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malfunction
P73914
inactivation of slr2089 leads to accumulation of squalene to a level over 70times higher than in wild-type cells, but no significant growth deficiency in the DELTAshc strain occur compared to the wild-type Synechocystis even at high light conditions
evolution

enzyme distribution in the different taxa, overview; structure-function relationships of squalene-hopene cyclases, the DXDD motif, which is typical for all squalene-hopene cyclases, overview
evolution
-
enzyme distribution in the different taxa, overview; structure-function relationships of squalene-hopene cyclases, the DXDD motif, which is typical for all squalene-hopene cyclases, overview
evolution
-
structure-function relationships of squalene-hopene cyclases, the DXDD motif, which is typical for all squalene-hopene cyclases, overview
evolution
-
structure-function relationships of squalene-hopene cyclases, the DXDD motif, which is typical for all squalene-hopene cyclases, overview
evolution
-
structure-function relationships of squalene-hopene cyclases, the DXDD motif, which is typical for all squalene-hopene cyclases, overview
evolution
-
structure-function relationships of squalene-hopene cyclases, the DXDD motif, which is typical for all squalene-hopene cyclases, overview
evolution
-
structure-function relationships of squalene-hopene cyclases, the DXDD motif, which is typical for all squalene-hopene cyclases, overview
evolution
-
squalene hopene cyclases are class II triterpene synthases that use a proton-initiated cationic polycyclization cascade to form carbopolycyclic products. The class II mechanism involves the Broensted acid sequence motif DxDD, catalytic mechanism compared to terpene cyclases, overview
metabolism

the enzyme converts squalene to hopanol, EC 4.2.1.129, and to hopene, EC 5.4.99.17, but not to tetrahymanol, EC 4.2.1.123, pathway overview; the enzyme is involved in biosynthesis of hopanoids, members of a large group of cyclic triterpenoic compounds that have important functions in many prokaryotic and eukaryotic organisms
metabolism
-
the enzyme converts squalene to tetrahymanol, EC 4.2.1.123, to hopene, EC 5.4.99.17, and to hopanol, EC 4.2.1.129, pathway overview; the enzyme is involved in biosynthesis of hopanoids, members of a large group of cyclic triterpenoic compounds that have important functions in many prokaryotic and eukaryotic organisms
metabolism
-
the enzyme is involved in biosynthesis of hopanoids, members of a large group of cyclic triterpenoic compounds that have important functions in many prokaryotic and eukaryotic organisms
metabolism
-
the enzyme is involved in biosynthesis of hopanoids, members of a large group of cyclic triterpenoic compounds that have important functions in many prokaryotic and eukaryotic organisms
metabolism
-
the enzyme is involved in biosynthesis of hopanoids, members of a large group of cyclic triterpenoic compounds that have important functions in many prokaryotic and eukaryotic organisms
metabolism
-
the nezym eis involved in biosynthesis of hopanoids, members of a large group of cyclic triterpenoic compounds that have important functions in many prokaryotic and eukaryotic organisms
metabolism
-
the enzyme is involved in biosynthesis of hopanoids, members of a large group of cyclic triterpenoic compounds that have important functions in many prokaryotic and eukaryotic organisms
metabolism
P73914
the enzyme converts squalene into hopene, the substrate for forming hopanoids
physiological function

-
hopene and hopanol are prokaryotic steroid analogues and have important functions as membrane constituents
physiological function
-
hopene and hopanol are prokaryotic steroid analogues and have important functions as membrane constituents
additional information

-
structure-function relationships of SHCs, active site structure, overview. A protruding part in the center of the nonpolar region contains a lipophilic channel and directs the substrate to the active-site cavity inside the protein. The channel and cavity are separated by a narrow constriction buildup of four amino acids, D376, F166, C435, and F434, that appear to block access to the active site. Residues C435 and F434 are part of a loop that seems to be flexible enough to permit passage of the substrate and the product; structure-function relationships of squalene-hopene cyclases, overview. A large central cavity represents the catalytic site in Alicyclobacillus acidocaldarius enzyme that takes up and orientates the squalene molecule. The channel and active-site cavity inside the protein are separated by a narrow constriction buildup of four amino acids, D376, F166, C435, and F434, that appear to block access to the active site
additional information
structure-function relationships of SHCs, active site structure, overview. A protruding part in the center of the nonpolar region contains a lipophilic channel and directs the substrate to the active-site cavity inside the protein. The channel and cavity are separated by a narrow constriction buildup of four amino acids, D376, F166, C435, and F434, that appear to block access to the active site. Residues C435 and F434 are part of a loop that seems to be flexible enough to permit passage of the substrate and the product; structure-function relationships of squalene-hopene cyclases, overview. A large central cavity represents the catalytic site in Alicyclobacillus acidocaldarius enzyme that takes up and orientates the squalene molecule. The channel and active-site cavity inside the protein are separated by a narrow constriction buildup of four amino acids, D376, F166, C435, and F434, that appear to block access to the active site
additional information
-
structure-function relationships of SHCs, active site structure, overview; structure-function relationships of squalene-hopene cyclases, overview
additional information
-
structure-function relationships of squalene-hopene cyclases, overview
additional information
-
structure-function relationships of squalene-hopene cyclases, overview
additional information
-
structure-function relationships of squalene-hopene cyclases, overview
additional information
-
structure-function relationships of squalene-hopene cyclases, overview
additional information
-
structure-function relationships of squalene-hopene cyclases, overview
additional information
-
the enzyme catalyzes the cyclization of triterpenoids via cationic intermediates in one of the most complex reactions known in biochemistry
additional information
-
the enzyme catalyzes the cyclization of triterpenoids via cationic intermediates in one of the most complex reactions known in biochemistry
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(3S)-2,3-oxidosqualene
lanosterol
-
-
-
-
?
(6E)-3,7,11-trimethyldodeca-1,6,10-trien-3-ol
(-)-caparrapioxide + (-)-8-epi-caparrapioxide
-
-
-
-
?
(6E,10E)-2,6,10-trimethyldodeca-2,6,10-triene
(4aR,5S,8aS)-1,1,4a,5,6-pentamethyl-1,2,3,4,4a,5,8,8a-octahydronaphthalene + (4aR,5S,8aS)-1,1,4a,5-tetramethyl-6-methylidenedecahydronaphthalene + (1R,2R,4aS,8aS)-1,2,5,5,8a-pentamethyldecahydronaphthalen-2-ol + (1R,2S,4aS,8aS)-1,2,5,5,8a-pentamethyldecahydronaphthalen-2-ol + (4aS,8aS)-4,4,7,8,8a-pentamethyl-1,2,3,4,4a,5,6,8a-octahydronaphthalene + (3S,4aS,8aS)-3,4,4,8,8a-pentamethyl-1,2,3,4,4a,5,6,8a-octahydronaphthalene
-
via bicyclic C8-cation
-
-
?
(E,E,E,E)-2,6,10,14,19,23-hexamethyltetracosa-2,6,10,14,18,22-hexaene
8-(4,8-Dimethyl-nona-3,7-dienyl)-1,1,4a,8a-tetramethyl-7-methylene-tetradecahydro-phenanthrene
-
-
low conversion, NMR spectroscopic analysis
-
?
(E,E,E,E)-2,6,10,15,18,23-hexamethyltetracosa-2,6,10,14,18,22-hexaene
1,1,4a,10a,10b-Pentamethyl-8-methylene-7-(4-methyl-pent-3-enyl)-octadecahydro-chrysene
-
-
one of the three major products, NMR spectroscopic analysis
-
?
(E,E,E,E)-2,6,10,15,18,23-hexamethyltetracosa-2,6,10,14,18,22-hexaene
1,1,4a,6a,8,10a-Hexamethyl-7-(4-methyl-pent-3-enyl)-1,2,3,4,4a,4b,5,6,6a,7,8,9,10,10a,12,12a-hexadecahydro-chrysene
-
-
one of the three major products, NMR spectroscopic analysis
-
?
(E,E,E,E)-2,6,10,15,18,23-hexamethyltetracosa-2,6,10,14,18,22-hexaene
1,1,4a,8,10a,10b-Hexamethyl-7-(4-methyl-pent-3-enyl)-1,2,3,4,4a,4b,5,6,8,9,10,10a,10b,11,12,12a-hexadecahydro-chrysene
-
-
one of the three major products, NMR spectroscopic analysis
-
?
(E,E,E,E)-2,6,10,15,18,23-hexamethyltetracosa-2,6,10,14,18,22-hexaene
2,4a,4b,7,7,10a-Hexamethyl-1-(4-methyl-pent-3-enyl)-octadecahydro-chrysen-2-ol
-
-
minor product, NMR spectroscopic analysis
-
?
(E,E,E,E)-2,6,10,15,18,23-hexamethyltetracosa-2,6,10,14,18,22-hexaene
2-(3a,5a,5b,8,8,11a-Hexamethyl-icosahydro-cyclopenta[a]chrysen-3-yl)-propan-2-ol
-
-
minor product, NMR spectroscopic analysis
-
?
(E,E,E,E)-2,6,10,15,18,23-hexamethyltetracosa-2,6,10,14,18,22-hexaene
alpha-3-Isopropenyl-3a,5a,5b,8,8,11a-hexamethyl-icosahydro-cyclopenta[a]chrysene
-
-
minor product, NMR spectroscopic analysis
-
?
(E,E,E,E)-2,6,10,15,18,23-hexamethyltetracosa-2,6,10,14,18,22-hexaene
beta-3-Isopropenyl-3a,5a,5b,8,8,11a-hexamethyl-icosahydro-cyclopenta[a]chrysene
-
-
minor product, NMR spectroscopic analysis
-
?
(E,E,E,E)-2,6,10,15,23-pentamethyltetracosa-2,6,10,14,18,22-hexaene
2-(5a,5b,8,8,11a-Pentamethyl-icosahydro-cyclopenta[a]chrysen-3-yl)-propan-2-ol
-
-
one of the three major products, yield 19.8%, NMR spectroscopic analysis
-
?
(E,E,E,E)-2,6,10,15,23-pentamethyltetracosa-2,6,10,14,18,22-hexaene
3-Isopropenyl-5a,5b,8,8,11a-pentamethyl-icosahydro-cyclopenta[a]chrysene
-
-
one of the three major products, yield 29.4%, NMR spectroscopic analysis
-
?
(E,E,E,E)-2,6,10,15,23-pentamethyltetracosa-2,6,10,14,18,22-hexaene
3-Isopropenyl-5a,5b,8,8,13b-pentamethyl-icosahydro-cyclopenta[a]chrysene
-
-
one of the three major products, yield 34.8%, NMR spectroscopic analysis
-
?
2-((2E,6E)-3,7,11-trimethyldodeca-2,6,10-trienyl)phenol + H2O
(3S,4aR,6aR,12aR,12bS)-4,4,6a,12b-tetramethyl-1,3,4,4a,5,6,6a,12,12a,12b-decahydro-2H-benzo[a]xanthen-3-ol + 2 H+
-
-
-
-
?
2-((2E,6E)-9-(3,3-dimethyloxiran-2-yl)-3,7-dimethylnona-2,6-dienyl)phenol
(4aS,6aR,12aR,12bS)-4,4,6a,12b-tetramethyl-1,3,4,4a,5,6,6a,12,12a,12b-decahydro-2H-benzo[a]xanthene + 2-[[(1S,4aS,8aS)-2,5,5,8a-tetramethyl-1,4,4a,5,6,7,8,8a-octahydronaphthalen-1-yl]methyl]phenol + 2-[[(1S,4aS,8aS)-5,5,8a-trimethyl-2-methylidenedecahydronaphthalen-1-yl]methyl]phenol
-
-
-
-
?
2-(farnesyldimethylallyl)pyrrole
?
-
-
product is a 10:1 mixture of a tricyclic and a bicyclic unnatural polyprenoid
-
?
3,7,11-trimethyldodeca-1,6,10-trien-3-ol
(-)-caparrapioxide + (-)-8-epi-caparrapioxide
-
-
-
-
-
3-(farnesyldimethylallyl)indole
?
-
-
conversion into a 2:1 mixture of a tetracyclic and a pentacyclic product
-
?
C33 polyprene
?
-
the enzymatic products consist of mono-, bi-, tri-, tetra- and pentacyclic skeletons, however, hexacyclic products are not generated
-
-
?
farnesol
drimenol + albicanol + driman-8,11-diol + [(1S,2R,8aS)-2,5,5,8a-tetramethyl-2-[[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]oxy]decahydronaphthalen-1-yl]methanol
-
-
drimane-type sequiterpenes
-
?
farnesyl phenyl ether
(4aS,5S,8aS)-1,1,4a,6-tetramethyl-5-(phenoxymethyl)-1,2,3,4,4a,5,8,8a-octahydronaphthalene + (4aS,4bR,10bR,12aS)-1,1,4a,10b-tetramethyl-2,3,4,4a,4b,5,10b,11,12,12a-decahydro-1H-naphtho[1,2-c]chromene
farnesylacetone
sclareoloxide
geranyl phenyl ether
(6aS,10aS)-7,7,10a-trimethyl-6a,7,8,9,10,10a-hexahydro-6H-benzo[c]chromene
geranylacetone
(8aS)-2,5,5,8a-tetramethyl-4a,5,6,7,8,8a-hexahydro-4H-chromene
geranylgeranyl phenyl ether
(14b)-8,13-dimethyl-14-(phenoxymethyl)podocarp-12-ene + (14b)-8-methyl-13-methylidene-14-(phenoxymethyl)podocarpane
-
-
-
-
?
homofarnesoic acid
sclareolide
hongoquercin A
?
-
-
-
-
?
hongoquercin B
?
-
-
-
-
?
squalene
hop-22(29)-ene + hopanol
squalene
hopene
-
-
-
-
?
additional information
?
-
citronellal

