesyltransferase, farnesyl-diphosphate:farnesyldiphosphate farnesyltransferase, farnesyldiphosphate farnesyltransferase 1, farnesyldiphosphate:farnesyldiphosphate farnesyltransferase, farnesyltransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Erg9
farnesyl-diphosphate farnesyltransferase
farnesyldiphosphate farnesyltransferase 1
farnesyldiphosphate:farnesyldiphosphate farnesyltransferase
-
-
-
-
farnesyltransferase
-
-
-
-
FDFT1
presqualene synthase
-
-
-
-
presqualene-diphosphate synthase
-
-
-
-
SQS
SQS1
squalene synthase
squalene synthase 1
squalene synthetase
-
-
-
-
SSN
synthase, squalene
-
-
-
-
farnesyl-diphosphate farnesyltransferase
-
-
-
-
squalene synthase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 (2E,6E)-farnesyl diphosphate = diphosphate + presqualene diphosphate
; 1a
-
-
-
presqualene diphosphate + NAD(P)H + H+ = squalene + diphosphate + NAD(P)+
; 1b
-
-
-
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)+
mechanism
-
2 (2E,6E)-farnesyl diphosphate + NAD(P)H + H+ = squalene + 2 diphosphate + NAD(P)+
enzyme also catalyses the reduction of presqualene diphosphate by NADPH to squalene
-
2 (2E,6E)-farnesyl diphosphate + NAD(P)H + H+ = squalene + 2 diphosphate + NAD(P)+
enzyme also catalyses the reduction of presqualene diphosphate by NADPH to squalene; mechanism
-
2 (2E,6E)-farnesyl diphosphate + NAD(P)H + H+ = squalene + 2 diphosphate + NAD(P)+
overview mechanism, kinetics
-
2 (2E,6E)-farnesyl diphosphate + NAD(P)H + H+ = squalene + 2 diphosphate + NAD(P)+
mechanism
2 (2E,6E)-farnesyl diphosphate + NAD(P)H + H+ = squalene + 2 diphosphate + NAD(P)+
enzyme also catalyses the reduction of presqualene diphosphate by NADPH to squalene
-
2 (2E,6E)-farnesyl diphosphate + NAD(P)H + H+ = squalene + 2 diphosphate + NAD(P)+
enzyme also catalyses the reduction of presqualene diphosphate by NADPH to squalene
-
2 (2E,6E)-farnesyl diphosphate + NAD(P)H + H+ = squalene + 2 diphosphate + NAD(P)+
overall reaction, reaction mechanism, overview
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
alkenyl group transfer
-
-
-
-
reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl-diphosphate:(2E,6E)-farnesyl-diphosphate farnesyltransferase
This microsomal enzyme catalyses the first committed step in the biosynthesis of sterols. The enzyme from yeast requires either Mg2+ or Mn2+ for activity. In the absence of NAD(P)H, presqualene diphosphate (PSPP) is accumulated. When NAD(P)H is present, presqualene diphosphate does not dissociate from the enzyme during the synthesis of squalene from farnesyl diphosphate (FPP) [8]. High concentrations of FPP inhibit the production of squalene but not of PSPP [8].
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CAS REGISTRY NUMBER
COMMENTARY
9077-14-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(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
-
-
?
(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
-
?
farnesyl diphosphate + NADPH + H+
squalene + diphosphate + NADP+
-
-
sole product
-
?
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 + 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+
-
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+
-
-
-
?
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+
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+
-
-
-
?
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
-
assay at pH 7.2, 30°C, 3 h
-
-
?
2 farnesyl diphosphate
presqualene diphosphate + diphosphate
-
-
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 + 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 + 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+
-
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
?
-
analysis of substrate specificity, overview
-
-
-
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
?
-
enzyme is key regulator not only for phytosterol but also for triterpene biosynthesis
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
reaction is completely regioselective
-
-
-
additional information
?
-
-
no substrate: 6,7-dihydrofarnesyl diphosphate, 3-desmethylfarnesyl diphosphate
-
-
-
additional information
?
-
-
not metabolized: (E)-6,7,10,11-tetrahydrofarnesyl diphosphate
-
-
-
additional information
?
-
-
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 (2E,6E)-farnesyl diphosphate
diphosphate + presqualene diphosphate
-
first half-reaction
-
-
?
2 (2E,6E)-farnesyl diphosphate
diphosphate + presqualene diphosphate
-
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
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
-
first pathway-specific enzyme in cholesterol biosynthesis
-
-
-
farnesyl diphosphate + farnesyl diphosphate
diphosphate + presqualene diphosphate
-
essential enzyme in cholesterol biosynthetic pathway
-
-
-
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 + 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
?
