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2 (2E,6E)-farnesyl diphosphate
15-cis-4,4'-diapophytoene + 2 diphosphate
2 (2E,6E)-farnesyl diphosphate
cis-4,4'-diapophytoene + 2 diphosphate
2 (2E,6E)-farnesyl diphosphate
presqualene diphosphate + diphosphate
presqualene diphosphate
15-cis-4,4'-diapophytoene + diphosphate
additional information
?
-
2 (2E,6E)-farnesyl diphosphate
15-cis-4,4'-diapophytoene + 2 diphosphate
-
-
-
-
?
2 (2E,6E)-farnesyl diphosphate
15-cis-4,4'-diapophytoene + 2 diphosphate
-
-
-
-
?
2 (2E,6E)-farnesyl diphosphate
15-cis-4,4'-diapophytoene + 2 diphosphate
-
-
-
-
?
2 (2E,6E)-farnesyl diphosphate
15-cis-4,4'-diapophytoene + 2 diphosphate
-
-
-
-
?
2 (2E,6E)-farnesyl diphosphate
15-cis-4,4'-diapophytoene + 2 diphosphate
-
-
-
-
?
2 (2E,6E)-farnesyl diphosphate
15-cis-4,4'-diapophytoene + 2 diphosphate
-
-
-
-
?
2 (2E,6E)-farnesyl diphosphate
15-cis-4,4'-diapophytoene + 2 diphosphate
Thermosynechococcus vestitus
-
-
-
-
?
2 (2E,6E)-farnesyl diphosphate
cis-4,4'-diapophytoene + 2 diphosphate
-
-
-
?
2 (2E,6E)-farnesyl diphosphate
cis-4,4'-diapophytoene + 2 diphosphate
-
-
-
?
2 (2E,6E)-farnesyl diphosphate
cis-4,4'-diapophytoene + 2 diphosphate
-
-
-
-
?
2 (2E,6E)-farnesyl diphosphate
cis-4,4'-diapophytoene + 2 diphosphate
-
-
-
?
2 (2E,6E)-farnesyl diphosphate
cis-4,4'-diapophytoene + 2 diphosphate
-
-
-
?
2 (2E,6E)-farnesyl diphosphate
presqualene diphosphate + diphosphate
-
-
-
-
?
2 (2E,6E)-farnesyl diphosphate
presqualene diphosphate + diphosphate
-
-
-
-
?
presqualene diphosphate
15-cis-4,4'-diapophytoene + diphosphate
-
-
-
-
?
presqualene diphosphate
15-cis-4,4'-diapophytoene + diphosphate
-
-
-
-
?
additional information
?
-
-
reaction mechanism of squalene and dehydrosqualene formation and their conversion into carotenoid pigments, overview
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-
?
additional information
?
-
-
reaction mechanism of squalene and dehydrosqualene formation and their conversion into carotenoid pigments, overview
-
-
?
additional information
?
-
Thermosynechococcus vestitus
-
reaction mechanism of squalene and dehydrosqualene formation and their conversion into carotenoid pigments, overview
-
-
?
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2 (2E,6E)-farnesyl diphosphate
15-cis-4,4'-diapophytoene + 2 diphosphate
2 (2E,6E)-farnesyl diphosphate
presqualene diphosphate + diphosphate
presqualene diphosphate
15-cis-4,4'-diapophytoene + diphosphate
additional information
?
-
2 (2E,6E)-farnesyl diphosphate
15-cis-4,4'-diapophytoene + 2 diphosphate
-
-
-
-
?
2 (2E,6E)-farnesyl diphosphate
15-cis-4,4'-diapophytoene + 2 diphosphate
-
-
-
-
?
2 (2E,6E)-farnesyl diphosphate
15-cis-4,4'-diapophytoene + 2 diphosphate
-
-
-
-
?
2 (2E,6E)-farnesyl diphosphate
15-cis-4,4'-diapophytoene + 2 diphosphate
-
-
-
-
?
2 (2E,6E)-farnesyl diphosphate
15-cis-4,4'-diapophytoene + 2 diphosphate
-
-
-
-
?
2 (2E,6E)-farnesyl diphosphate
15-cis-4,4'-diapophytoene + 2 diphosphate
-
-
-
-
?
2 (2E,6E)-farnesyl diphosphate
15-cis-4,4'-diapophytoene + 2 diphosphate
Thermosynechococcus vestitus
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-
-
-
?
