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Information on EC 5.4.99.17 - squalene-hopene cyclase
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5.4.99.17 squalene-hopene cyclaseIUBMB Comments
The enzyme also produces the cyclization product hopan-22-ol by addition of water (cf. EC 4.2.1.129, squalene-hopanol cyclase). Hopene and hopanol are formed at a constant ratio of 5:1.
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Word Map
- 5.4.99.17
-
cyclization
- acidocaldarius
- alicyclobacillus
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hopanoids
- cyclases
- oxidosqualene
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triterpene
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pentacyclic
- 2,3-oxidosqualene
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tetracyclic
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polyolefinic
- tetrahymanol
- lanosterol
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aspartate-rich
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carbocation
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5.4.99.7
- synthesis
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
AacSHC, cyclase, squalene-hopanoid, SHC, SHC1, SHC2, Spterp25, SQ-hopene cyclase, squalene hopene cyclase, squalene-hopene cyclase, ZmoSHC1, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cyclase, squalene-hopanoid
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SHC
SHC1
SHC2
SQ-hopene cyclase
squalene hopene cyclase
squalene-hopene cyclase
ZmoSHC1
ZmSHC1
SHC
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SHC
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squalene hopene cyclase
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squalene-hopene cyclase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
squalene + H2O = hopan-22-ol
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squalene = hop-22(29)-ene
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squalene = hop-22(29)-ene
catalytic mechanism via Friedel-Crafts alkylation and substrate specificity, overview
squalene = hop-22(29)-ene
catalytic mechanism, the initial reaction catalyzed is the protonation of the terminal double bond of squalene. The conserved DXDD motif of SHCs is essential for this protonation reaction, overview
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squalene = hop-22(29)-ene
catalytic mechanism, the initial reaction catalyzed is the protonation of the terminal double bond of squalene. The conserved DXDD motif of SHCs is essential for this protonation reaction, overview
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squalene = hop-22(29)-ene
catalytic mechanism, the initial reaction catalyzed is the protonation of the terminal double bond of squalene. The conserved DXDD motif of SHCs is essential for this protonation reaction, overview
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squalene = hop-22(29)-ene
catalytic mechanism, the initial reaction catalyzed is the protonation of the terminal double bond of squalene. The conserved DXDD motif of SHCs is essential for this protonation reaction, overview
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squalene = hop-22(29)-ene
catalytic mechanism, the initial reaction catalyzed is the protonation of the terminal double bond of squalene. The conserved DXDD motif of SHCs is essential for this protonation reaction, overview
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squalene = hop-22(29)-ene
catalytic mechanism, the initial reaction catalyzed is the protonation of the terminal double bond of squalene. The conserved DXDD motif of SHCs is essential for this protonation reaction, overview
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squalene = hop-22(29)-ene
catalytic mechanism, the initial reaction catalyzed is the protonation of the terminal double bond of squalene. The conserved DXDD motif of SHCs is essential for this protonation reaction. In Alicyclobacillus acidocaldarius SHC, Asp376 of this motif is hydrogen bonded to His451, and an additional hydrogen bond exists to an ordered water molecule, which connects D376 to the hydroxyl group of the Y495 side chain and thus further enhances its acidity. The carboxyl groups of Asp374 and Asp377 accommodate the positive charge of the D376-H451 pair prior to proton transfer. After proton transfer to the 2,3-double bond of squalene, the D376-H451 pair loses its charge, leaving the remaining negative charge on the D374-D377 pair for stabilization of the initial cationic intermediates (24, 101). Reprotonation of D376 occurs through a water molecule bound to Y495-OH, which can transfer protons from disordered water in the solvent-accessible upper cavity of SHC
squalene = hop-22(29)-ene
overall mechanism of the polycyclization reaction of SHCs and structures of squalene cyclization products, overview
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squalene = hop-22(29)-ene
overall mechanism of the polycyclization reaction of SHCs and structures of squalene cyclization products, overview
squalene = hop-22(29)-ene
catalytic mechanism via Friedel-Crafts alkylation and substrate specificity, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
cyclization
cyclization
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
squalene mutase (cyclizing)
The enzyme also produces the cyclization product hopan-22-ol by addition of water (cf. EC 4.2.1.129, squalene-hopanol cyclase). Hopene and hopanol are formed at a constant ratio of 5:1.
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CAS REGISTRY NUMBER
COMMENTARY
76600-69-6
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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
(23E)-hydroxysqualene
rac-(2R)-2-((3aS,5aR,5bR,7aS,11aS,11bR)-5a,5b,8,8,11a,13b-hexamethylicosahydro-1H-cyclopenta[a]chrysen-3-yl)propanal + rac-(2R)-2-((3aR,5aS,5bS,7aR,11aR,11bS)-5a,5b,8,8,11a,13b-hexamethylicosahydro-1H-cyclopenta[a]chrysen-3-yl)propanal + rac-2-((3aR,5aS,5bS,7aR,11aR,11bS)-5a,5b,8,8,11a,13b-hexamethylicosahydro-1H-cyclopenta[a]chrysen-3-yl)prop-2-en-1-ol
-
-
-
-
?