-
-
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
?
-
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.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
additional information
-
squalene synthase is a divalent metal-ion-dependent enzyme
Mg2+
the aspartate side chains are involved in binding multiple Mg2? ions that stabilize binding of diphosphate groups in the substrate
Mg2+
-
Mn2+ is more effective than Mg2+ in activation of dehydrosqualene formation; most effective in stimulation of squalene formation, half-maximal activity at 2.5 mM
Mg2+
-
Mn2+ is more effective than Mg2+ in activation of dehydrosqualene formation; required for squalene synthase reaction
Mg2+
required, 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
Mn2+
-
more effective than Mg2+ in activation of dehydrosqualene formation
Mn2+
-
in presence of Mn2+ and Mg2+ the activity is reduced to one-third of that in presence of Mn2+ alone; six times more effective in activation than Mg2+
Mn2+
-
more effective than Mg2+ in activation of dehydrosqualene formation; stimulates, maximum stimulation at 0.1 mM
Mn2+
-
in presence of Mn2+ and Mg2+ the activity is reduced to one-third of that in presence of Mn2+ alone; stimulation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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
-
-
(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
-
-
(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
-
-
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
-
-
1-allyl-2-(3-anilinopropoxy)-9H-carbazole
-
50% inhibition at above 0.001 mM 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-[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
-
-
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-([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-[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-(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-([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-[(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-[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
-
-
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-[[(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
-
-
[(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 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
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
farnesyl diphosphate
-
no inhibition of presqualene diphosphate synthase reaction; substrate inhibitor of squalene synthase reaction
farnesyl diphosphate
-
substrate inhibitor of squalene synthase reaction
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
YM-53601
-
reduction of non-high-density lipoprotein cholesterol concentrations
YM-53601
-
reduction of non-high-density lipoprotein cholesterol concentrations
zaragozic acid
-
hypolipidemic effects but potential toxicity because of high levels of urinary dicarboxylic acid
zaragozic acid
-
hypolipidemic effects but potential toxicity because of high levels of urinary dicarboxylic acid
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
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0052
(2E,6E)-farnesyl diphosphate
pH 7.2, 37°C, recombinant mutant enzyme
0.0134
(2E,6E)-farnesyl diphosphate
pH 8.0, 33°C, recombinant enzyme
0.00525
farnesyl diphosphate
-
in 50 mM morpholinepropanesulfonic acid-NaOH buffer (pH 7.4), 20 mM MgCl2, 5 mM 3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate, 1% Tween 80, 10 mM dithiothreitol, 0.025 mg/ml bovine serum albumin, 0.25 mM NADPH, at 37°C
0.02334
NADPH
-
in 50 mM morpholinepropanesulfonic acid-NaOH buffer (pH 7.4), 20 mM MgCl2, 5 mM 3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate, 1% Tween 80, 10 mM dithiothreitol, 0.025 mg/ml bovine serum albumin, 0.25 mM NADPH, at 37°C
additional information
additional information
-
kinetics, recombinant LdSSN, overview
-
additional information
additional information
kinetics, recombinant LdSSN, overview
-
additional information
additional information
-
Michaelis-Menten kinetic analysis
-
additional information
additional information
Michaelis-Menten kinetic analysis
-
additional information
additional information
Michaelis-Menten kinetic model
-
additional information
additional information
-
Michaelis-Menten kinetic model
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.478
(2E,6E)-farnesyl diphosphate
pH 8.0, 33°C, recombinant enzyme
0.48
(2E,6E)-farnesyl diphosphate
pH 7.2, 37°C, recombinant mutant E186K enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
35.05
(2E,6E)-farnesyl diphosphate
pH 8.0, 33°C, recombinant enzyme
90
(2E,6E)-farnesyl diphosphate
pH 7.2, 37°C, recombinant mutant E186K enzyme
510
(2E,6E)-farnesyl diphosphate
-
pH and temperature not specified in the publication, recombinant enzyme
1800
(2E,6E)-farnesyl diphosphate
-
pH and temperature not specified in the publication, recombinant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.000007
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
0.0000023
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
0.000004
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
0.0000016
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
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
0.00022
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
0.0153
[(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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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.2 - 8.2
-
pH 5.2: about 45% of maximum activity, pH 8.2: about 75% of maximum activity
6 - 9
activity range, over 90% of maximal activity at pH 7.0-8.0, 30% at pH 6.0, 20% at pH 9.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
collected in autumn 2014, from Qianshan County in Anhui Province, China, gene MoSQS
UniProt
brenda
isoform Sqs1. Sqs1 is the only functional squalene synthase in Arabidopsis thaliana. Isoform Sqs2 has no squalene synthase activity
UniProt
brenda
isoform Sqs2, lacking enzymatic activity due to the presence of an unusual Ser replacing the highly conserved Phe at position 287