2 (2E,6E)-farnesyl diphosphate
presqualene diphosphate + diphosphate
-
-
-
-
?
2 (2E,6E)-farnesyl diphosphate
presqualene diphosphate + diphosphate
-
-
-
-
?
presqualene diphosphate
15-cis-4,4'-diapophytoene + diphosphate
-
-
-
-
?
presqualene diphosphate
15-cis-4,4'-diapophytoene + diphosphate
-
-
-
-
?
additional information
?
-
-
reaction mechanism of squalene and dehydrosqualene formation and their conversion into carotenoid pigments, overview
-
-
?
additional information
?
-
-
reaction mechanism of squalene and dehydrosqualene formation and their conversion into carotenoid pigments, overview
-
-
?
additional information
?
-
Thermosynechococcus vestitus
-
reaction mechanism of squalene and dehydrosqualene formation and their conversion into carotenoid pigments, overview
-
-
?
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(3R)-3-biphenyl-4-yl-1-azabicyclo[2.2.2]octan-3-ol
i.e. BPH-651, forms two crystal structures in complex with the enzyme. In both, the quinuclidine headgroup binds in the allylic S1 site with the side chain in S2, but in the presence of diphosphate and Mg2+, the quinuclidine's cationic center interacts with diphosphate and three Mg2+, mimicking a transition state involved in diphosphate ionization
(S)-1-phosphono-4-(3-phenoxyphenyl)butylsulfonic acid
far more active than (R)-compound both in vitro an in cells
([[(E)-[[(3E)-4,8-dimethylnona-3,7-dien-1-yl](methyl)iminio]methyl]amino]methyl)(phosphonomethyl)phosphinate
-
competitive inhibitor
1-phosphono-4-[3-(3,4-difluorophenoxy)phenyl]butylsulfonic acid
-
1-phosphono-4-[3-(3-fluorophenoxy)phenyl]butylsulfonic acid
-
1-phosphono-4-[3-(4-fluorophenoxy)phenyl]butylsulfonic acid
-
1-phosphono-4-[3-(4-propylphenoxy)phenyl]butylsulfonic acid
potent inhibitor in cell-based assay
2-(4-phenoxyphenoxy)ethyl thiocyanate
i.e. WC-9, binds to the S2 site with its -SCN group surrounded by four hydrogen bond donors
4-(3-phenoxyphenyl)-1-phosphonobutane-1-sulfonic acid
i.e. BPH-652
4-(4'-butylbiphenyl-4-yl)-1-phosphonobutane-1-sulfonic acid
i.e. BPH-698
4-(4-biphenyl)butyldiphosphonic acid
4-(biphenyl-4-yl)-1-phosphonobutane-1-sulfonic acid
i.e. BPH-700
4-[4-(4-trifluoromethylphenyl)phenyl]butyldiphosphonic acid
-
lapaquistat acetate
-
docking analysis, interaction with residues H18, R45, D48, D52, Y129, Q165, N168 and D172
N-[(2E)-3,7-dimethylocta-2,6-dien-1-yl]-N'-[(1R,3S,5R,7R)-tricyclo[3.3.1.1-3,7-]dec-2-yl]ethane-1,2-diamine
i.e. SQ-109, forms two crystal structurs in complex with the enzyme. In one, the geranyl side chain binds to either S1 or S2 and the adamantane headgroup binds to S1. In the second, the side chain binds to S2 while the headgroup binds to S1
squalestatin
-
docking analysis, interaction with residues H18, R45, D48, D52, Y129, Q165, N168 and D172
zaragozic acid A
-
crystallization data of complex
[([(E)-amino[(4,8-dimethylnonyl)(methyl)iminio]methyl]amino)methyl](phosphonomethyl)phosphinate
-
competitive inhibitor
[[([[(4,8-dimethylnonyl)(methyl)carbamoyl]amino]methyl)(hydroxy)phosphoryl]methyl]phosphonic acid
-
competitive inhibitor
4-(4-biphenyl)butyldiphosphonic acid
-
4-(4-biphenyl)butyldiphosphonic acid
i.e. BPH-674
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malfunction
-
a mutant of squalene synthase is converted to a dehydrosqualene synthase, the various mutations are lustered around the residues that are proposed to be important for NADPH binding
malfunction
-
a mutant of squalene synthase is converted to a dehydrosqualene synthase, the various mutations are lustered around the residues that are proposed to be important for NADPH binding
malfunction
Thermosynechococcus vestitus
-
a mutant of squalene synthase is converted to a dehydrosqualene synthase, the various mutations are lustered around the residues that are proposed to be important for NADPH binding
metabolism
-
Bacillus firmus synthesizes C30 carotenoids via farnesyl pyrophosphate, forming apophytoene as the first committed step in the pathway. The products of the pathway is methyl 4'-[(6-O-acyl-glycosyl)oxy]-4,4'-diapolycopen-4-oic acid and 4,4'-diapolycopen-4,4'-dioic acid with putative glycosyl esters