(23E)-methylsqualene
rac-(5R,9S,10R,13R,14R,17S)-4,4,10,13,14-pentamethyl-17-((E)-6-methyloct-5-en-2-yl)-2,3,4,5,6,9,10,11,12,13,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthrene + rac-(5R,8S,9S,10R,13S,14S)-4,4,8,10,14-pentamethyl-17-((E)-6-methylocta-1,5-dien-2-yl)hexadecahydro-1H-cyclopenta[a]phenanthrene + rac-(3aR,5aS,5bS,7aR,11aR,11bS,13aS)-3-(but-1-en-2-yl)-5a,5b,8,8,11a,13b-hexamethylicosahydro-1H-cyclopenta[a]chrysene + rac-2-((3aR,5aS,5bS,7aR,11aR,11bS,13aS)-5a,5b,8,8,11a,13b-hexamethylicosahydro-1H-cyclopenta[a]chrysen-3-yl)butan-2-ol
-
-
-
-
?
(23Z)-hydroxysqualene
rac-(2R)-2-((3aS,5aR,5bR,7aS,11aS,11bR)-5a,5b,8,8,11a,13b-hexamethylicosahydro-1H-cyclopenta[a]chrysen-3-yl)propanal + rac-(2R)-2-((3aR,5aS,5bS,7aR,11aR,11bS)-5a,5b,8,8,11a,13b-hexamethylicosahydro-1H-cyclopenta[a]chrysen-3-yl)propanal + rac-2-((3aR,5aS,5bS,7aR,11aR,11bS)-5a,5b,8,8,11a,13b-hexamethylicosahydro-1H-cyclopenta[a]chrysen-3-yl)prop-2-en-1-ol + ((9beta,10alpha,13xi,20xi)-20,26-epoxydammar-24-ene)
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-
-
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?
(23Z)-methylsqualene
(23Z)-methylsqualene + rac-(3aR,5aS,5bS,7aR,11aR,11bS,13aS)-3-(but-1-en-2-yl)-5a,5b,8,8,11a,13b-hexamethylicosahydro-1H-cyclopenta[a]chrysene + rac-(3aR,5aS,5bS,7aR,11aR,11bS)-3-((E)-but-2-en-2-yl)-5a,5b,8,8,11a,13b-hexamethylicosahydro-1H-cyclopenta[a]chrysene
-
-
-
-
?
(2E)-methylsqualene
rac-(3aR,5aS,5bS,7aR,11aR,11bS,13aS)-8-ethyl-5a,5b,8,11a,13b-pentamethyl-3-(prop-1-en-2-yl)icosahydro-1H-cyclopenta[a]chrysene
-
-
-
-
?
(2E,6E)-farnesol + geraniol
drimane-8,11-diol + [(1R,2S)-2-[[(2E)-3,7-dimethylocta-2,6-dien-1-yl]oxy]-2,6,6-trimethylcyclohexyl]methanol + 8-O-geranyl-drimane-8,11-diol + drimenol + albicanol
drimane-8,11-diol is the major product of the wild-type enzyme
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-
?
(2E,6E)-farnesol + H2O
8-O-((2E,6E)-farnesyl)-drimane-8,11-diol + drimane-8,11-diol + drimenol + albicanol
drimane-8,11-diol is the major product of the wild-type enzyme
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?
(2E,6E)-farnesol + H2O
[(1S,4aS,8aS)-5,5,8a-trimethyl-2-methylidenedecahydronaphthalen-1-yl]methanol + [(1S,4aS,8aS)-2,5,5,8a-tetramethyl-1,4,4a,5,6,7,8,8a-octahydronaphthalen-1-yl]methanol + (1S,2R,4aS,8aS)-1-(hydroxymethyl)-2,5,5,8a-tetramethyldecahydronaphthalen-2-ol + (1S,2R,4aS,8aS)-1-(hydroxymethyl)-2-O-((2E,6E)-farnesyl)-2,5,5,8a-tetramethyldecahydronaphthalen-2-ol
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?
(2E,6E)-farnesol + n-butanol
drimane-8,11-diol + drimenol + albicanol + 8-O-((2E,6E)-farnesyl)-drimane-8,11-diol + drimane-8,11-diol + farnesyl pentyl ether
drimane-8,11-diol is the major product of the wild-type enzyme
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?
(3R)-2,3-oxidosqualene + H2O
3alpha-hydroxyhopene + 3alpha-hydroxyhopanol
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?
(3S)-2,3-oxidosqualene + H2O
3beta-hydroxyhopene + 3beta-hydroxyhopanol
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?
