Enzymes
UniProtKB help_outline | 5 proteins |
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- 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 102 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline lithocholate Identifier CHEBI:29744 Charge -1 Formula C24H39O3 InChIKeyhelp_outline SMEROWZSTRWXGI-HVATVPOCSA-M SMILEShelp_outline [H][C@]12CC[C@]3([H])[C@]([H])(CC[C@]4(C)[C@]([H])(CC[C@@]34[H])[C@H](C)CCC([O-])=O)[C@@]1(C)CC[C@@H](O)C2 2D coordinates Mol file for the small molecule Search links Involved in 16 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 137 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 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline lithocholate sulfate Identifier CHEBI:133940 Charge -2 Formula C24H38O6S InChIKeyhelp_outline AXDXVEYHEODSPN-HVATVPOCSA-L SMILEShelp_outline C1[C@@]2([C@]3(CC[C@]4([C@]([C@@]3(CC[C@@]2(C[C@@H](C1)OS([O-])(=O)=O)[H])[H])(CC[C@@]4([C@H](C)CCC([O-])=O)[H])[H])C)[H])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
Cross-references
RHEA:51064 | RHEA:51065 | RHEA:51066 | RHEA:51067 | |
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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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Structural and chemical profiling of the human cytosolic sulfotransferases.
Allali-Hassani A., Pan P.W., Dombrovski L., Najmanovich R., Tempel W., Dong A., Loppnau P., Martin F., Thornton J., Edwards A.M., Bochkarev A., Plotnikov A.N., Vedadi M., Arrowsmith C.H.
The human cytosolic sulfotransfases (hSULTs) comprise a family of 12 phase II enzymes involved in the metabolism of drugs and hormones, the bioactivation of carcinogens, and the detoxification of xenobiotics. Knowledge of the structural and mechanistic basis of substrate specificity and activity i ... >> More
The human cytosolic sulfotransfases (hSULTs) comprise a family of 12 phase II enzymes involved in the metabolism of drugs and hormones, the bioactivation of carcinogens, and the detoxification of xenobiotics. Knowledge of the structural and mechanistic basis of substrate specificity and activity is crucial for understanding steroid and hormone metabolism, drug sensitivity, pharmacogenomics, and response to environmental toxins. We have determined the crystal structures of five hSULTs for which structural information was lacking, and screened nine of the 12 hSULTs for binding and activity toward a panel of potential substrates and inhibitors, revealing unique "chemical fingerprints" for each protein. The family-wide analysis of the screening and structural data provides a comprehensive, high-level view of the determinants of substrate binding, the mechanisms of inhibition by substrates and environmental toxins, and the functions of the orphan family members SULT1C3 and SULT4A1. Evidence is provided for structural "priming" of the enzyme active site by cofactor binding, which influences the spectrum of small molecules that can bind to each enzyme. The data help explain substrate promiscuity in this family and, at the same time, reveal new similarities between hSULT family members that were previously unrecognized by sequence or structure comparison alone. << Less
PLoS Biol. 5:E97-E97(2007) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.