metabolism
-
Bacillus indicus synthesizes C30 carotenoids via farnesyl pyrophosphate, forming apophytoene as the first committed step in the pathway. The products of the pathway is methyl 4'-[(6-O-acyl-glycosyl)oxy]-4,4'-diapolycopen-4-oic acid and 4,4'-diapolycopen-4,4'-dioic acid with putative glycosyl esters
metabolism
-
Bacillus indicus synthesizes C30 carotenoids via farnesyl pyrophosphate, forming apophytoene as the first committed step in the pathway. The products of the pathway is methyl 4'-[(6-O-acyl-glycosyl)oxy]-4,4'-diapolycopen-4-oic acid and 4,4'-diapolycopen-4,4'-dioic acid with putative glycosyl esters
-
metabolism
-
Bacillus firmus synthesizes C30 carotenoids via farnesyl pyrophosphate, forming apophytoene as the first committed step in the pathway. The products of the pathway is methyl 4'-[(6-O-acyl-glycosyl)oxy]-4,4'-diapolycopen-4-oic acid and 4,4'-diapolycopen-4,4'-dioic acid with putative glycosyl esters
-
physiological function
the biosynthesis of 4,4'-diaponeurosporene starts with the condensation of two molecules of farnesyl diphosphate by dehydrosqualene synthase CrtM, the reaction product of this enzyme is dehydrosqualene and not squalene. Dehydrosqualene, i.e.4,4'-diapophytoene, is successively dehydrogenated by desaturase CrtN to form the yellow main intermediate 4,4'-diaponeurosporene
physiological function
-
the biosynthesis of 4,4'-diaponeurosporene starts with the condensation of two molecules of farnesyl diphosphate by dehydrosqualene synthase CrtM, the reaction product of this enzyme is dehydrosqualene and not squalene. Dehydrosqualene, i.e.4,4'-diapophytoene, is successively dehydrogenated by desaturase CrtN to form the yellow main intermediate 4,4'-diaponeurosporene
-
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docking analysis of lapaquistat acetate and squalestatin to crtM. Residues H18, R45, D48, D52, Y129, Q165, N168 and D172 interact with the inhibitors
-
in complex with three inhibitors bound, to about 2.1 A resolution. with inhibitor (3R)-3-biphenyl-4-yl-1-azabicyclo[2.2.2]octan-3-ol, enzyme forms two crystal structures. In both, the quinuclidine headgroup binds in the allylic S1 site with the side chain in S2, but in the presence of diphosphate and Mg2+, the quinuclidine's cationic center interacts with diphosphate and three Mg2+, mimicking a transition state involved in diphosphate ionization. Inhibitor 2-(4-phenoxyphenoxy)ethyl thiocyanate binds to the S2 site with its -SCN group surrounded by four hydrogen bond donors. Inhibitor N-[(2E)-3,7-dimethylocta-2,6-dien-1-yl]-N'-[(1R,3S,5R,7R)-tricyclo[3.3.1.1-3,7-]dec-2-yl]ethane-1,2-diamine forms two crystal structurs in complex with the enzyme. In one, the geranyl side chain binds to either S1 or S2 and the adamantane headgroup binds to S1. In the second, the side chain binds to S2 while the headgroup binds to S1
in with its reaction intermediate, presqualene diphosphate, the dehydrosqualene product, as well as a series of inhibitors. The results indicate that, on initial diphosphate loss, the primary carbocation so formed bends down into the interior of the protein to react with C2,3 double bond in the prenyl acceptor to form presqualene diphosphate, with the lower two-thirds of both presqualene diphosphate chains occupying essentially the same positions as found in the two farnesyl chains in the substrates. The second-half reaction is then initiated by the presqualene diphosphate returning back to the Mg2+ cluster for ionization, with the resultant dehydrosqualene so formed being trapped in a surface pocket
mutant Y248A in complex with zaragozic acid A, to 2.1 A resolution. Crystals grow in the hexagonal space group P3121 and contain two molecules per asymmetric unit. The active site of each protein is occupied by a molecule zazgozic acid A. The highly oxygenated core structure contacts residues 19SKSF22. The C-1 lipophilic tail extends into the narrow pocket which is lined with hydrophobic residues that help to stabilize the interaction with the isoprenoid moiety of the donor farnesyl diphosphate, S1 site.The side chains of Phe22 and Phe26 are moved toward the bottom of the active site, and the orientation of the Tyr41 side chain provides sufficient space for stabilization of the zaragozic acid A C-1 unit in the S1 site
