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- Name help_outline 5α-cholane-3α,7α,12α,24-tetrol Identifier CHEBI:50108 (Beilstein: 5965024) help_outline Charge 0 Formula C24H42O4 InChIKeyhelp_outline BMSROUVLRAQRBY-JLIFGLSWSA-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)CCCO 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 3α,7α,12α-trihydroxy-5α-cholan-24-yl sulfate Identifier CHEBI:58809 (Beilstein: 11197773) help_outline Charge -1 Formula C24H41O7S InChIKeyhelp_outline BKZKSSHAWFCVDU-JLIFGLSWSA-M 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)CCCOS([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:16997 | RHEA:16998 | RHEA:16999 | RHEA:17000 | |
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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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Isolation, partial purification, and characterization of a novel petromyzonol sulfotransferase from Petromyzon marinus (lamprey) larval liver.
Venkatachalam K.V., Llanos D.E., Karami K.J., Malinovskii V.A.
We have isolated, partially purified, and characterized the 5 alpha-petromyzonol (5 alpha-PZ), (5 alpha-cholan-3 alpha, 7 alpha, 12 alpha, 24-tetrahydroxy-) sulfotransferase (PZ-SULT) from larval lamprey liver. Crude liver extracts exhibited a PZ-SULT activity of 0.9120 pmol/min/mg in juvenile and ... >> More
We have isolated, partially purified, and characterized the 5 alpha-petromyzonol (5 alpha-PZ), (5 alpha-cholan-3 alpha, 7 alpha, 12 alpha, 24-tetrahydroxy-) sulfotransferase (PZ-SULT) from larval lamprey liver. Crude liver extracts exhibited a PZ-SULT activity of 0.9120 pmol/min/mg in juvenile and 12.62 pmol/min/mg in larvae. Using crude larval liver extracts and various 5 beta-cholan substrates and allocholic acid there was negligible activity, however, with 5 alpha-PZ and 3-keto-5 alpha-PZ the SULT activity was 231.5 pmol/min/mg and 180.8 pmol/min/mg respectively. This established that the sulfotransferase of lamprey larval liver extracts prefers (5 alpha) substrates and it is selective for hydroxyl at C-24. PZ-SULT was purified through various chromatography procedures. Partially purified PZ-SULT exhibited a pH optimum of 8.0, a temperature optimum of 22 degrees C, and activity was linear for 1h. PZ-SULT exhibited a K(m) of 2.5 microM for PAPS and a K(m) of 8 microM for PZ. The affinity purified peak PZ-SULT exhibited a specific activity of 2,038 pmol/min/mg. The peak protein upon SDS-PAGE, correlated to an Mw 47 kDa. Photoaffinity labeling with PAP(35)S, specifically crosslinked the 47 kDa protein, further confirming the identity of PZ-SULT. Partial amino acid sequencing of the putative 47 kDa PZ-SULT protein yielded a peptide sequence (M)SISQAVDAAFXEI, which possessed an overall (approximately 35-40%) homology with mammalian SULT2B1a. << Less