isopulegol
YP3187836
activity of mutant F481C, not of the wild-type enzyme
i.e. 2-isopropenyl-5-methyl-cyclohexanol
-
?
citronellal
isopulegol
-
-
i.e. 2-isopropenyl-5-methyl-cyclohexanol
-
?
citronellal
isopulegol
-
activity of mutant Y420C, not of the wild-type enzyme
i.e. 2-isopropenyl-5-methyl-cyclohexanol
-
?
citronellal
isopulegol
activity of mutant Y420C, not of the wild-type enzyme
i.e. 2-isopropenyl-5-methyl-cyclohexanol
-
?
citronellal
isopulegol
-
activity of mutant F447C, not of the wild-type enzyme
i.e. 2-isopropenyl-5-methyl-cyclohexanol
-
?
citronellal
isopulegol
activity of mutant F449C, not of the wild-type enzyme
i.e. 2-isopropenyl-5-methyl-cyclohexanol
-
?
citronellal
isopulegol
-
-
i.e. 2-isopropenyl-5-methyl-cyclohexanol
-
?
citronellal
isopulegol
-
i.e. 2-isopropenyl-5-methyl-cyclohexanol
-
?
citronellal
isopulegol
Q5NM88
-
i.e. 2-isopropenyl-5-methyl-cyclohexanol
-
?
citronellal
isopulegol
-
-
i.e. 2-isopropenyl-5-methyl-cyclohexanol
-
?
citronellal
isopulegol
activity of mutant F438C, not of the wild-type enzyme
i.e. 2-isopropenyl-5-methyl-cyclohexanol
-
?
citronellal
isopulegol
wild-type enzyme, and increased activity in mutant F486C
i.e. 2-isopropenyl-5-methyl-cyclohexanol
-
?
citronellal
isopulegol
activity of mutant F438C, not of the wild-type enzyme
i.e. 2-isopropenyl-5-methyl-cyclohexanol
-
?
citronellal
isopulegol
Q5NM88
-
i.e. 2-isopropenyl-5-methyl-cyclohexanol
-
?
citronellal
isopulegol
Q5NM88
wild-type enzyme, and increased activity in mutant F486C
i.e. 2-isopropenyl-5-methyl-cyclohexanol
-
?
citronellal
isopulegol
Q5NM88
-
i.e. 2-isopropenyl-5-methyl-cyclohexanol
-
?
citronellal
isopulegol
-
-
i.e. 2-isopropenyl-5-methyl-cyclohexanol
-
?
farnesyl phenyl ether

(4aS,5S,8aS)-1,1,4a,6-tetramethyl-5-(phenoxymethyl)-1,2,3,4,4a,5,8,8a-octahydronaphthalene + (4aS,4bR,10bR,12aS)-1,1,4a,10b-tetramethyl-2,3,4,4a,4b,5,10b,11,12,12a-decahydro-1H-naphtho[1,2-c]chromene
-
-
-
-
?
farnesyl phenyl ether
(4aS,5S,8aS)-1,1,4a,6-tetramethyl-5-(phenoxymethyl)-1,2,3,4,4a,5,8,8a-octahydronaphthalene + (4aS,4bR,10bR,12aS)-1,1,4a,10b-tetramethyl-2,3,4,4a,4b,5,10b,11,12,12a-decahydro-1H-naphtho[1,2-c]chromene
-
-
-
-
?
farnesylacetone

sclareoloxide
-
-
-
-
?
farnesylacetone
sclareoloxide
-
-
-
-
?
geranyl phenyl ether

(6aS,10aS)-7,7,10a-trimethyl-6a,7,8,9,10,10a-hexahydro-6H-benzo[c]chromene
-
-
-
-
?
geranyl phenyl ether
(6aS,10aS)-7,7,10a-trimethyl-6a,7,8,9,10,10a-hexahydro-6H-benzo[c]chromene
-
-
-
-
?
geranylacetone