-
native protein to 1.58 A resolution. CrtM crystallizes in the P3221 space group and there is one molecule per asymmetric unit. The overall fold shows similarity to that seen in human squalene synthase. In the complex with substrate analogue farnesyl thiodiphosphate, two farnesyl thiodiphosphate molecules are found in the large central cavity. Their diphosphate head groups interact with three Mg2+ ions, which in turn interact with Asp residues in two conserved Asp-X-X-X-Asp repeats. The space group of the complex is P3121, and there are two molecules per asymmetric unit. In docking studies with phosphonosulfonate inhibitors, only one phosphonosulfonate is bound per CrtM. All three inhibitors tested have different binding modes. 4-(3-phenoxyphenyl)-1-phosphonobutane-1-sulfonic acid binds into the farnesyl thiodiphosphate-1 site with two Mg2+, 4-(4'-butylbiphenyl-4-yl)-1-phosphonobutane-1-sulfonic acid binds into the farnesyl thiodiphosphate-2 site with only one Mg2+, and 4-(biphenyl-4-yl)-1-phosphonobutane-1-sulfonic acid binds into the farnesyl thiodiphosphate-2 site with no Mg2+. The phosphonosulfonate side chains do closely track the locations of the two farnesyl thiodiphosphate inhibitor side chains
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Q33R/D34N/S38N
-
directed evolution of human Q33R/D34N/S38N mutant squalene synthase, EC 2.5.1.21, in an attempt to mimic the activity of dehydroqsqualene synthase, EC 2.5.1.96, by replacement of hsqs in pAC-hsqs with the Saccharomyces mutant gene ysqs G856A/G1125A/T1128C/T1176C
G856A/G1125A/T1128C/T1176C
-
directed evolution of squalene synthase, EC 2.5.1.21, in an attempt to mimic the activity of dehydroqsqualene synthase, EC 2.5.1.96, by mutation of gene ysqs
A726G, A850G
-
mutant with phytoene synthase activity, decrease in dehydrosqualene synthase activity
F26L
-
mutation is sufficient to gain phytoene synthase activity, decrease in dehydrosqualene synthase activity
F26L/E149G
-
mutant with phytoene synthase activity, decrease in dehydrosqualene synthase activity
F26L/F267S
-
mutant with phytoene synthase activity, decrease in dehydrosqualene synthase activity
F26L/V43M
-
mutant with phytoene synthase activity, decrease in dehydrosqualene synthase activity
F26S/I40T
-
mutant with phytoene synthase activity, decrease in dehydrosqualene synthase activity
H12R/F26L/D27G/90G/K97R/H207R
-
mutant with phytoene synthase activity, decrease in dehydrosqualene synthase activity
K20E/F26S
-
mutant with phytoene synthase activity, decrease in dehydrosqualene synthase activity
M4V/H12R/F59S/Q81R/E180G
-
mutant with phytoene synthase activity, without decrease in dehydrosqualene synthase activity
Y129A
no activity with substrate farnesyl diphophate, 7% residual activity with geranyl diphosphate
Y248A
-
crystallization data of complex with zaragozic acid A
F26L
-
mutation is sufficient to gain phytoene synthase activity, decrease in dehydrosqualene synthase activity
-
F26L/E149G
-
mutant with phytoene synthase activity, decrease in dehydrosqualene synthase activity
-
F26L/V43M
-
mutant with phytoene synthase activity, decrease in dehydrosqualene synthase activity
-
K20E/F26S
-
mutant with phytoene synthase activity, decrease in dehydrosqualene synthase activity
-
additional information
expression of CrtM in Escherichia coli leads to synthesis of diapophytoene from pre-existing farnesyl diphosphate
additional information
-
expression of CrtM in Escherichia coli leads to synthesis of diapophytoene from pre-existing farnesyl diphosphate
additional information
-
expression of CrtM in Escherichia coli leads to synthesis of diapophytoene from pre-existing farnesyl diphosphate
-
additional information
-