(6E)-3,7,11-trimethyldodeca-1,6,10-trien-3-ol
(-)-caparrapioxide + (-)-8-epi-caparrapioxide
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?
(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
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via bicyclic C8-cation
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?
(E,E)-homofarnesol
(-)-ambrox + (3aS,5aS,9aS,9bS)-3a,6,6,9a-tetramethyldodeca-hydronaphtho[2,1-b]furan
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-
-
?
(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
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low conversion, NMR spectroscopic analysis
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?
(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
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one of the three major products, NMR spectroscopic analysis
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?
(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
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one of the three major products, NMR spectroscopic analysis
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?
(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
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one of the three major products, NMR spectroscopic analysis
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?
(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
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minor product, NMR spectroscopic analysis
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?
(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
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minor product, NMR spectroscopic analysis
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?
(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
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minor product, NMR spectroscopic analysis
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?
(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
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minor product, NMR spectroscopic analysis
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?
(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
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one of the three major products, yield 19.8%, NMR spectroscopic analysis
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?
(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
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one of the three major products, yield 29.4%, NMR spectroscopic analysis
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?
(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
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one of the three major products, yield 34.8%, NMR spectroscopic analysis
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?
(E,Z)-homofarnesol
(4Z,7aS,11aS)-5,8,8,11a-tetramethyl-2,3,6,7,7a,8,9,10,11,11a-decahydrobenzo[b]oxonine + 9-epi-ambrox
-
-
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?
(R)-citronellal + H2O
(-)-isopulegol + (+)-neoiso-isopulegol
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-
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?
(S)-6,7-epoxygeraniol + H2O
(1S,3R)-3-(hydroxymethyl)-2,2-dimethyl-4-methylidenecyclohexan-1-ol
0.57% conversion with high enzyme concentrations
-
-
?
(S)-citronellal + H2O
(-)-iso-isopulegol
0.59% conversion with high enzyme concentrations
-
-
?
10-ethylsqualene
(2R)-2-[(7E,11E)-3-ethyl-8,12,16-trimethylheptadeca-7,11,15-trien-1-yl]-1,1-dimethyl-3-methylidenecyclohexane + (3R,5aR,9aS)-3-[(5Z)-6,10-dimethylundeca-5,9-dien-2-yl]-3-ethyl-6,6,9a-trimethyl-2,3,5,5a,6,7,8,9,9a,9b-decahydro-1H-cyclopenta[a]naphthalene + (4aS,5R,8aR)-6-ethylidene-1,1,4a-trimethyl-5-[(3E,7E)-4,8,12-trimethyltrideca-3,7,11-trien-1-yl]decahydronaphthalene + (4aR,5S,8aR)-6-ethyl-1,1,4a-trimethyl-5-[(3E,7E)-4,8,12-trimethyltrideca-3,7,11-trien-1-yl]decahydronaphthalene + (2R)-2-[(3E,7E,11E)-3-ethyl-8,12,16-trimethylheptadeca-3,7,11,15-tetraen-1-yl]-1,3,3-trimethylcyclohexanol
-
-
-
-
?
15-ethylsqualene
(2R)-2-[(3E,11E)-8-ethyl-3,12,16-trimethylheptadeca-3,7,11,15-tetraen-1-yl]-1,1-dimethyl-3-methylidenecyclohexane + (4aS,5S,8aR)-5-[(7E)-4-ethyl-8,12-dimethyltrideca-3,7,11-trien-1-yl]-1,1,4a-trimethyl-6-methylidenedecahydronaphthalene + (4aS,5S,8aR)-5-[(7E)-4-ethyl-8,12-dimethyltrideca-3,7,11-trien-1-yl]-1,1,4a,6-tetramethyl-1,2,3,4,4a,5,8,8a-octahydronaphthalene + (2R)-2-[(3E,11E)-8-ethyl-3,12,16-trimethylheptadeca-3,7,11,15-tetraen-1-yl]-1,3,3-trimethylcyclohexanol
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-
-
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?
19-ethylsqualene
(2R)-2-[(3E,7E,11E)-12-ethyl-3,8,16-trimethylheptadeca-3,7,11,15-tetraen-1-yl]-1,1-dimethyl-3-methylidenecyclohexane + (6R)-6-[(3E,7E,11E)-12-ethyl-3,8,16-trimethylheptadeca-3,7,11,15-tetraen-1-yl]-1,5,6-trimethylcyclohexene + (4aS,5S,8aR)-5-[(3E,7E)-8-ethyl-4,12-dimethyltrideca-3,7,11-trien-1-yl]-1,1,4a-trimethyl-6-methylidenedecahydronaphthalene + (5R,8R,9R,10S,14S)-4,4,8,10,14-pentamethyl-17-(7-methyloct-6-en-3-yl)-2,3,4,5,6,7,8,9,10,11,12,14,15,16-tetradecahydro-1H-cyclopenta[a]phenanthrene + (4aS,5S,8aR)-5-[(3E,7E)-9-ethyl-4,12-dimethyltrideca-3,7,11-trien-1-yl]-1,1,4a,6-tetramethyl-1,2,3,4,4a,5,8,8a-octahydronaphthalene + (3S,3aS,5aR,5bR,7aR,11aS,11bS,13aR,13bS)-13b-ethyl-5a,5b,8,8,11a-pentamethyl-3-(prop-1-en-2-yl)icosahydro-1H-cyclopenta[a]chrysene
-
-
-
-
?