(8aS)-2,5,5,8a-tetramethyl-4a,5,6,7,8,8a-hexahydro-4H-chromene
-
-
-
-
?
geranylacetone
(8aS)-2,5,5,8a-tetramethyl-4a,5,6,7,8,8a-hexahydro-4H-chromene
-
-
-
-
?
homofarnesoic acid

sclareolide
-
-
-
-
?
homofarnesoic acid
sclareolide
-
-
-
-
?
homofarnesol

ambroxan
-
-
-
-
?
homofarnesol
ambroxan
-
-
-
-
?
homofarnesol
ambroxan
Q5NM88
-
-
-
?
homofarnesol
ambroxan
-
-
-
-
?
homofarnesol
ambroxan
Q5NM88
-
-
-
?
squalene

hop-22(29)-ene
YP3187836
-
-
-
?
squalene
hop-22(29)-ene
-
-
-
?
squalene
hop-22(29)-ene
-
-
-
?
squalene
hop-22(29)-ene
-
-
-
?
squalene
hop-22(29)-ene
-
-
-
-
?
squalene
hop-22(29)-ene
-
-
-
?
squalene
hop-22(29)-ene
-
-
-
-
?
squalene
hop-22(29)-ene
-
-
-
?
squalene
hop-22(29)-ene
-
-
-
-
?
squalene
hop-22(29)-ene
-
-
-
?
squalene
hop-22(29)-ene
-
-
-
-
?
squalene
hop-22(29)-ene
-
-
hopanol is also formed
-
?
squalene
hop-22(29)-ene
-
-
the enzyme from Alicyclobacillus acidocaldarius yields pentacyclic hopene and hopanol (diplopterol) via a hopanyl cation from squalene
-
?
squalene
hop-22(29)-ene
-
products are formed in a molar ratio of hopene:hopanol, 5:1
-
-
?
squalene
hop-22(29)-ene
-
two types of water molecules ("front water" and "back waters") are involved around the deprotonation site. The two residues of Gln262 and Pro263 probably work to keep away the isopropyl group of the hopanyl cation intermediate from the "front water molecule", that is, to place the "front water" in a favorable position, leading to the minimal production of by-products, i.e., hopanol and hop-21(22)-ene. The five residues of Thr41, Glu45, Glu93, Arg127 and Trp133, by which the hydrogen-bonded network incorporating the "back waters" is constructed, increase the polarization of the "front water" to facilitate proton elimination from the isopropyl moiety of the hopanyl cation, leading to the normal product, hop-22(29)-ene
-
-
?
squalene
hop-22(29)-ene
-
products are formed in a molar ratio of hopene:hopanol, 5:1
-
-
?
squalene
hop-22(29)-ene
-
-
-
?
squalene
hop-22(29)-ene
-
-
-
?
squalene
hop-22(29)-ene
-
-
-
-
?
squalene
hop-22(29)-ene
-
-
-
?
squalene
hop-22(29)-ene
-
-
-
?
squalene
hop-22(29)-ene
-
-
-
-
?
squalene
hop-22(29)-ene
-
-
-
-
?
squalene
hop-22(29)-ene
-
-
-
?
squalene
hop-22(29)-ene
-
-
-
-
?
squalene
hop-22(29)-ene
-
-
-
?
squalene
hop-22(29)-ene
-
-
-
-
?
squalene
hop-22(29)-ene
-
-
-
?
squalene
hop-22(29)-ene
-
-
-
?
squalene
hop-22(29)-ene
-
-
-
-
?
squalene
hop-22(29)-ene
-
-
-
-
?
squalene
hop-22(29)-ene
-
-
-
-
?
squalene
hop-22(29)-ene
-
-
-
?
squalene
hop-22(29)-ene
-
-
-
?
squalene
hop-22(29)-ene
Q5NM88
-
-
-
?
squalene

hop-22(29)-ene + hopanol
-
the enzyme catalyzes cyclization of the linear triterpenoid squalene to hopene and hopanol by the class II mechanism
-
-
?
squalene
hop-22(29)-ene + hopanol
Q5NM88
-
-
-
?
squalene
hop-22(29)-ene + hopanol
-
-
-
-
?
squalene
hop-22(29)-ene + hopanol
-
the enzyme catalyzes cyclization of the linear triterpenoid squalene to hopene and hopanol by the class II mechanism
-
-
?
squalene
hop-22(29)-ene + hopanol
Q5NM88
-
-
-
?
squalene
hop-22(29)-ene + hopanol
-
-
-
-
?
additional information