construction of C40 carotenoid synthase pathway in Escherichia coli by expression of crtE encoding GGPP synthase, crtB encoding phytoene synthase, and crtI encoding phytoene desaturase, all from Erwinia uredovora. Replacement of phytoene synthase crtB by dehydrosqualene synthase crtM results in negligible ability to synthesize the C40 product. Some crtM mutants perform comparably to crtB in an in vivo C40 pathway. These mutants show significant variation in performance in their original C30 pathway, indicating the emergence of enzymes with broadened substrate specificity as well as those with shifted specificity
additional information
-
construction of C40 carotenoid synthase pathway in Escherichia coli by expression of crtE encoding GGPP synthase, crtB encoding phytoene synthase, and crtI encoding phytoene desaturase, all from Erwinia uredovora. Replacement of phytoene synthase crtB by dehydrosqualene synthase crtM results in negligible ability to synthesize the C40 product. Some crtM mutants perform comparably to crtB in an in vivo C40 pathway. These mutants show significant variation in performance in their original C30 pathway, indicating the emergence of enzymes with broadened substrate specificity as well as those with shifted specificity
-
additional information
Thermosynechococcus vestitus
-
directed evolution of squalene synthase, EC 2.5.1.21, in an attempt to mimic the activity of dehydroqsqualene synthase, EC 2.5.1.96, by mutation gene tsqs replacement with the human gene mutant Q33R/D34N/S38N/G856A/G1125A/T1128C/T1176C
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expressed in Escherichia coli Rosetta(DE3) cells
-
expression in Escherichia coli
gene crtM, DNA and amino acid sequence determination and analysis, genetic organization, sequence comparisons, phylogenetic tree, functional pathway complementation by recombinant enzyme expression in Escherichia coli
gene ysqs, recombinant expression of the engineered mutant enzyme in Escherichia coli strain XL1-Blue, coexpression with gene crtN encoding DSQ desaturase from Staphylococcus aureus in Escherichia coli results in carotinoid production and accumulation of C30 carotenoid pigments, which does not happen with coexpression of gene crtI encoding Pantoea ananatis phytoene desaturase, carotenoid pigment analysis, overview
-
recombinant expression of the endgineered enzymes in Escherichia coli strain XL1-Blue, coexpression with gene crtN encoding DSQ desaturase from Staphylococcus aureus in Escherichia coli results in carotinoid production and accumulation of C30 carotenoid pigments, which does not happen with coexpression of gene crtI encoding Pantoea ananatis phytoene desaturase, carotenoid pigment analysis, overview
-
recombinant expression of the engineered mutant enzyme in Escherichia coli strain XL1-Blue, coexpression with gene crtN encoding DSQ desaturase from Staphylococcus aureus in Escherichia coli results in carotinoid production and accumulation of C30 carotenoid pigments, which does not happen with coexpression of gene crtI encoding Pantoea ananatis phytoene desaturase, carotenoid pigment analysis, overview
Thermosynechococcus vestitus
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-
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expression in Escherichia coli
-
expression in Escherichia coli
gene crtM, DNA and amino acid sequence determination and analysis, genetic organization, sequence comparisons, phylogenetic tree, functional pathway complementation by recombinant enzyme expression in Escherichia coli
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gene crtM, DNA and amino acid sequence determination and analysis, genetic organization, sequence comparisons, phylogenetic tree, functional pathway complementation by recombinant enzyme expression in Escherichia coli
-
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Ku, B.; Jeong, J.C.; Mijts, B.N.; Schmidt-Dannert, C.; Dordick, J.S.
Preparation, characterization, and optimization of an in vitro C30 carotenoid pathway
Appl. Environ. Microbiol.
71
6578-6583
2005
Staphylococcus aureus
brenda
Koecher, S.; Breitenbach, J.; Mueller, V.; Sandmann, G.