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
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-
-
-
?
2-(farnesyldimethylallyl)pyrrole
?
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product is a 10:1 mixture of a tricyclic and a bicyclic unnatural polyprenoid
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?
3,7,11-trimethyldodeca-1,6,10-trien-3-ol
(-)-caparrapioxide + (-)-8-epi-caparrapioxide
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-
-
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?
3-(farnesyldimethylallyl)indole
?
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conversion into a 2:1 mixture of a tetracyclic and a pentacyclic product
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?
6,7-epoxygeraniol
?
-
-
-
?
beta-pinene + H2O
alpha-pinene + terpinolene + 1-methyl-4-(propan-2-yl)cyclohexa-1,3-diene + camphene + 2-(4-methylcyclohexa-1,3-dien-1-yl)propan-2-ol + limonene
-
-
-
?
C33 polyprene
?
-
the enzymatic products consist of mono-, bi-, tri-, tetra- and pentacyclic skeletons, however, hexacyclic products are not generated
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-
?
citronellal + H2O
isopulegol + neo-isopulegol + iso-isopulegol
-
-
-
?
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
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-
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
geraniol + H2O
gamma-cyclogeraniol + cyclogeraniol hydrate
0.4% conversion with high enzyme concentrations
-
-
?
geranyl phenyl ether
(6aS,10aS)-7,7,10a-trimethyl-6a,7,8,9,10,10a-hexahydro-6H-benzo[c]chromene
geranylgeranyl phenyl ether
(14b)-8,13-dimethyl-14-(phenoxymethyl)podocarp-12-ene + (14b)-8-methyl-13-methylidene-14-(phenoxymethyl)podocarpane
-
-
-
?
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
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
-
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
-
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
-
-
-
?
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
-
-
-
-
?
squalene
hop-22(29)-ene
-
-
-
-
?
squalene
hop-22(29)-ene
-
-
-
-
?
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 + 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
-
the enzyme catalyzes cyclization of the linear triterpenoid squalene to hopene and hopanol by the class II mechanism
-
-
?
squalene + H2O
hopan-22-ol
-
-
-
-
?
squalene + H2O
hopan-22-ol
-
-
-
?
squalene + H2O
hopan-22-ol
-
-
-
?
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 6-ethylsqualene
-
-
?
additional information
?
-
no activity with citronellal or isopulegol (2-isopropenyl-5-methyl-cyclohexanol)
-
-
?
additional information
?
-
no activity with geraniol
-
-
?
additional information
?
-
Q81YD8
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
?
-
no activity with citronellal or isopulegol (2-isopropenyl-5-methyl-cyclohexanol)
-
-
?
additional information
?
-
Burkholderia ambifaria ATCC BAA-244 / AMMD
no activity with citronellal or isopulegol (2-isopropenyl-5-methyl-cyclohexanol)
-
-
?
additional information
?
-
Burkholderia ambifaria ATCC BAA-244 / AMMD
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
?
-
-
hydroxysqualene is a poor substrate
-
-
?
additional information
?
-
-
hydroxysqualene is a poor substrate
-
-
?
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
?
-
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
?
-
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
?
-
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.
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
citronellal
isopulegol
-
-
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
-
?
squalene
hop-22(29)-ene
-
-
-
-
?
squalene
hop-22(29)-ene
-
-
-
?
squalene + H2O
hopan-22-ol
-
-
-
-
?
squalene + H2O
hopan-22-ol
-
-
-
?
squalene + H2O
hopan-22-ol
-
-
-
?
additional information
?
-
YP3187836
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
?
-
-
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
?
-
Q81YD8
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
?
-
no activity with citronellal or isopulegol (2-isopropenyl-5-methyl-cyclohexanol)
-
-
?
additional information
?
-
Burkholderia ambifaria ATCC BAA-244 / AMMD
no activity with citronellal or isopulegol (2-isopropenyl-5-methyl-cyclohexanol)
-
-
?
additional information
?
-
Burkholderia ambifaria ATCC BAA-244 / AMMD
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
?
-
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
?
-
no activity with citronellal or isopulegol (2-isopropenyl-5-methyl-cyclohexanol)
-
-
?
additional information
?