?
-
YP3187836
no activity with citronellal or isopulegol (2-isopropenyl-5-methyl-cyclohexanol)
-
-
-
additional information
?
-
-
substrate specificity, overview
-
-
-
additional information
?
-
substrate specificity, overview
-
-
-
additional information
?
-
-
mutations lead to altered product pattern
-
-
-
additional information
?
-
-
mutations lead to altered product pattern
-
-
-
additional information
?
-
-
mutations lead to altered product pattern
-
-
-
additional information
?
-
-
mutations lead to altered product pattern
-
-
-
additional information
?
-
-
overview of cyclization products of wild type and mutant enzymes
-
-
-
additional information
?
-
-
overview of cyclization products of wild type and mutant enzymes
-
-
-
additional information
?
-
-
(E,E,E,E)-2,6,11,14,19,23-hexamethyltetracosa-2,6,10,14,18,22-hexaene: no detectable enzymatic activity
-
-
-
additional information
?
-
-
no enzymatic cyclization of 3-(geranylgeranyl)indole
-
-
-
additional information
?
-
-
no substrate: 2-(geranylgeranyl)pyrrole
-
-
-
additional information
?
-
-
no activity with citronellal or isopulegol (2-isopropenyl-5-methyl-cyclohexanol)
-
-
-
additional information
?
-
-
enzyme substrate specificity in polycyclization reactions, overview
-
-
-
additional information
?
-
-
no activity with linalool and pseudoionone
-
-
-
additional information
?
-
-
the enzyme also catalyzes 2,3-oxidosqualene cyclization, but no tetrahymanol formation. Substrate specificity, detailed overview
-
-
-
additional information
?
-
the enzyme also catalyzes 2,3-oxidosqualene cyclization, but no tetrahymanol formation. Substrate specificity, detailed overview
-
-
-
additional information
?
-
-
the enzyme shows substrate diversity for polycyclization reactions, since squalene-hopene cyclases specifically address and protonate terminal double bonds of linear terpenoids, molecules with functional groups like carboxylic acids or amides can be used as substrates, overview. It is active with squalene, a C-35 squalene analogue substrate, farnesol, and geranyl geraniol, but not with geraniol, products overview
-
-
-
additional information
?
-
-
product pattern of alternative substrates, overview
-
-
-
additional information
?
-
product pattern of alternative substrates, overview
-
-
-
additional information
?
-
no activity with citronellal or isopulegol (2-isopropenyl-5-methyl-cyclohexanol)
-
-
-
additional information
?
-
no activity with citronellal or isopulegol (2-isopropenyl-5-methyl-cyclohexanol)
-
-
-
additional information
?
-
-
no activity with citronellal or isopulegol (2-isopropenyl-5-methyl-cyclohexanol)
-
-
-
additional information
?
-
-
the enzyme also catalyzes 2,3-oxidosqualene cyclization, but no tetrahymanol formation. Substrate specificity, detailed overview
-
-
-
additional information
?
-
no activity with citronellal or isopulegol (2-isopropenyl-5-methyl-cyclohexanol)
-
-
-
additional information
?
-
Q0B5S3
no activity with citronellal or isopulegol (2-isopropenyl-5-methyl-cyclohexanol)
-
-
-
additional information
?
-
no activity with citronellal or isopulegol (2-isopropenyl-5-methyl-cyclohexanol)
-
-
-
additional information
?
-
Q0B5S3
no activity with citronellal or isopulegol (2-isopropenyl-5-methyl-cyclohexanol)
-
-
-
additional information
?
-
-
the enzyme does not catalyze 2,3-oxidosqualene cyclization nor tetrahymanol formation. Substrate specificity, detailed overview
-
-
-
additional information
?
-
-
no activity with citronellal or isopulegol (2-isopropenyl-5-methyl-cyclohexanol)
-
-
-
additional information
?
-
-
the enzyme does not catalyze tetrahymanol formation. Substrate specificity, detailed overview
-
-
-
additional information
?
-
no activity with citronellal or isopulegol (2-isopropenyl-5-methyl-cyclohexanol)
-
-
-
additional information
?
-
-
substrate specificity, detailed overview
-
-
-
additional information
?
-
no activity with citronellal or isopulegol (2-isopropenyl-5-methyl-cyclohexanol)
-
-
-
additional information
?
-
-
no activity with citronellal or isopulegol (2-isopropenyl-5-methyl-cyclohexanol)
-
-
-
additional information
?
-
-
the enzyme also catalyzes 2,3-oxidosqualene cyclization, substrate specificity, detailed overview
-
-
-
additional information
?
-
-
enzyme produces a wide variety of products due to lack of specificity
-
-
-
additional information
?
-
no activity with citronellal or isopulegol (2-isopropenyl-5-methyl-cyclohexanol)
-
-
-
additional information
?
-
Q5NM88
no activity with citronellal or isopulegol (2-isopropenyl-5-methyl-cyclohexanol)
-
-
-
additional information
?
-
-
no activity with linalool and pseudoionone
-
-
-
additional information
?
-
-
substrate specificity, detailed overview
-
-
-
additional information
?
-
-
substrate specificity, overview. No activity with prenyl phenyl ether
-
-
-
additional information
?
-
Q5NM88
ZmoSHC1 shows cyclization of the non-natural substrates homofarnesol (C16) and citronellal (C10) in addition to hopene formation from squalene, substrate specificity, overview. ZmoSHC1 exhibits a shift of activity towards substrates of shorter chain lengths, displaying over 50fold higher conversion of homofarnesol and more than 2fold higher conversion of citronellal in comparison to squalene conversion
-
-
-
additional information
?
-
no activity with citronellal or isopulegol (2-isopropenyl-5-methyl-cyclohexanol)
-
-
-
additional information
?
-
Q5NM88
ZmoSHC1 shows cyclization of the non-natural substrates homofarnesol (C16) and citronellal (C10) in addition to hopene formation from squalene, substrate specificity, overview. ZmoSHC1 exhibits a shift of activity towards substrates of shorter chain lengths, displaying over 50fold higher conversion of homofarnesol and more than 2fold higher conversion of citronellal in comparison to squalene conversion
-
-
-
additional information
?
-
-
substrate specificity, overview. No activity with prenyl phenyl ether
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(18E)-29-methylidenehexanor-2,3-oxidosqualene
-
IC50 0.2 microMol, pH 6.0, 55°C
-
(1E,3E,7E,11E)-15,16-epoxy-8,12,16-trimethyl-1-methylthio-1,3,7,11-heptadecatetraene
-
IC50 1 microMol, pH 6.0, 55°C
-
(1E,3E,7E,11E,15E)-19,20-epoxy-7,12,16,20-tetramethyl-1-methylthio-1,3,7,11,15-heneicosapentaene
-
IC50 1.4 microMol, pH 6.0, 55°C, not time-dependency up to 10fold higher concentration than IC50
-
(1Z,3E,7E,11E)-15,16-epoxy-8,12,16-trimethyl-1-methylthio-1,3,7,11-heptadecatetraene
-
IC50 4 microMol, pH 6.0, 55°C
-
(1Z,3E,7E,11E,15E)-19,20-epoxy-7,12,16,20-tetramethyl-1-methylthio-1,3,7,11,15-heneicosapentaene
-
IC50 1.8 microMol, pH 6.0, 55°C, not time-dependency up to 10fold higher concentration than IC50
-
(2E)-4-[4-(6-bromo-1,2-benzisothiazol-3-yl)phenoxy]-N-methyl-N-prop-2-en-1-ylbut-2-en-1-aminium
-
-
(2E)-4-[4-[(4-bromophenyl)carbonyl]phenoxy]-N-methyl-N-prop-2-en-1-ylbut-2-en-1-aminium
-
-
(2E)-4-[[3-(4-bromophenyl)-1,2-benzisoxazol-6-yl]oxy]-N-methyl-N-prop-2-en-1-ylbut-2-en-1-aminium
-
-
(2E)-4-[[3-(4-bromophenyl)-1-benzofuran-6-yl]oxy]-N-methyl-N-prop-2-en-1-ylbut-2-en-1-aminium
-
-
(2E)-4-[[3-(4-bromophenyl)-1-benzothiophen-6-yl]oxy]-N-methyl-N-prop-2-en-1-ylbut-2-en-1-aminium
-
-
(3E,7E,11E)-15,16-epoxy-8,12,16-trimethyl-1-phenylthio-1,3,7,11-heptadecatetraene
-
IC50 2.2 microMol, pH 6.0, 55°C
-
(4-(2-[(allyl-cyclopropyl-amino)-methyl]-cyclopropylmethoxy)-phenyl)-(4-bromo-phenyl)-methanone
-
IC50 59 nM
