Enzymes
UniProtKB help_outline | 1 proteins |
Enzyme class help_outline |
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- Name help_outline tetrahymanol Identifier CHEBI:9493 (CAS: 2130-17-8) help_outline Charge 0 Formula C30H52O InChIKeyhelp_outline BFNSRKHIVITRJP-VJBYBJRLSA-N SMILEShelp_outline [H][C@@]12CC[C@]3(C)[C@]([H])(CC[C@]4([H])[C@@]5(C)CC[C@H](O)C(C)(C)[C@]5([H])CC[C@@]34C)[C@@]1(C)CCCC2(C)C 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,048 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline squalene Identifier CHEBI:15440 (Beilstein: 1728920; CAS: 111-02-4) help_outline Charge 0 Formula C30H50 InChIKeyhelp_outline YYGNTYWPHWGJRM-AAJYLUCBSA-N SMILEShelp_outline CC(C)=CCC\C(C)=C\CC\C(C)=C\CC\C=C(/C)CC\C=C(/C)CCC=C(C)C 2D coordinates Mol file for the small molecule Search links Involved in 13 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:30675 | RHEA:30676 | RHEA:30677 | RHEA:30678 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Detection of 1,2-hydride shifts in the formation of euph-7-ene by the squalene-tetrahymanol cyclase of Tetrahymena pyriformis.
Giner J.L., Rocchetti S., Neunlist S., Rohmer M., Arigoni D.
Incubation of samples of 2,3-dihydrosqualene, specifically labeled with deuterium at either carbon position 7 or 11, with an enzyme extract from Tetrahymena pyriformis, containing a squalene-tetrahymanol cyclase, provided specimens of euph-7-enes displaying deuterium patterns consistent with the b ... >> More
Incubation of samples of 2,3-dihydrosqualene, specifically labeled with deuterium at either carbon position 7 or 11, with an enzyme extract from Tetrahymena pyriformis, containing a squalene-tetrahymanol cyclase, provided specimens of euph-7-enes displaying deuterium patterns consistent with the biosynthetic operation of two consecutive 1,2-hydride shifts. << Less
Chem Commun (Camb) 2005:3089-3091(2005) [PubMed] [EuropePMC]
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Purification and some properties of the squalene-tetrahymanol cyclase from Tetrahymena thermophila.
Saar J., Kader J.C., Poralla K., Ourisson G.
The membrane-bound enzyme from Tetrahymena thermophila responsible for the conversion of squalene into the quasi-hopanoid tetrahymanol was purified 297-fold to near homogeneity. Purification involved solubilization by octylthioglucoside, chromatography on DEAE-trisacryl, hydroxyapatite and FPLC io ... >> More
The membrane-bound enzyme from Tetrahymena thermophila responsible for the conversion of squalene into the quasi-hopanoid tetrahymanol was purified 297-fold to near homogeneity. Purification involved solubilization by octylthioglucoside, chromatography on DEAE-trisacryl, hydroxyapatite and FPLC ion-exchange on Mono Q. The apparent KM was found to be 18 microM. 2,3-Iminosqualene and N,N-dimethyldodecylamine-N-oxide are effective inhibitors of the cyclase with I50 values of 50 and 30 nM, respectively. The cyclase has a molecular mass of 72 kDa as judged by electrophoresis in polyacrylamide gels under denaturating conditions. The optimal enzymatic activity was obtained at pH 7.0 and 30 degrees C. The solubilized enzyme needs the presence of detergent for maintaining activity. The influence of different detergents on cyclase activity was studied. Triton X-100 proved to be a strong inactivator of the enzyme. Solubilization of the cyclase in Tween 80 and digitonin inactivates the enzyme. However, its activity can be recovered by complementation of the assay buffer with octylthioglucoside above its critical micellar concentration. We suggest that this approach might be applicable to other membrane-bound proteins. << Less
Biochim. Biophys. Acta 1075:93-101(1991) [PubMed] [EuropePMC]