-
no activity with citronellal or isopulegol (2-isopropenyl-5-methyl-cyclohexanol)
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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
(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-(allylmethylamino)-hexyloxy)chromen-2-one
-
IC50 4-5 microMol
7-(8'-(dimethylamino-N-octyloxy))chromen-2-one
-
IC50 5-7 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
dodecyltrimethylammonium bromide
-
competitive inhibition, 50% inhibition at 0.0001 mM
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
-
-
(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
-
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.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ethanol
-
1.6fold increase of activity when added to the enzyme test system at a concentration of 6%
Propanol
-
1.6fold increase of activity when added to the enzyme test system at a concentration of 6%
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001
(3S)-2,3-oxidosqualene
-
quintuple mutant, 50°C, pH 6.0
0.0023
(3S)-2,3-oxidosqualene
-
sextuple mutant, 50°C, pH 6.0
0.0279
squalene
-
mutant F605 changed to fluorophenylalanine plus mutation Y606A, pH 6.0, 50°C
0.0324
squalene
-
mutant F605 changed to difluorophenylalanine plus mutation Y606A, pH 6.0, 50°C
0.0352
squalene
-
mutant F365 changed to fluorophenylalanine, pH 6.0, 50°C
0.0416
squalene
-
mutant F365 changed to difluorophenylalanine, pH 6.0, 50°C
0.0479
squalene
-
mutant F6365 changed to trifluorophenylalanine, pH 6.0, 50°C
0.105
squalene
-
mutant F605 changed to O-methyltyrosine, pH 6.0, 40°C
0.152
squalene
-
mutant F605Y changed to O-methyltyrosine, pH 6.0, 50°C
0.185
squalene
-
mutant F365Y changed to O-methyltyrosine, pH 6.0, 50°C
additional information
additional information
-
Km for wild type and mutant enzymes
-
additional information
additional information
-
Km for wild type and mutant enzymes
-
additional information
additional information
-
Km for wild type and mutant enzymes
-
additional information
additional information
-
Km for wild type and mutant enzymes
-
additional information
additional information
-
Km for wild type and mutant enzymes
-
additional information
additional information
-
Km for wild type and mutant enzymes
-
additional information
additional information
-
squalene sextuple mutant: no activity
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.15
squalene
-
mutant F365Y changed to O-methyltyrosine, pH 6.0, 50°C
0.45
squalene
-
mutant F605 changed to O-methyltyrosine, pH 6.0, 40°C
0.54
squalene
-
mutant F605 changed to difluorophenylalanine plus mutation Y606A, pH 6.0, 50°C
0.7
squalene
-
mutant F605Y changed to O-methyltyrosine, pH 6.0, 50°C
0.75
squalene
-
mutant F6365 changed to trifluorophenylalanine, pH 6.0, 50°C
0.82
squalene
-
mutant F605 changed to fluorophenylalanine plus mutation Y606A, pH 6.0, 50°C
0.92
squalene
-
mutant F365 changed to difluorophenylalanine, pH 6.0, 50°C
1.1
squalene
-
mutant F365 changed to fluorophenylalanine, pH 6.0, 50°C
additional information
additional information
-
wild type and mutant enzymes
-
additional information
additional information
-
wild type and mutant enzymes
-
additional information
additional information
-
wild type and mutant enzymes
-
additional information
additional information
-
wild type and mutant enzymes
-
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
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
0.00054
(5-hydroxycarvacryl)trimethylammonium chloride 1-piperidine carboxylate
-
-
additional information
additional information
-
Ki for sulfur-substituted oxidosqualene analogues
-
additional information
additional information
-
Ki for sulfur-substituted oxidosqualene analogues
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
Alicyclobacillus acidocaldarius
-
IC50 5 microMol
0.005
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
0.000281
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
specific activities for wild type and mutant enzymes
additional information
-
specific activities for wild type and mutant enzymes
additional information
-
specific activities for wild type and mutant enzymes
additional information
-
specific activities for wild type and mutant enzymes
additional information
-
enzyme activities in mg/ml of product with different substrates and at different enzyme concentrations, overview
additional information
-
enzyme activities in mg/ml of product with different substrates and at different enzyme concentrations, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
6.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
45
50
50 - 60
55
60
additional information
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
brenda
-
440042, 440043, 440045, 440046, 440047, 440048, 440049, 440051, 440052, 440053, 440054, 440055, 440057
-
-
brenda
formerly Bacillus acidocaldarius, gene shc
Uniprot
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
enzyme SHC in vivo is a membrane-associated protein and can be solubilized from cell extracts by nonionic detergents, such as Triton X-100 or octylthioglucopyranoside. The enzyme is attached to the inner side of the cytoplasmic membrane by interactions of hydrophobic residues with the phospholipids. The membrane-binding part of the enzyme is a nonpolar region that is encircled by positive-charged amino acids enforcing the anchoring of the enzyme to the negatively charged surface of the phospholipid membrane