(4-bromo-phenyl)-(4-(2-[(cyclopropyl-methyl-amino)-methyl]-cyclopropylmethoxy)-2-fluoro-phenyl)-methanone
-
IC50 50 nM
(4-bromo-phenyl)-(4-(2-[(cyclopropyl-methyl-amino)-methyl]-cyclopropylmethoxy)-phenyl)-methanone
-
IC50 62 nM
(4-bromo-phenyl)-(4-[4-(cyclopropyl-methyl-amino)-but-2-enyloxy]-phenyl)-methanone
-
IC50 18 nM
(4-bromo-phenyl)-(4-[6-(cyclopropyl-methyl-amino)-hexyloxy]-2-fluoro-phenyl)-methanone
-
IC50 38 nM
(4-chloro-phenyl)-(4-[4-(4,5-dihydro-oxazol-2-yl)-benzylidene]-piperidin-1-yl)-methanone
-
IC50 2800 nM
(4-[6-(allyl-methyl-amino)-hexyloxy]-2-fluoro-phenyl)-(4-bromo-phenyl)-methanone
-
IC50 60 nM
(4-[6-(allyl-methyl-amino)-hexyloxy]-phenyl)-(4-bromo-phenyl)-methanone
-
IC50 96 nM
(5-hydroxycarvacryl)trimethylammonium chloride 1-piperidine carboxylate
(5E,9E)-13,14-epoxy-6,10,14-trimethyl-1-phenylthio-1,5,9-pentadecatriene
-
IC50 7 microMol, pH 6.0, 55°C
-
(5E,9E,13E)-17,18-epoxy-5,10,14,18-tetramethyl-1-phenylthio-1,5,9,13-nonadecatetraene
-
IC50 3 microMol, pH 6.0, 55°C
-
1-(4-(4-[(4-chloro-phenoxycarbonyl)-methyl-amino]-cyclohexyl)-benzyl)-1-hydroxy-piperidinium
-
IC50 123 nM
1-[(4-chlorophenyl)carbonyl]-4-[[4-(4,5-dihydro-1,3-oxazol-2-yl)phenyl]methylidene]piperidine
-
-
1-[4-(trans-4-[[(4-chlorophenoxy)carbonyl](methyl)amino]cyclohexyl)benzyl]piperidinium
-
-
3-(10'-(allylmethylamino)decanoyl)chroman-2,4-dione
-
IC50 100 microMol
-
3-carboxy-4-nitrophenyl-dithio-1,1',2-trisnorsqualene
-
covalently modifies C435
4'-[4-(allyl-methyl-amino)-but-2-enyloxy]-biphenyl-4-yl-(4-bromo-phenyl)-methanone
-
IC50 29 nM
4-chlorophenyl methyl(trans-4-[4-[(1-oxidopiperidin-1-yl)methyl]phenyl]cyclohexyl)carbamate
-
-
4-[4-(allyl-methyl-amino)-but-2-enyloxy]-phenyl-(4-bromo-phenyl)-methanone
-
IC50 40 nM
4-[6-(allyl-methyl-amino)-hexyloxy]-piperidin-1-yl-(4-fluoro-phenyl)-methanone
-
IC50 1200 nM
4-[6-(cyclopropyl-methyl-amino)-hexyloxy]-piperidin-1-yl-(4-fluoro-phenyl)-methanone
-
IC50 760 nM
6-([1-[(4-fluorophenyl)carbonyl]piperidin-4-yl]oxy)-N-methyl-N-prop-2-en-1-ylhexan-1-aminium
-
-
6-[(1,3-dimethyl-1H-indazol-5-yl)oxy]-N-methyl-N-prop-2-en-1-ylhexan-1-aminium
-
-
6-[4-(6-bromo-1,2-benzisothiazol-3-yl)phenoxy]-N-methyl-N-prop-2-en-1-ylhexan-1-aminium
-
-
6-[4-[(4-bromophenyl)carbonyl]-3-fluorophenoxy]-N-methyl-N-prop-2-en-1-ylhexan-1-aminium
-
-
6-[4-[(4-bromophenyl)carbonyl]phenoxy]-N-(3-hydroxypropyl)-N-methylhexan-1-aminium
-
-
6-[4-[(4-bromophenyl)carbonyl]phenoxy]-N-methyl-N-prop-2-en-1-ylhexan-1-aminium
-
-
6-[[1-(4-bromophenyl)isoquinolin-6-yl]oxy]-N-methyl-N-prop-2-en-1-ylhexan-1-aminium
-
-
6-[[3-(4-bromophenyl)-1,2-benzisothiazol-5-yl]oxy]-N-methyl-N-prop-2-en-1-ylhexan-1-aminium
-
-
6-[[3-(4-bromophenyl)-1,2-benzisoxazol-6-yl]oxy]-N-methyl-N-prop-2-en-1-ylhexan-1-amine
-
-
6-[[3-(4-bromophenyl)-1,2-benzisoxazol-6-yl]oxy]-N-methyl-N-prop-2-en-1-ylhexan-1-aminium
-
-
6-[[3-(4-bromophenyl)-1-benzofuran-6-yl]oxy]-N-methyl-N-prop-2-en-1-ylhexan-1-amine
-
-
6-[[3-(4-bromophenyl)-1-benzofuran-6-yl]oxy]-N-methyl-N-prop-2-en-1-ylhexan-1-aminium
-
-
6-[[3-(4-bromophenyl)-1-methyl-1H-indol-6-yl]oxy]-N-methyl-N-prop-2-en-1-ylhexan-1-amine
-
-
6-[[3-(4-bromophenyl)-1H-indazol-6-yl]oxy]-N-methyl-N-prop-2-en-1-ylhexan-1-amine
-
-
6-[[3-(4-bromophenyl)-1H-indazol-6-yl]oxy]-N-methyl-N-prop-2-en-1-ylhexan-1-aminium
-
-
6-[[4-(4-bromophenyl)-1H-2,3-benzoxazin-7-yl]oxy]-N-methyl-N-prop-2-en-1-ylhexan-1-aminium
-
-
7-(10'-(dimethylamino-N-decyloxy))chromen-2-one
-
IC50 5 microMol
-
7-(10-(allylmethylamino)-decyloxy)chromen-2-one
-
IC50 2 microMol
-
7-(4'-(N,N,N'-trimethylethylethylendiamino)-but-2-ynyloxy)chromen-2-one
-
not active at 100 microMol
-
7-(4'-(N-diethylamino)-but-2-ynyloxy)chromen-2-one
-
IC50 5 microMol
-
7-(4'-(N-pyrrolidyn)-but-2-ynyloxy)chromen-2-one
-
IC50 5 microMol
-
7-(4-allylmethylamino-but-2-ynyloxy)chromen-2-one
-
IC50 0.75 microMol
7-(6'-(benzylamino-hexyloxy))chromen-2-one
-
IC50 8 microMol
-
7-(6-(allylmethylamino)-hexyloxy)chromen-2-one
-
IC50 4-5 microMol
-
7-(8'-(dimethylamino-N-octyloxy))chromen-2-one
-
IC50 5-7 microMol
-
7-(morpholinyl-N-hexyloxy)chromen-2-one
-
IC50 6 microMol
7-(morpholinyl-N-octyloxy)chromen-2-one
-
IC50 7 microMol
-
7-(piperidinyl-N-hexyloxy)chromen-2-one
-
IC50 8 microMol
allyl-(4-[3-(4-bromo-phenyl)-5-fluoro-1-methyl-1H-indazol-6-yloxy]-but-2-enyl)-methyl-amine
-
IC50 281 nM; IC50 332 nM
allyl-(4-[3-(4-bromo-phenyl)-benzofuran-6-yloxy]-but-2-enyl)-methyl-amine
-
IC50 23 nM
allyl-(4-[3-(4-bromo-phenyl)-benzo[b]thiophen-6-yloxy]-butyl)-methyl-amine
-
IC50 75 nM
allyl-(4-[3-(4-bromo-phenyl)-benzo[d]isoxazol-6-yloxy]-but-2-enyl)-amine
-
IC50 49 nM
allyl-(4-[4-(6-bromo-benzo[d]isothiazol-3-yl)-phenoxy]-but-2-enyl)-methyl-amine
-
IC50 130 nM
allyl-(6-[1-(4-bromo-phenyl)-isoquinolin-6-yloxy]-hexyl)-methyl-amine
-
IC50 186 nM
allyl-(6-[3-(4-bromo-phenyl)-1-methyl-1H-indazol-6-yloxy]-hexyl)-methyl-amine
-
IC50 289 nM
allyl-(6-[3-(4-bromo-phenyl)-1H-indazol-6-yloxy]-hexyl)-methyl-amine
-
IC50 180 nM
allyl-(6-[3-(4-bromo-phenyl)-benzofuran-6-yloxy]-hexyl)-methyl-amine
-
IC50 80 nM
allyl-(6-[3-(4-bromo-phenyl)-benzo[d]isothiazol-6-yloxy]-hexyl)-methyl-amine
-
IC50 306 nM
allyl-(6-[3-(4-bromo-phenyl)-benzo[d]isoxazol-6-yloxy]-hexyl)-methyl-amine
-
IC50 75 nM
allyl-(6-[4-(4-bromo-phenyl)-1H-benzo[d][1,2]oxazin-7-yloxy]-hexyl)-methyl-amine
-
IC50 172 nM
allyl-(6-[4-(6-bromo-benzo[d]isothiazol-3-yl)-phenoxy]-hexyl)-methyl-amine
-
IC50 141 nM
azasqualene
-
inhibition at 0.001 mM
-
Cu2+
-
slight inhibition at 1 mM
diethyldicarbonate
-
92% inhibition at 5 mM
dodecyldimethylamine N-oxide
-
competitive inhibition
dodecyltrimethylammonium bromide
-
competitive inhibition, 50% inhibition at 0.0001 mM
farnesol
-
inhibition at 0.1 mM
Fe2+
-
slight inhibition at 1 mM
HECAMEG
-
80% inactivation compared to CHAPS
methyl-[4-(4-piperidin-1-ylmethyl-phenyl)-cyclohexyl]-carbamic acid 4-chloro-phenyl ester
-
IC50 406 nM
N,N-dimethyldodecylamine N-oxide
-
forms a complex with the enzyme
N-(6-[4-[(4-bromophenyl)carbonyl]-3-fluorophenoxy]hexyl)-N-methylcyclopropanaminium
-
-
N-([4'-[(4-bromophenyl)carbonyl]biphenyl-4-yl]methyl)-N-methylprop-2-en-1-aminium
-
-
N-dodecyliodoacetamide
-
IC50 wild-type >200 microMol, quintuple mutant >200 microMol, sextuple mutant >200 microMol, pH 6.0, 50°C
-
N-ethylmaleimide
-
65% inhibition at 5 mM, 20% inhibition at 1 mM
N-squalenyliodoacetamide
-
IC50 wild-type >200 microMol, quintuple mutant >200 microMol, sextuple mutant 50 microMol, pH 6.0, 50°C
-
N-[(2E)-4-[4-[(4-bromophenyl)carbonyl]phenoxy]but-2-en-1-yl]-N-methylcyclopropanaminium
-
-
N-[6-([1-[(4-fluorophenyl)carbonyl]piperidin-4-yl]oxy)hexyl]-N-methylcyclopropanaminium
-
-
N-[[(1S,2S)-2-([4-[(4-bromophenyl)carbonyl]-3-fluorophenoxy]methyl)cyclopropyl]methyl]-N-methylcyclopropanaminium
-
-
N-[[(1S,2S)-2-([4-[(4-bromophenyl)carbonyl]phenoxy]methyl)cyclopropyl]methyl]-N-methylcyclopropanaminium
-
-
N-[[(1S,2S)-2-([4-[(4-bromophenyl)carbonyl]phenoxy]methyl)cyclopropyl]methyl]-N-prop-2-en-1-ylcyclopropanaminium
-
-
octylthiogucopyranoside
-
complete inactivation
p-chloromercuribenzenesulfonic acid
-
96% inhibition at 1 mM
Ro 48-8071
-
IC50 0.35 microMol
sodium dodecylsulfate
-
strong inhibition
sodium taurodeoxycholate
-
under 0.15% and above 0.25%
squalene-maleimide
-
time-dependent inhibitor
taurodeoxycholate
-
80% inactivation compared to CHAPS
Triton-X100
-
96% inhibition
Zn2+
-
slight inhibition at 5 mM
Zwittergent
-
80% inactivation compared to CHAPS
-
(5-hydroxycarvacryl)trimethylammonium chloride 1-piperidine carboxylate

