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- Name help_outline 5β-scymnol Identifier CHEBI:50106 (Beilstein: 5451487; CAS: 6785-34-8) help_outline Charge 0 Formula C27H48O6 InChIKeyhelp_outline DIPHJTHZUWDJIK-JPLAUYQNSA-N SMILEShelp_outline [H][C@@]12C[C@H](O)CC[C@]1(C)[C@@]1([H])C[C@H](O)[C@]3(C)[C@]([H])(CC[C@@]3([H])[C@]1([H])[C@H](O)C2)[C@H](C)CC[C@@H](O)C(CO)CO 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 3'-phosphoadenylyl sulfate Identifier CHEBI:58339 Charge -4 Formula C10H11N5O13P2S InChIKeyhelp_outline GACDQMDRPRGCTN-KQYNXXCUSA-J SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OS([O-])(=O)=O)[C@@H](OP([O-])([O-])=O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 125 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 5β-scymnol sulfate Identifier CHEBI:58808 (Beilstein: 7697279) help_outline Charge -1 Formula C27H47O9S InChIKeyhelp_outline JKUSPYUETNXNRO-JWBDLDPOSA-M SMILEShelp_outline [H][C@@]12C[C@H](O)CC[C@]1(C)C1C[C@H](O)[C@]3(C)[C@]([H])(CC[C@@]3([H])[C@]1([H])[C@H](O)C2)[C@H](C)CC[C@@H](O)C(CO)COS([O-])(=O)=O 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 adenosine 3',5'-bisphosphate Identifier CHEBI:58343 Charge -4 Formula C10H11N5O10P2 InChIKeyhelp_outline WHTCPDAXWFLDIH-KQYNXXCUSA-J SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])([O-])=O)[C@@H](OP([O-])([O-])=O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 159 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,932 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:15477 | RHEA:15478 | RHEA:15479 | RHEA:15480 | |
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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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Enzymic sulfation of bile salts. Partial purification and characterization of an enzyme from the liver of the shark Heterodontus portusjacksoni that catalyses the sulfation of the shark bile steroid 5 beta-scymnol.
Macrides T.A., Faktor D.A., Kalafatis N., Amiet R.G.
An enzyme system which catalyses the transfer of the sulfate group from 3'-phosphoadenosine-5'-phosphosulfate to the bile steroid 5 beta-scymnol has been isolated and characterized from the liver of the shark Heterodontus portusjacksoni (Meyer 1793). The enzyme is present in the cytosol fraction o ... >> More
An enzyme system which catalyses the transfer of the sulfate group from 3'-phosphoadenosine-5'-phosphosulfate to the bile steroid 5 beta-scymnol has been isolated and characterized from the liver of the shark Heterodontus portusjacksoni (Meyer 1793). The enzyme is present in the cytosol fraction of liver cells. It was partially purified by hydroxylapatite chromatography, molecular sizing by G100-Sephadex and isoelectrofocusing electrophoresis. The apparent Km value for 3'-phosphoadenosine-5'-phosphosulfate was 4 microM and that for 5 beta-scymnol, 14 microM. The enzyme activity is inhibited by iodoacetate and p-chloromercuribenzoate indicating the possible requirement of a sulfhydryl group for activity. The molecular weight of the enzyme was estimated to be 40 kDa by gel filtration. This was verified by running the partially purified material on a native gel and electrophoretically separating two major bands corresponding to molecular weights of 40 and 45 kDa, respectively. Isoelectric focusing of the purified material resulted in two major bands with pI values of 5.0 and 5.85. Enzymatic activity was found to be optimal at a pH of 6.5 with little activity recorded at pH 5.0 and 8.0. << Less
Comp Biochem Physiol Biochem Mol Biol 107:461-469(1994) [PubMed] [EuropePMC]