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
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
metabolism
physiological function
additional information
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
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
-
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
enzyme distribution in the different taxa, overview
metabolism
the enzyme converts squalene into hopene, the substrate for forming hopanoids
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 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 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
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
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 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
-
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 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
the enzyme catalyzes the cyclization of triterpenoids via cationic intermediates in one of the most complex reactions known in biochemistry
additional information
-
structure-function relationships of SHCs, active site structure, overview
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
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
additional information
-
the enzyme catalyzes the cyclization of triterpenoids via cationic intermediates in one of the most complex reactions known in biochemistry
-
Show AA Sequence and Transmembrane Helices (2544 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
71600
72000
74100
75000
76300
75000
-
2 * 75000, SDS-PAGE, enzyme forms aggregates in absence of detergent
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
2 * 75000, SDS-PAGE, enzyme forms aggregates in absence of detergent
additional information
additional information
-
dumbbell-shaped structure of chain A with a more structured beta-barrel structure in domain 1, active site structure, structure analysis, overview
additional information
dumbbell-shaped structure of chain A with a more structured beta-barrel structure in domain 1, active site structure, structure analysis, overview
additional information
-
each subunit consists of alpha-helical domains that build up a dumbbell-shaped structure. The first domain consists of a regular (alpha/alpha)6 barrel structure, whereas the second domain shows an alpha-barrel structure in a less periodic manner
additional information
each subunit consists of alpha-helical domains that build up a dumbbell-shaped structure. The first domain consists of a regular (alpha/alpha)6 barrel structure, whereas the second domain shows an alpha-barrel structure in a less periodic manner
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complexes with 11 human oxidosqualene cyclase inhibitors produced by cocrystallization, elucidation of the structures by X-ray diffraction analyses
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F481C
YP3187836
site-directed mutagenesis, the mutant performs interconversion of citronellal and isopulegol
C435S/D374I/D374V/H451F
D376C
D376E
D376G
-
0.2% activity when enzyme concentration is increased to 100fold
D377C/D377N/Y612A
D377E
-
0.2% activity when enzyme concentration is increased to 100fold
D377E/D376Q/D376R/D377R/E45K/W406V/W417A/D377C
D377G
-
0.2% activity when enzyme concentration is increased to 100fold
D377Q
-
0.2% activity when enzyme concentration is increased to 100fold
E45A
E93A
F365A
F365C
F365G
the mutant shows increased activity with (S)-6,7-epoxygeraniol and no activity with geraniol compared to the wild type enzyme
F365W
F365Y
-
and mutant with F365 changed to unnatural amino acid O-methyltyrosine. Both show increased decreased activity at high temperature
F434A
F437A
F601A
F605A
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
G600F
the mutant exhibits 68% conversion of geraniol to cyclogeraniol hydrate
I261A
I261W
the mutant shows increased activity with (S)-6,7-epoxygeraniol and no activity with geraniol compared to the wild type enzyme
L36A
the mutant shows increased activity with (S)-6,7-epoxygeraniol compared to the wild type enzyme
P263A
P263G
Q262A
-
mutation located between C29 of the hopanyl cation and the "front water"
Q262G
Q262G/Q262A/P263G/P263A
R127Q
S307A
the mutant shows increased activity with (S)-6,7-epoxygeraniol and no activity with geraniol compared to the wild type enzyme
T41A
V380E
V381A/D376C
W133A
W169A
W169F/W169H/W489A/F605K
W23V
-
same activity and optimal temperature as wild type enzyme
W312G
-
the mutant produces (-)-neo-isopulegol from (S)-citronellal
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
Y420A
Y420C
Y420W
the mutant exhibits 54% conversion of (S)-6,7-epoxygeraniol to (1S,3R)-3-(hydroxymethyl)-2,2-dimethyl-4-methylidenecyclohexan-1-ol
Y420W/G600F
the mutant exhibits 78% conversion of (S)-6,7-epoxygeraniol to (1S,3R)-3-(hydroxymethyl)-2,2-dimethyl-4-methylidenecyclohexan-1-ol
Y606A/W23V/W495V/W522V/W533A/W591L/W78S/E35Q/E197Q/D530N/T378A
Y609A
-
the mutant produces (+)-isopulegol from (S)-citronellal
Y609A/Y612A/L607K
Y609F
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
Y420C
-
site-directed mutagenesis, the mutant performs interconversion of citronellal and isopulegol
-
A306F
the mutant produces apolypodatetraene, gamma-polypodatetraene and neopolypoda-5(6),13,17,21-teraene from squalene and polypoda-8(9),13,17,21-tetraen-3a-ol, polypoda-7(8),13,17,21-tetraen-3alpha-ol and polypoda-7(8),13,17,21-tetraen-3beta-ol from a racemic mixture of (3S)-2,3-oxidosqualene and (3R)-2,3-oxidosqualene