-
i.e. AMO 1618, competitive inhibition
(5-hydroxycarvacryl)trimethylammonium chloride 1-piperidine carboxylate
-
99% inhibition at 1 mM
additional information

-
vinyl sulfide and ketene dithioacetal derivates of truncated 2,3-ocidosqualene interact with active site of the enzyme
-
additional information
-
sulfur-substituted oxidosqualene analogues serve as inhibitors
-
additional information
-
effect of thiol-modifying inhibitors on mutant enzymes
-
additional information
-
inhibition by n-alkyldimethylammoniumhalides with alkyl chain lengths between 12 and 18 C atoms, inhibition increases with decreasing chain length
-
additional information
-
sulfur-containing analogues of 2,3-oxidosqualene inhibit enzyme activity, 50% inhibition at concentrations in the nanomolar range
-
additional information
-
inhibitors designed as cholesterol-lowering agents, for 11 inhibitors the structures of the enzyme-inhibitor complexes were determined by X-ray crystallography
-
additional information
-
several detergents have inhibitory effect
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.0002
(18E)-29-methylidenehexanor-2,3-oxidosqualene
Alicyclobacillus acidocaldarius
-
IC50 0.2 microMol, pH 6.0, 55°C
-
0.001
(1E,3E,7E,11E)-15,16-epoxy-8,12,16-trimethyl-1-methylthio-1,3,7,11-heptadecatetraene
Alicyclobacillus acidocaldarius
-
IC50 1 microMol, pH 6.0, 55°C
-
0.0014
(1E,3E,7E,11E,15E)-19,20-epoxy-7,12,16,20-tetramethyl-1-methylthio-1,3,7,11,15-heneicosapentaene
Alicyclobacillus acidocaldarius
-
IC50 1.4 microMol, pH 6.0, 55°C, not time-dependency up to 10fold higher concentration than IC50
-
0.004
(1Z,3E,7E,11E)-15,16-epoxy-8,12,16-trimethyl-1-methylthio-1,3,7,11-heptadecatetraene
Alicyclobacillus acidocaldarius
-
IC50 4 microMol, pH 6.0, 55°C
-
0.0018
(1Z,3E,7E,11E,15E)-19,20-epoxy-7,12,16,20-tetramethyl-1-methylthio-1,3,7,11,15-heneicosapentaene
Alicyclobacillus acidocaldarius
-
IC50 1.8 microMol, pH 6.0, 55°C, not time-dependency up to 10fold higher concentration than IC50
-
0.0022
(3E,7E,11E)-15,16-epoxy-8,12,16-trimethyl-1-phenylthio-1,3,7,11-heptadecatetraene
Alicyclobacillus acidocaldarius
-
IC50 2.2 microMol, pH 6.0, 55°C
-
0.000059
(4-(2-[(allyl-cyclopropyl-amino)-methyl]-cyclopropylmethoxy)-phenyl)-(4-bromo-phenyl)-methanone
Alicyclobacillus acidocaldarius
-
IC50 59 nM
0.00005
(4-bromo-phenyl)-(4-(2-[(cyclopropyl-methyl-amino)-methyl]-cyclopropylmethoxy)-2-fluoro-phenyl)-methanone
Alicyclobacillus acidocaldarius
-
IC50 50 nM
0.000062
(4-bromo-phenyl)-(4-(2-[(cyclopropyl-methyl-amino)-methyl]-cyclopropylmethoxy)-phenyl)-methanone
Alicyclobacillus acidocaldarius
-
IC50 62 nM
0.000018
(4-bromo-phenyl)-(4-[4-(cyclopropyl-methyl-amino)-but-2-enyloxy]-phenyl)-methanone
Alicyclobacillus acidocaldarius
-
IC50 18 nM
0.000038
(4-bromo-phenyl)-(4-[6-(cyclopropyl-methyl-amino)-hexyloxy]-2-fluoro-phenyl)-methanone
Alicyclobacillus acidocaldarius
-
IC50 38 nM
0.0028
(4-chloro-phenyl)-(4-[4-(4,5-dihydro-oxazol-2-yl)-benzylidene]-piperidin-1-yl)-methanone
Alicyclobacillus acidocaldarius
-
IC50 2800 nM
0.00006
(4-[6-(allyl-methyl-amino)-hexyloxy]-2-fluoro-phenyl)-(4-bromo-phenyl)-methanone
Alicyclobacillus acidocaldarius
-
IC50 60 nM
0.000096
(4-[6-(allyl-methyl-amino)-hexyloxy]-phenyl)-(4-bromo-phenyl)-methanone
Alicyclobacillus acidocaldarius
-
IC50 96 nM
0.007
(5E,9E)-13,14-epoxy-6,10,14-trimethyl-1-phenylthio-1,5,9-pentadecatriene
Alicyclobacillus acidocaldarius
-
IC50 7 microMol, pH 6.0, 55°C
-
0.003
(5E,9E,13E)-17,18-epoxy-5,10,14,18-tetramethyl-1-phenylthio-1,5,9,13-nonadecatetraene
Alicyclobacillus acidocaldarius
-
IC50 3 microMol, pH 6.0, 55°C
-
0.000123
1-(4-(4-[(4-chloro-phenoxycarbonyl)-methyl-amino]-cyclohexyl)-benzyl)-1-hydroxy-piperidinium
Alicyclobacillus acidocaldarius
-
IC50 123 nM
0.1
3-(10'-(allylmethylamino)decanoyl)chroman-2,4-dione
Alicyclobacillus acidocaldarius
-
IC50 100 microMol
-
0.000029
4'-[4-(allyl-methyl-amino)-but-2-enyloxy]-biphenyl-4-yl-(4-bromo-phenyl)-methanone
Alicyclobacillus acidocaldarius
-
IC50 29 nM
0.00004
4-[4-(allyl-methyl-amino)-but-2-enyloxy]-phenyl-(4-bromo-phenyl)-methanone
Alicyclobacillus acidocaldarius
-
IC50 40 nM
0.0012
4-[6-(allyl-methyl-amino)-hexyloxy]-piperidin-1-yl-(4-fluoro-phenyl)-methanone
Alicyclobacillus acidocaldarius
-
IC50 1200 nM
0.00076
4-[6-(cyclopropyl-methyl-amino)-hexyloxy]-piperidin-1-yl-(4-fluoro-phenyl)-methanone
Alicyclobacillus acidocaldarius
-
IC50 760 nM
0.000075
6-[[3-(4-bromophenyl)-1,2-benzisoxazol-6-yl]oxy]-N-methyl-N-prop-2-en-1-ylhexan-1-amine
Alicyclobacillus acidocaldarius
-
-
0.005
7-(10'-(dimethylamino-N-decyloxy))chromen-2-one
Alicyclobacillus acidocaldarius
-
IC50 5 microMol
-
0.002
7-(10-(allylmethylamino)-decyloxy)chromen-2-one
Alicyclobacillus acidocaldarius
-
IC50 2 microMol
-
0.005
7-(4'-(N-diethylamino)-but-2-ynyloxy)chromen-2-one, 7-(4'-(N-pyrrolidyn)-but-2-ynyloxy)chromen-2-one
Alicyclobacillus acidocaldarius
-
IC50 5 microMol
-
0.00075
7-(4-allylmethylamino-but-2-ynyloxy)chromen-2-one
Alicyclobacillus acidocaldarius
-
IC50 0.75 microMol
0.008
7-(6'-(benzylamino-hexyloxy))chromen-2-one
Alicyclobacillus acidocaldarius
-
IC50 8 microMol
-
0.004 - 0.005
7-(6-(allylmethylamino)-hexyloxy)chromen-2-one
Alicyclobacillus acidocaldarius
-
IC50 4-5 microMol
-
0.005 - 0.007
7-(8'-(dimethylamino-N-octyloxy))chromen-2-one
Alicyclobacillus acidocaldarius
-
IC50 5-7 microMol
-
0.006
7-(morpholinyl-N-hexyloxy)chromen-2-one
Alicyclobacillus acidocaldarius
-
IC50 6 microMol
0.007
7-(morpholinyl-N-octyloxy)chromen-2-one
Alicyclobacillus acidocaldarius
-
IC50 7 microMol
-
0.008
7-(piperidinyl-N-hexyloxy)chromen-2-one
Alicyclobacillus acidocaldarius
-
IC50 8 microMol
0.000281 - 0.000332
allyl-(4-[3-(4-bromo-phenyl)-5-fluoro-1-methyl-1H-indazol-6-yloxy]-but-2-enyl)-methyl-amine
0.000023
allyl-(4-[3-(4-bromo-phenyl)-benzofuran-6-yloxy]-but-2-enyl)-methyl-amine
Alicyclobacillus acidocaldarius
-
IC50 23 nM
0.000075
allyl-(4-[3-(4-bromo-phenyl)-benzo[b]thiophen-6-yloxy]-butyl)-methyl-amine
Alicyclobacillus acidocaldarius
-
IC50 75 nM
0.000049
allyl-(4-[3-(4-bromo-phenyl)-benzo[d]isoxazol-6-yloxy]-but-2-enyl)-amine
Alicyclobacillus acidocaldarius
-
IC50 49 nM
0.00013
allyl-(4-[4-(6-bromo-benzo[d]isothiazol-3-yl)-phenoxy]-but-2-enyl)-methyl-amine
Alicyclobacillus acidocaldarius
-
IC50 130 nM
0.000186
allyl-(6-[1-(4-bromo-phenyl)-isoquinolin-6-yloxy]-hexyl)-methyl-amine
Alicyclobacillus acidocaldarius
-
IC50 186 nM
0.000289
allyl-(6-[3-(4-bromo-phenyl)-1-methyl-1H-indazol-6-yloxy]-hexyl)-methyl-amine
Alicyclobacillus acidocaldarius
-
IC50 289 nM
0.00018
allyl-(6-[3-(4-bromo-phenyl)-1H-indazol-6-yloxy]-hexyl)-methyl-amine
Alicyclobacillus acidocaldarius
-
IC50 180 nM
0.00008
allyl-(6-[3-(4-bromo-phenyl)-benzofuran-6-yloxy]-hexyl)-methyl-amine
Alicyclobacillus acidocaldarius
-
IC50 80 nM
0.000306
allyl-(6-[3-(4-bromo-phenyl)-benzo[d]isothiazol-6-yloxy]-hexyl)-methyl-amine
Alicyclobacillus acidocaldarius
-
IC50 306 nM
0.000075
allyl-(6-[3-(4-bromo-phenyl)-benzo[d]isoxazol-6-yloxy]-hexyl)-methyl-amine
Alicyclobacillus acidocaldarius
-
IC50 75 nM
0.000172
allyl-(6-[4-(4-bromo-phenyl)-1H-benzo[d][1,2]oxazin-7-yloxy]-hexyl)-methyl-amine
Alicyclobacillus acidocaldarius
-
IC50 172 nM
0.000141
allyl-(6-[4-(6-bromo-benzo[d]isothiazol-3-yl)-phenoxy]-hexyl)-methyl-amine
Alicyclobacillus acidocaldarius
-
IC50 141 nM
0.000406
methyl-[4-(4-piperidin-1-ylmethyl-phenyl)-cyclohexyl]-carbamic acid 4-chloro-phenyl ester
Alicyclobacillus acidocaldarius
-
IC50 406 nM
0.2
N-dodecyliodoacetamide
Alicyclobacillus acidocaldarius
-
IC50 wild-type >200 microMol, quintuple mutant >200 microMol, sextuple mutant >200 microMol, pH 6.0, 50°C
-
0.05 - 0.2
N-squalenyliodoacetamide
-
0.00035
Ro 48-8071
Alicyclobacillus acidocaldarius
-
IC50 0.35 microMol
0.000281
allyl-(4-[3-(4-bromo-phenyl)-5-fluoro-1-methyl-1H-indazol-6-yloxy]-but-2-enyl)-methyl-amine

Alicyclobacillus acidocaldarius
-
IC50 281 nM
0.000332
allyl-(4-[3-(4-bromo-phenyl)-5-fluoro-1-methyl-1H-indazol-6-yloxy]-but-2-enyl)-methyl-amine
Alicyclobacillus acidocaldarius
-
IC50 332 nM
0.05
N-squalenyliodoacetamide