O23118
UniProt
brenda
-
-
-
brenda
overexpression 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
Uniprot
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
expression level is relatively low in mycelia incubated for 12 days, increases after 14 to 20 days of incubation, and reaches a relatively high level in the mushroom primordia
brenda
expression level is relatively low in mycelia incubated for 12 days, increases after 14 to 20 days of incubation, and reaches a relatively high level in the mushroom primordia
brenda
additional information
induction of enzyme by methyl jasmonate treatment, enhanced activity results in increase in phytosterols as well as ginsenoside contents
brenda
additional information
O23118
isoform Sqs1 is widely expressed in all tissues throughout plant development
brenda
additional information
isoform Sqs1 is widely expressed in all tissues throughout plant development
brenda
additional information
-
SqS expression is 14.3% higher in leaves compared to roots, semi-quantitative RT-PCR expression analysis, ovverview. CbSqS shows distinct pattern of expression in leaf and root tissues
brenda
additional information
SqS expression is 14.3% higher in leaves compared to roots, semi-quantitative RT-PCR expression analysis, ovverview. CbSqS shows distinct pattern of expression in leaf and root tissues
brenda
additional information
-
tissue real-time RTPCR expression analysis, the enzyme is expressed constitutively in all tested tissues, with the highest expression in stems
brenda
additional information
constitutive expression in all tissues examined
brenda
additional information
-
constitutive expression in all tissues examined
brenda
additional information
quantitative real-time PCR tissue expression analysis, overview. WsSQS expresses more in young leaves than mature leaves, stem and root
brenda
additional information
the age and type of donor tissue play crucial roles in the biochemistry of subsequent cultures lines. In vitro cultures have differential capacity to synthesize secondary metabolites depending on the morphological nature of type of explant utilized
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
O23118, P53799
localization depends on the protein's N-terminal hydrophobic transmembrane domain
brenda
associated enzyme with C-terminus anchored in the endoplasmic reticulum membrane and the N-terminus including active site is exposed in the cytosol
brenda
-
squalene synthase consists of both an N-terminal catalytic domain and a C-terminal domain tethering the enzyme to the endoplasmic reticulum membrane
brenda
squalene synthase consists of both an N-terminal catalytic domain and a C-terminal domain tethering the enzyme to the endoplasmic reticulum membrane
brenda
-
CrSQS protein has two putative transmembrane domains at the C-terminus, Phe398-Glu420 and Gln436-Leu458
brenda
squalene synthase consists of both an N-terminal catalytic domain and a C-terminal domain tethering the enzyme to the endoplasmic reticulum membrane
brenda
squalene synthase consists of both an N-terminal catalytic domain and a C-terminal domain which consists of a hinge region and a membrane spanning helix responsible for tethering the enzyme to the cytosolic face of the endoplasmic reticulum
brenda
-
bound, the membrane-binding domains of the human enzyme are 30 residues of the N-terminus and 47 residues of the C-terminus
brenda
-
model of the secondary structure and its possible membrane orientation
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
the enzyme belongs to the isoprenoid biosynthesis enzymes class 1 superfamily
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
-
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
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
malfunction
enzyme overexpression in transgenic Withania somnifera plants affects the shoot elongation and multiplication, phenotype, overview
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 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 a key enzyme in the regulation of isoprenoid biosynthesis and is important in the withanolides biosynthesis pathway, overview
metabolism
squalene synthase is the key enzyme of saponin biosynthesis pathway
metabolism
squalene synthase catalyzes the first enzymatic step of the central isoprenoid pathway in sterol and triterpenoid biosynthesis
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
-
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 is a key enzyme in the isoprenoid biosynthesis
metabolism
the enzyme catalyzes the first dedicated step in the biosynthesis of sterols and other triterpenoids
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
-
the enzyme is involved in squalene synthesis and sterol metabolism
metabolism
-
squalene synthase is a major enzyme in the sterol biosynthetic pathway
-
metabolism
-
the enzyme is a key enzyme in the isoprenoid biosynthesis
-
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
-
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
-
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
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
-
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
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
-
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
-
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
the hinge domain plays an essential functional role, such as assembly of ergosterol multi-enzymecomplexes in fungi
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
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
homology modelling of SQS enzyme of Withania somnifera for the prediction of three-dimensional structure, molecular docking study of considered substrates, 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
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
-
Show AA Sequence and Transmembrane Helices (1519 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Trypanosoma cruzi (strain CL Brener)