A306T
the mutant produces (20R)-dammara-13(17),24-dien-3a-ol, (20R)-dammara-13(17),24-dien-3b-ol, (20R)-dammara-12(13),24-dien-3a-ol, (20R)-dammara-12(13),24-dien-3b-ol and (20R,24R)-17-epi-epoxydammarane from a racemic mixture of (3S)-2,3-oxidosqualene and (3R)-2,3-oxidosqualene
A306V
the mutant produces apolypodatetraene, dammara-13(17)-24-diene, gamma-polypodatetraene, (17E)(13aH)-malabarica-14(27),17,21-triene, (20R)-dammara-12(13),24-diene, (20R)-eupha-7(8),24-diene, (20S)-tirucalla-7(8),24-diene, and 17-epi-dammara-20(21),24-diene from squalene
F129L
the mutant shows a (E,E)-homofarnesol conversion at 24 h of reaction which is comparable to the wild type enzyme
F129L/F601Y
the mutant shows lower (E,E)-homofarnesol conversion at 24 h of reaction compared to the wild type enzyme
F129L/M132R/I432T
the mutant shows much lower (E,E)-homofarnesol conversion at 24 h of reaction compared to the wild type enzyme
F129L/M132R/I432T/F601Y
the mutant shows much lower (E,E)-homofarnesol conversion compared to the wild type enzyme
F365C
the mutant is able to convert geraniol into (S)-gamma-cyclogeraniol and cyclogeraniol hydrate
F601Y
the mutant shows a (E,E)-homofarnesol conversion at 24 h of reaction which is comparable to the wild type enzyme
G600F
the mutant is able to convert geraniol into (S)-gamma-cyclogeraniol and cyclogeraniol hydrate
I261A
the mutant exclusively converts (S)-citronellal to ( -)-iso-isopulegol isomer (1R,2S,5S)-5-methyl-2-(prop-1-en-2-yl)cyclohexan-1-ol with an 11times improved activity as compared to the wild type enzyme
L607F
the mutant produces the farnesyl ether with 6times higher yield from farnesol than the wild type enzyme
M132R/A224V/I432T
the mutant shows better (E,E)-homofarnesol conversion at 24 h of reaction compared to the wild type enzyme
M132R/I432T
the mutant shows better (E,E)-homofarnesol conversion at 24 h of reaction compared to the wild type enzyme
M132R/I432T/F601Y
the mutant shows much lower (E,E)-homofarnesol conversion at 24 h of reaction compared to the wild type enzyme
Q579H/F601Y
the mutant shows better (E,E)-homofarnesol conversion at 24 h of reaction compared to the wild type enzyme
T77A/I92V/F129L
the mutant shows better (E,E)-homofarnesol conversion at 24 h of reaction compared to the wild type enzyme
Y420W/G600F
the mutant produces selectively (1S)-3-(hydroxymethyl)-2,2-dimethyl-4-methylidenecyclohexan-1-ol from 6,7-epoxygeraniol with a conversion of up to 78%
F409C
Q81YD8
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
Burkholderia ambifaria ATCC BAA-244 / AMMD
-
site-directed mutagenesis, the mutant does not perform interconversion of citronellal and isopulegol
-
F450C
Burkholderia ambifaria ATCC BAA-244 / AMMD
-
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
F438C
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
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
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
W555Y
additional information
C435S/D374I/D374V/H451F
site-directed mutagenesis, inactive mutant
D377C/D377N/Y612A
the mutant shows an altered product pattern compared to the wild-type enzyme, overview
D377C/D377N/Y612A
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview
D377E/D376Q/D376R/D377R/E45K/W406V/W417A/D377C
inactive mutant
D377E/D376Q/D376R/D377R/E45K/W406V/W417A/D377C
site-directed mutagenesis, inactive mutant
E45A
-
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
E93A
-
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
the mutant shows an altered product pattern compared to the wild-type enzyme, overview
F365A
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview
F365A
the mutant shows increased activity with geraniol and (S)-6,7-epoxygeraniol compared to the wild type enzyme
F365C
the mutant exhibits 15% conversion of geraniol to gamma-cyclogeraniol
F365C
the mutant shows increased activity with geraniol compared to the wild type enzyme
F434A
-
production of hop-22(29)-ene is decreased, production of hopanol is markedly increased at lower temperatures
F437A
-
production of hop-22(29)-ene is decreased, production of hopanol is markedly increased at lower temperatures
F601A
the mutant shows an altered product pattern compared to the wild-type enzyme, overview
F601A
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview
F605A
the mutant shows an altered product pattern compared to the wild-type enzyme, overview
F605A
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview
I261A
the mutant shows an altered product pattern compared to the wild-type enzyme, overview
I261A
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview
I261A
the mutant exhibits 11% conversion of citronellal to (-)-iso-isopulegol. The mutant shows increased activity with geraniol and (S)-6,7-epoxygeraniol compared to the wild type enzyme
I261A
-
the mutant has higher activity with (S)-citronellal compared to the wild type enzyme
P263A
-
mutation located between C29 of the hopanyl cation and the "front water"
P263A
-
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"
P263G
-
the mutant produces hopanol as the main product instead of hop-22(29)-ene. The mutant also produces hop-21(22)ene
Q262G
-
mutation located between C29 of the hopanyl cation and the "front water"
Q262G
-
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
the mutant shows an altered product pattern compared to the wild-type enzyme, overview
Q262G/Q262A/P263G/P263A