Structure, function and biosynthesis of carotenoids in the moderately halophilic bacterium Halobacillus halophilus
Arch. Microbiol.
191
95-104
2009
Halobacillus halophilus (B9UXM0), Halobacillus halophilus, Halobacillus halophilus DSM 2266T (B9UXM0)
brenda
Garrido-Fernandez, J.; Maldonado-Barragan, A.; Caballero-Guerrero, B.; Hornero-Mendez, D.; Ruiz-Barba, J.
Carotenoid production in Lactobacillus plantarum
Int. J. Food Microbiol.
140
34-39
2010
Lactiplantibacillus plantarum (D3YHN9), Lactiplantibacillus plantarum
brenda
Wieland, B.; Feil, C.; Gloria-Maercker, E.; Thumm, G.; Lechner, M.; Bravo, J.M.; Poralla, K.; Gotz, F.
Genetic and biochemical analyses of the biosynthesis of the yellow carotenoid 4,4'-diaponeurosporene of Staphylococcus aureus
J. Bacteriol.
176
7719-7726
1994
Staphylococcus aureus (O07854), Staphylococcus aureus, Staphylococcus aureus Newman (O07854), Staphylococcus aureus Newman
brenda
Umeno, D.; Arnold, F.
Evolution of a pathway to novel long-chain carotenoids
J. Bacteriol.
186
1531-1536
2004
Staphylococcus aureus, Staphylococcus aureus ATCC 35556
brenda
Kahlon, A.; Roy, S.; Sharma, A.
Molecular docking studies to map the binding site of squalene synthase inhibitors on dehydrosqualene synthase of Staphylococcus aureus
J. Biomol. Struct. Dyn.
28
201-210
2010
Staphylococcus aureus
brenda
Song, Y.; Lin, F.; Yin, F.; Hensler, M.; Poveda, C.; Mukkamala, D.; Cao, R.; Wang, H.; Morita, C.; Pacanowska, D.; Nizet, V.; Oldfield, E.
Phosphonosulfonates are potent, selective inhibitors of dehydrosqualene synthase and staphyloxanthin biosynthesis in Staphylococcus aureus
J. Med. Chem.
52
976-988
2009
Staphylococcus aureus (A9JQL9), Staphylococcus aureus
brenda
Lin, F.; Liu, C.; Liu, Y.; Zhang, Y.; Wang, K.; Jeng, W.; Ko, T.; Cao, R.; Wang, A.; Oldfield, E.
Mechanism of action and inhibition of dehydrosqualene synthase
Proc. Natl. Acad. Sci. USA
107
21337-21342
2010
Staphylococcus aureus (A9JQL9), Staphylococcus aureus
brenda
Liu, C.; Liu, G.; Song, Y.; Yin, F.; Hensler, M.; Jeng, W.; Nizet, V.; Wang, A.; Oldfield, E.
A cholesterol biosynthesis inhibitor blocks Staphylococcus aureus virulence
Science
319
1391-1394
2008
Staphylococcus aureus (A9JQL9), Staphylococcus aureus
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
Staphylococcus aureus
brenda
Lin, F.Y.; Liu, Y.L.; Li, K.; Cao, R.; Zhu, W.; Axelson, J.; Pang, R.; Oldfield, E.
Head-to-head prenyl tranferases: anti-infective drug targets
J. Med. Chem.
55
4367-4372
2012
Staphylococcus aureus (A9JQL9), Staphylococcus aureus
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
Saccharomyces cerevisiae, Homo sapiens, Thermosynechococcus vestitus
brenda
Steiger, S.; Perez-Fons, L.; Cutting, S.M.; Fraser, P.D.; Sandmann, G.
Annotation and functional assignment of the genes for the C30 carotenoid pathways from the genomes of two bacteria: Bacillus indicus and Bacillus firmus
Microbiology
161
194-202
2015
Cytobacillus firmus, Metabacillus indicus, Metabacillus indicus HU36, Cytobacillus firmus GB1
brenda
Abdelmagid, W.M.; Adak, T.; Freeman, J.O.; Tanner, M.E.
Studies with guanidinium- and amidinium-based inhibitors suggest minimal stabilization of allylic carbocation intermediates by dehydrosqualene and squalene synthases
Biochemistry
57
5591-5601
2018
Staphylococcus aureus, Staphylococcus aureus MS4
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