Alicyclobacillus acidocaldarius
-
IC50 sextuple mutant 50 microMol, pH 6.0, 50°C
-
0.2
N-squalenyliodoacetamide
Alicyclobacillus acidocaldarius
-
IC50 quintuple mutant >200 microMol; IC50 wild-type >200 microMol
-
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F481C
YP3187836
site-directed mutagenesis, the mutant performs interconversion of citronellal and isopulegol
C25S/C50S/C435S/C455S/C537S
-
quintuple mutant
C25S/C50S/D376C/C435S/C455S/C537S
-
sextuple mutant
C435S/D374I/D374V/H451F
inactive mutant; site-directed mutagenesis, inactive mutant
D376E/D377E
-
no enzyme activity
D376G
-
0.2% activity when enzyme concentration is increased to 100fold
D376Q
-
no enzyme activity
D376R
-
no enzyme activity
D377C/D377N/Y612A
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview; the mutant shows an altered product pattern compared to the wild-type enzyme, overview
D377C/V380E/V381A
-
no detectable cyclization of squalene
D377E
-
0.2% activity when enzyme concentration is increased to 100fold
D377E/D376Q/D376R/D377R/E45K/W406V/W417A/D377C
inactive mutant; site-directed mutagenesis, inactive mutant
D377G
-
0.2% activity when enzyme concentration is increased to 100fold
D377Q
-
0.2% activity when enzyme concentration is increased to 100fold
D377R
-
no enzyme activity
E45D
-
reduced enzyme activity
E45K
-
no enzyme activity
E45Q
-
slightly increased enzyme activity
E93A
-
mutation located around the 'back waters'; production of hop-22(29)-ene is less throughout the entire temperature range than that by the wild-type. Hop-21(22)ene is not produced
F365A
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview; the mutant shows an altered product pattern compared to the wild-type enzyme, overview
F365W
-
marginal catalytic activity
F365Y
-
and mutant with F365 changed to unnatural amino acid O-methyltyrosine. Both show increased decreased activity at high temperature
F434A
-
mutation near the substrat channel; production of hop-22(29)-ene is decreased, production of hopanol is markedly increased at lower temperatures
F437A
-
mutation near the substrat channel; production of hop-22(29)-ene is decreased, production of hopanol is markedly increased at lower temperatures
F601A
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview; the mutant shows an altered product pattern compared to the wild-type enzyme, overview
F605W
-
increased catalytic acitivy at low temperature, but decreased activity at high temperature due to higher cation-pi binding energies
F605Y
-
and mutant with F605 changed to unnatural amino acid O-methyltyrosine. Both show increased catalytic acitivy at low temperature, but decreased activity at high temperature due to higher cation-pi binding energies
G262A
-
the mutant produces hopanol as the main product instead of hop-22(29)-ene. The mutant also produces hop-21(22)ene
I261A
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview; the mutant shows an altered product pattern compared to the wild-type enzyme, overview
P263A
-
mutation located between C29 of the hopanyl cation and the 'front water'; the mutant produces hopanol as the main product instead of hop-22(29)-ene. The mutant also produces hop-21(22)ene
P263G
-
mutation located between C29 of the hopanyl cation and the 'front water'; the mutant produces hopanol as the main product instead of hop-22(29)-ene. The mutant also produces hop-21(22)ene
Q262A
-
mutation located between C29 of the hopanyl cation and the 'front water'
Q262G
-
mutation located between C29 of the hopanyl cation and the 'front water'; the mutant produces hopanol as the main product instead of hop-22(29)-ene. The mutant also produces hop-21(22)ene
Q262G/Q262A/P263G/P263A
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview; the mutant shows an altered product pattern compared to the wild-type enzyme, overview
R127Q
-
mutation located around the 'back waters'; production of hop-22(29)-ene is less throughout the entire temperature range than that by the wild-type. Hop-21(22)ene is not produced
T41A
-
mutation located around the 'back waters'; production of hop-22(29)-ene is less throughout the entire temperature range than that by the wild-type. Hop-21(22)ene is not produced
V380E
inactive mutant; site-directed mutagenesis, inactive mutant
V381A/D376C
inactive mutant; site-directed mutagenesis, inactive mutant
W133A
-
mutation located around the 'back waters'; production of hop-22(29)-ene is less throughout the entire temperature range than that by the wild-type. Hop-21(22)ene is not produced
W169F/W169H/W489A/F605K
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview; the mutant shows an altered product pattern compared to the wild-type enzyme, overview
W23V
-
same activity and optimal temperature as wild type enzyme
W258L
-
60% of wild type activity, lower temperature optimum
W406V
-
no enzyme activity
W417A
-
no enzyme activity
W485V
-
same activity and optimal temperature as wild type enzyme
W522V
-
same activity and optimal temperature as wild type enzyme
W533A
-
same activity and optimal temperature as wild type enzyme
W591L
-
same activity and optimal temperature as wild type enzyme
W78S
-
same activity and optimal temperature as wild type enzyme
Y267A
-
mutation near the substrat channel; production of hop-22(29)-ene is decreased, production of hopanol is markedly increased at lower temperatures
Y420A
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview; the mutant shows an altered product pattern compared to the wild-type enzyme, overview
Y420C
-
site-directed mutagenesis, the mutant performs interconversion of citronellal and isopulegol
Y495F
-
reduced enzyme activity, wild-type product pattern
Y606A
-
kinetics identical to wild-type
Y606A/W23V/W495V/W522V/W533A/W591L/W78S/E35Q/E197Q/D530N/T378A
site-directed mutagenesis, the mutant shows the same product pattern and activity as the wild-type; the mutant shows the same product pattern and activity as the wild-type
Y609A/Y612A/L607K
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview; the mutant shows an altered product pattern compared to the wild-type enzyme, overview
Y612F
-
reduced enzyme activity, wild-type product pattern
Y612F/D376E/D376G/D377E/D377G/D377Q/E45A/E45D/F365W/T41A/E93A/R127Q/W133A/Y267A/F434A/F437A/W258L/D350N/D421N/D442N/H451R/D447N/D377N/D313N/E535Q/D374E
site-directed mutagenesis, the mutant shows the same product pattern as the wild-type with less enzyme activity; the mutant shows the same product pattern as the wild-type with less enzyme activity
Y420C
-
site-directed mutagenesis, the mutant performs interconversion of citronellal and isopulegol
-
F409C
site-directed mutagenesis, the mutant does not perform interconversion of citronellal and isopulegol
F447C
-
site-directed mutagenesis, the mutant performs interconversion of citronellal and isopulegol
F436C
site-directed mutagenesis, the mutant does not perform interconversion of citronellal and isopulegol
F450C
site-directed mutagenesis, the mutant does not perform interconversion of citronellal and isopulegol
F436C
-
site-directed mutagenesis, the mutant does not perform interconversion of citronellal and isopulegol
-
F450C
-
site-directed mutagenesis, the mutant does not perform interconversion of citronellal and isopulegol
-
F445C
-
site-directed mutagenesis, the mutant does not perform interconversion of citronellal and isopulegol
F438C
site-directed mutagenesis, the mutant does not perform interconversion of citronellal and isopulegol
F457C
site-directed mutagenesis, the mutant does not perform interconversion of citronellal and isopulegol
F486C
site-directed mutagenesis, the mutant shows increased activity in interconversion of citronellal and isopulegol compared to the wild-type enzyme
W555A
site-directed mutagenesis, the mutant shows no squalene hopene cyclase activity, and low citronellal cyclase activity
W555C
site-directed mutagenesis, the mutant shows no squalene hopene cyclase activity, and low citronellal cyclase activity
W555D
site-directed mutagenesis, the mutant shows no squalene hopene cyclase activity, and moderate citronellal cyclase activity
W555E
site-directed mutagenesis, the mutant shows highly reduced squalene hopene cyclase activity, and low citronellal cyclase activity
W555F
site-directed mutagenesis, the mutant shows no squalene hopene cyclase activity, and higher citronellal cyclase activity; W555 is essential for hopene formation but W555Y and W555F have enhanced citronellal cyclase activity. All muteins of position W555 show abolished or strongly reduced hopene-forming activity compared to wild-type protein. W555Y is the only mutein with low but significant residual SHC activity
W555G
site-directed mutagenesis, the mutant shows no squalene hopene cyclase activity, and low citronellal cyclase activity
W555H
site-directed mutagenesis, the mutant shows no squalene hopene cyclase activity, and moderate citronellal cyclase activity
W555I
site-directed mutagenesis, the mutant shows no squalene hopene cyclase activity, and low citronellal cyclase activity
W555K
site-directed mutagenesis, the mutant shows no squalene hopene cyclase activity, and low citronellal cyclase activity
W555L
site-directed mutagenesis, the mutant shows no squalene hopene cyclase activity, and low citronellal cyclase activity
W555M
site-directed mutagenesis, the mutant shows highly reduced squalene hopene cyclase activity, and low citronellal cyclase activity
W555N
site-directed mutagenesis, the mutant shows highly reduced squalene hopene cyclase activity, and moderate citronellal cyclase activity
W555P
site-directed mutagenesis, the mutant shows no squalene hopene cyclase activity, and low citronellal cyclase activity
W555Q
site-directed mutagenesis, the mutant shows highly reduced squalene hopene cyclase activity, and low citronellal cyclase activity
W555R
site-directed mutagenesis, the mutant shows no squalene hopene cyclase activity, and low citronellal cyclase activity
W555S
site-directed mutagenesis, the mutant shows no squalene hopene cyclase activity, and low citronellal cyclase activity
W555T
site-directed mutagenesis, the mutant shows no squalene hopene cyclase activity, and higher citronellal cyclase activity
W555V
site-directed mutagenesis, the mutant shows no squalene hopene cyclase activity, and low citronellal cyclase activity
W555Y
site-directed mutagenesis, the mutant shows highly reduced squalene hopene cyclase activity,and higher citronellal cyclase activity; W555 is essential for hopene formation but W555Y and W555F have enhanced citronellal cyclase activity. All muteins of position W555 show abolished or strongly reduced hopene-forming activity compared to wild-type protein. W555Y is the only mutein with low but significant residual SHC activity
F438C
-
site-directed mutagenesis, the mutant performs interconversion of citronellal and isopulegol
-
F486C
-
site-directed mutagenesis, the mutant shows increased activity in interconversion of citronellal and isopulegol compared to the wild-type enzyme
-
W555F
-
site-directed mutagenesis, the mutant shows no squalene hopene cyclase activity, and higher citronellal cyclase activity; W555 is essential for hopene formation but W555Y and W555F have enhanced citronellal cyclase activity. All muteins of position W555 show abolished or strongly reduced hopene-forming activity compared to wild-type protein. W555Y is the only mutein with low but significant residual SHC activity
-
W555Y
-
site-directed mutagenesis, the mutant shows highly reduced squalene hopene cyclase activity,and higher citronellal cyclase activity; W555 is essential for hopene formation but W555Y and W555F have enhanced citronellal cyclase activity. All muteins of position W555 show abolished or strongly reduced hopene-forming activity compared to wild-type protein. W555Y is the only mutein with low but significant residual SHC activity
-
D376E