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview
R127Q
-
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
-
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
V381A/D376C
site-directed mutagenesis, inactive mutant
W133A
-
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
W169A
-
the mutant has higher activity with (S)-citronellal compared to the wild type enzyme
W169F/W169H/W489A/F605K
the mutant shows an altered product pattern compared to the wild-type enzyme, overview
W169F/W169H/W489A/F605K
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview
Y267A
-
production of hop-22(29)-ene is decreased, production of hopanol is markedly increased at lower temperatures
Y420A
the mutant shows an altered product pattern compared to the wild-type enzyme, overview
Y420A
site-directed mutagenesis, 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
Y606A/W23V/W495V/W522V/W533A/W591L/W78S/E35Q/E197Q/D530N/T378A
the mutant shows the same product pattern and activity as the 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
Y609A/Y612A/L607K
the mutant shows an altered product pattern compared to the wild-type enzyme, overview
Y609A/Y612A/L607K
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview
Y609F
the mutant shows an altered product pattern compared to the wild-type enzyme, overview
Y609F
site-directed mutagenesis, the mutant shows an altered product pattern compared to the wild-type enzyme, overview
Y609F
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
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
the mutant shows the same product pattern as the wild-type with less enzyme activity
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
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
W555F
site-directed mutagenesis, the mutant shows no squalene hopene cyclase activity, and higher citronellal cyclase activity
W555F
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
W555Y
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
W555F
-
site-directed mutagenesis, the mutant shows no squalene hopene cyclase activity, and higher citronellal cyclase activity
-
W555F
-
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
-
W555Y
-
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
-
additional information
-
modification of critically located Cys residues
additional information
-
various mutations of conserved amino acid residues
additional information
-
mutations of Y609, Y495, Y612 and Y420 lead to an altered product pattern, compared to wild-type enzyme
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
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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
-
wild type enzyme: 50% loss of activity after 120 min, D376E mutant: 50% loss of activity after 100 min
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
bicontinuous microemulsions can be used as reaction media for enzyme-catalysed reactions
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native and/or recombinant enzyme, the enzyme in vivo is a membrane-associated protein and can be solubilized from cell extracts by nonionic detergents, such as Triton X-100 or octylthioglucopyranoside
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparison, expression in Escherichia coli strain DH5alpha
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli JM 105
gene shc, DNA and amino acid sequence determination, expression in Escherichia coli
gene slr2089, DNA and amino acid sequence determination and analysis, sequence comparison, expression in Escherichia coli strain DH5alpha
-
-
DNA and amino acid sequence determination and analysis, sequence comparison, expression in Escherichia coli strain DH5alpha
-
DNA and amino acid sequence determination and analysis, sequence comparison, expression in Escherichia coli strain DH5alpha
-
DNA and amino acid sequence determination and analysis, sequence comparison, expression in Escherichia coli strain DH5alpha
-
DNA and amino acid sequence determination and analysis, sequence comparison, expression in Escherichia coli strain DH5alpha
-
DNA and amino acid sequence determination and analysis, sequence comparison, expression in Escherichia coli strain DH5alpha
-
DNA and amino acid sequence determination and analysis, sequence comparison, expression in Escherichia coli strain DH5alpha
-
DNA and amino acid sequence determination and analysis, sequence comparison, expression in Escherichia coli strain DH5alpha
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
production of unnatural polyprenoids and supranatural steroids by manipulation of the enzyme reaction by combination of substrate analogues
synthesis
cyclization of homofarnesol to ambroxan as well as the conversion of citronellal to 2-isopropenyl-5-methyl-cyclohexanol bythe isozyme SHC1 can be economically attractive, as both products are used in the flavour and fragrance industry
synthesis
it is possible to use the cyanobacterium Synechocystis to generate squalene, a hydrocarbon of commercial interest and a potential biofuel
synthesis
-
cyclization of homofarnesol to ambroxan as well as the conversion of citronellal to 2-isopropenyl-5-methyl-cyclohexanol bythe isozyme SHC1 can be economically attractive, as both products are used in the flavour and fragrance industry
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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.
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