-
10% enzyme activity
D376E
inactive mutant; site-directed mutagenesis, inactive mutant
E45A

-
reduced enzyme activity
E45A
-
mutation located around the 'back waters'; production of hop-22(29)-ene is less throughout the entire temperature range than that by the wild-type. Hop-21(22)ene is not produced
F605A

-
altered product pattern
F605A
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview; the mutant shows an altered product pattern compared to the wild-type enzyme, overview
Y609F

-
wild type activity, altered product pattern
Y609F
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview; site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview. The phenotype of Y609F mutein is contrarily described in two publications; the mutant shows an altered product pattern compared to the wild-type enzyme, overview
F438C

-
site-directed mutagenesis, the mutant does not perform interconversion of citronellal and isopulegol
F438C
site-directed mutagenesis, the mutant performs interconversion of citronellal and isopulegol
additional information

-
mutations of Y609, Y495, Y612 and Y420 lead to an altered product pattern, compared to wild-type enzyme
additional information
-
overview
additional information
-
modification of critically located Cys residues
additional information
-
various mutations of conserved amino acid residues
additional information
-
replacement of F605 by mono-, di- or trifluorophenylalanine, with or without additional mutation Y606A, kinetic analysis. Mutant F605 changed to trifluorophenylalanine plus mutation Y606A has negligibly small activity
additional information
-
product patterns of mutant enzymes, detailed overview
additional information
product patterns of mutant enzymes, detailed overview
additional information
P73914
knockout of gene slr2089, phenotype and self-complementation by gene slr2089 expression
additional information
-
knockout of gene slr2089, phenotype and self-complementation by gene slr2089 expression
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Ceruti, M.; Balliano, G.; Rocco, F.; Milla, P.; Arpicco, S.; Cattel, L.; Viola, F.
Vinyl sulfide derivatives of truncated oxidosqualene as selective inhibitors of oxidosqualene and squalene-hopene cyclases
Lipids
36
629-636
2001
Alicyclobacillus acidocaldarius
brenda
Dang, T.; Prestwich, G.D.
Site-directed mutagenesis of squalene-hopene cyclase: altered substrate specificity and product distribution
Chem. Biol.
7
643-649
2000
Alicyclobacillus acidocaldarius
brenda
Douka, E.; Koukkou, A.; Drainas, C.; Grosdemange-Billiard, C.; Rohmer, M.
Structural diversity of the triterpenic hydrocarbons from the bacterium Zymomonas mobilis: the signature of defective squalene cyclization by the squalene/hopene cyclase
FEMS Microbiol. Lett.
199
247-251
2001
Zymomonas mobilis
brenda
Feil, C.; Suessmuth, R.; Jung, G.; Poralla, K.
Site-directed mutagenesis of putative active-site residues in squalene-hopene cyclase
Eur. J. Biochem.
242
51-55
1996
Alicyclobacillus acidocaldarius
brenda
Full, C.
Bicyclic triterpenes as new main products of squalene-hopene cyclase by mutation at conserved tyrosine residues
FEBS Lett.
509
361-364
2001
Alicyclobacillus acidocaldarius
brenda
Full, C.; Poralla, K.
Conserved Tyr residues determine functions of Alicyclobacillus acidocaldarius squalene-hopene cyclase
FEMS Microbiol. Lett.
183
221-224
2000
Alicyclobacillus acidocaldarius
brenda
Hoshino, T.; Kouda, M.; Abe, T.; Sato, T.
Functional analysis of Phe605, a conserved aromatic amino acid in squalene-hopene cyclases
Chem. Commun. (Camb.)
2000
1485-1486
2000
Alicyclobacillus acidocaldarius
-
brenda
Hoshino, T.; Sato, T.
Squalene-hopene cyclase: catalytic mechanism and substrate recognition
Chem. Commun. (Camb.)
2000
291-301
2002
Alicyclobacillus acidocaldarius
-
brenda
Kleemann, G.; Kellner, R.; Poralla, K.
Purification and properties of the squalene-hopene cyclase from Rhodopseudomonas palustris, a purple non-sulfur bacterium producing hopanoids and tetrahymanol
Biochim. Biophys. Acta
1210
317-320
1994
Rhodopseudomonas palustris
brenda
Milla, P.; Lenhart, A.; Grosa, G.; Viola, F.; Weihofen, W.A.; Schulz, G.E.; Balliano, G.
Thiol-modifying inhibitors for understanding squalene cyclase function
Eur. J. Biochem.
269
2108-2116
2002
Alicyclobacillus acidocaldarius
brenda
Ochs, D.; Tappe, C.H.; Gaertner, P.; Kellner, R.; Poralla, K.
Properties of purified squalene-hopene cyclase from Bacillus acidocaldarius
Eur. J. Biochem.
194
75-80
1990
Alicyclobacillus acidocaldarius
brenda
Sato, T.; Hoshino, T.
Functional analysis of the DXDDTA motif in squalene-hopene cyclase by site-directed mutagenesis experiments: initiation site of the polycyclization reaction and stabilization site of the carbocation intermediate of the initially cyclized A-ring
Biosci. Biotechnol. Biochem.
63
2189-2198
1999
Alicyclobacillus acidocaldarius
brenda
Sato, T.; Hoshino, T.
Kinetic studies on the function of all the conserved tryptophans involved inside and outside the QW motifs of squalene-hopene cyclase: stabilizing effect of the protein structure against thermal denaturation
Biosci. Biotechnol. Biochem.
63
1171-1180
1999
Alicyclobacillus acidocaldarius
brenda
Sato, T.; Sasahara, S.; Yamakami, T.; Hoshino, T.
Functional analyses of Tyr420 and Leu607 of Alicyclobacillus acidocaldarius squalene-hopene cyclase. Neoachillapentaene, a novel triterpene with the 1,5,6-trimethylcyclohexene moiety produced through folding of the constrained boat structure
Biosci. Biotechnol. Biochem.
66
1660-1670
2002
Alicyclobacillus acidocaldarius
brenda
Schmidt, A.; Bringer-Meyer, S.; Poralla, K.; Sahm, H.
Influence of ethanol on the activities of 3-hydroxy-3-methylglutaryl-coenzyme A-reductase and squalene-hopene-cyclase in Zymomonas mobilis
Appl. Microbiol. Biotechnol.
30
170-175
1989
Zymomonas mobilis
-
brenda
Seckler, B.; Poralla, K.
Characterization and partial purification of squalene-hopene cyclase from Bacillus acidocaldarius
Biochim. Biophys. Acta
881
356-363
1986
Alicyclobacillus acidocaldarius, Alicyclobacillus acidocaldarius 104-IA
-
brenda
Tippelt, A.; Jahnke, L.; Poralla, K.
Squalene-hopene cyclase from Methylococcus capsulatus (Bath): a bacterium producing hopanoids and steroids
Biochim. Biophys. Acta
1391
223-232
1998
Methylococcus capsulatus, Methylococcus capsulatus Bath
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Wendt, K.U.; Lenhart, A.; Schulz, G.E.
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Alicyclobacillus acidocaldarius
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Synthesis and biological activity of new iodoacetamide derivatives on mutants of squalene-hopene cyclase
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Alicyclobacillus acidocaldarius
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Alicyclobacillus acidocaldarius
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Computational study of the mechanism and the relative free energies of binding of anticholesteremic inhibitors to squalene-hopene cyclase
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Alicyclobacillus acidocaldarius (P33247)
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Hoshino, T.; Kumai, Y.; Sato, T.
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Alicyclobacillus acidocaldarius
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Alicyclobacillus acidocaldarius
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Seitz, M.; Syren, P.; Steiner, L.; Klebensberger, J.; Nestl, B.; Hauer, B.
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ChemBioChem
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Alicyclobacillus acidocaldarius, Zymomonas mobilis
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Alicyclobacillus acidocaldarius
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Substrate specificity of a novel squalene-hopene cyclase from Zymomonas mobilis
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Yonemura, Y.; Ohyama, T.; Hoshino, T.
Chemo-enzymatic syntheses of drimane-type sesquiterpenes and the fundamental core of hongoquercin meroterpenoid by recombinant squalene-hopene cyclase
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Alicyclobacillus acidocaldarius
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Englund, E.; Pattanaik, B.; Ubhayasekera, S.J.; Stensjoe, K.; Bergquist, J.; Lindberg, P.
Production of squalene in Synechocystis sp. PCC 6803
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Synechocystis sp. (P73914), Synechocystis sp.
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Hammer, S.; Dominicus, J.; Syrén, P.; Nestl, B.; Hauer, B.
Stereoselective Friedel-Crafts alkylation catalyzed by squalene hopene cyclases
Tetrahedron
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2012
Zymomonas mobilis (Q5NM88), Zymomonas mobilis CP4 (Q5NM88)
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