Ask about this productRelated genes to: SULT6B1 Blocking Peptide
- Gene:
- SULT6B1 NIH gene
- Name:
- sulfotransferase family 6B member 1
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 2p22.2
- Locus Type:
- gene with protein product
- Date approved:
- 2007-07-26
- Date modifiied:
- 2015-11-06
Related products to: SULT6B1 Blocking Peptide
Related articles to: SULT6B1 Blocking Peptide
- F-53B, primarily composed of 6:2 chlorinated polyfluoroalkyl ether sulfonate (Cl-PFESA) and 8:2 Cl-PFESA, has been widely used as an alternative to perfluorooctane sulfonic acid (PFOS), but emerging evidence indicates that F-53B also exhibits toxicity and may not be a safe substitute. We conducted systematic molecular interaction analysis between three compounds - PFOS, 6:2 Cl-PFESA, and 8:2 Cl-PFESA - and 19,508 human proteins using AlphaFold3-predicted three-dimensional structures combined with AutoDock Vina molecular docking. Binding affinity distributions, compound-specific binding patterns, and functional enrichment analyses were performed to identify differential toxicity mechanisms. This study completed a total of 58,496 molecular docking calculations between the three compounds and human proteins. 8:2 Cl-PFESA demonstrated the strongest overall binding capacity, with top-ranked binding targets including emopamil-binding protein-like protein (EBPL) and lanosterol synthase (LSS). In comparison, PFOS showed highest-ranked binding to olfactory receptor 5D14 (OR5D14), while 6:2 Cl-PFESA preferentially bound to sulfotransferase 6B1 (SULT6B1). For ultra-strong binding targets with binding affinity ≤ -10.0 kcal/mol, 8:2 Cl-PFESA exhibited 413 targets, 6:2 Cl-PFESA showed 98 targets, and PFOS had 78 targets. Functional enrichment analysis revealed significant enrichment in olfactory transduction pathways across all compounds, suggesting potential impacts on chemosensory functions. Additionally, 8:2 Cl-PFESA showed preferential binding to cholesterol synthesis enzymes, while 6:2 Cl-PFESA demonstrated interactions with epigenetic regulatory enzymes, including histone deacetylase 11 (HDAC11) and sirtuin 6 (SIRT6). The findings suggest that F-53B, particularly its 8:2 Cl-PFESA component, may exhibit enhanced toxicity potential compared to PFOS across multiple molecular dimensions. These computational predictions require experimental validation through in vitro binding assays, cell-based toxicity tests, and in vivo studies. - Source: PubMed
Publication date: 2025/10/13
Li HaoranChen NannanYu BoPeng YiYuan YeGuo HuicaiZhang Zhiqing - Aryl hydrocarbon receptor (AhR), a ligand-activated transcription factor, is crucial in maintaining the skeletal system. Our study focuses on encapsulating the role of AhR in bone biology and identifying novel signaling pathways in musculoskeletal pathologies using the GEO dataset. The GEO2R analysis identified 8 genes (CYP1C1, SULT6B1, CYB5A, EDN1, CXCR4B, CTGFA, TIPARP, and CXXC5A) involved in the AhR pathway, which play a pivotal role in bone remodeling. The AhR knockout in hematopoietic stem cells showed alteration in several novel bone-related transcriptomes (eg, Defb14, ZNF 51, and Chrm5). Gene Ontology Enrichment Analysis demonstrated 54 different biological processes associated with bone homeostasis. Mainly, these processes include bone morphogenesis, bone development, bone trabeculae formation, bone resorption, bone maturation, bone mineralization, and bone marrow development. Employing Functional Annotation and Clustering through DAVID, we further uncovered the involvement of the xenobiotic metabolic process, p450 pathway, oxidation-reduction, and nitric oxide biosynthesis process in the AhR signaling pathway. The conflicting evidence of current research of AhR signaling on bone (positive and negative effects) homeostasis may be due to variations in ligand binding affinity, binding sites, half-life, chemical structure, and other unknown factors. In summary, our study provides a comprehensive understanding of the underlying mechanisms of the AhR pathway in bone biology. - Source: PubMed
Publication date: 2024/05/15
Vyavahare SagarAhluwalia PankajGupta Sonu KumarKolhe RavindraHill William DHamrick MarkIsales Carlos MFulzele Sadanand - Cytosolic sulfotransferases (SULTs) catalyze phase II (conjugation) reactions of drugs and endogenous compounds. A complete set of recombinant fission yeast strains each expressing one of the 14 human SULTs was generated, including SULT4A1 and SULT6B1. Sulfation of test substrates by whole-cell biotransformation was successfully demonstrated for all enzymes for which substrates were previously known. The results proved that the intracellular production of the cofactor 3'-phosphoadenosine 5'-phosphosulfate (PAPS) necessary for SULT activity in fission yeast is sufficiently high to support metabolite production. A modified variant of sulfotransferase assay was also developed that employs permeabilized fission yeast cells (enzyme bags). Using this approach, SULT4A1-dependent sulfation of 1-naphthol was observed. Additionally, a new and convenient SULT activity assay is presented. It is based on the sulfation of a proluciferin compound, which was catalyzed by SULT1E1, SULT2A1, SULT4A1, and SULT6B1. For the latter two enzymes this study represents the first demonstration of their enzymatic functionality. Furthermore, the first catalytically competent homology models for SULT4A1 and SULT6B1 in complex with PAPS are reported. Through mechanistic molecular modeling driven by substrate docking, we pinned down the increased activity levels of these two isoforms to optimized substrate binding. - Source: PubMed
Publication date: 2020/11/06
Sun YananMachalz DavidWolber GerhardParr Maria KristinaBureik Matthias - Nevirapine, a non-nucleoside reverse transcriptase inhibitor used for the treatment of AIDS, can cause serious skin rashes and hepatotoxicity. Previous studies have indicated that the benzylic sulfate 12-sulfoxynevirapine, the formation of which is catalyzed by human sulfotransferases (SULTs), may play a causative role in these toxicities. To characterize better the role of 12-sulfoxynevirapine in nevirapine-induced cytotoxicity, the ability of 12 expressed human SULT isoforms to conjugate 12-hydroxynevirapine was assessed. Of the 12 human SULTs, no detectable 12-sulfoxynevirapine was observed with SULT1A3, SULT1C2, SULT1C3, SULT2B1, SULT4A1, or SULT6B1. As determined by the V/K ratio, SULT2A1 had the highest overall 12-hydoxynevirapine sulfonation activity; lower activities were observed with SULT1A1, SULT1A2, SULT1B1, SULT1C4, and SULT1E1. Incubation of 12-sulfoxynevirapine with glutathione and cysteine led to adduct formation; lower yields were obtained with deoxynucleosides. 12-Hydroxynevirapine was more cytotoxic than nevirapine to TK6, TK6/SULT vector, and TK6/SULT2A1 cells. With nevirapine, there was no difference in cytotoxicity among the three cell lines, whereas with 12-hydroxynevirapine, TK6/SULT2A1 cells were more resistant than TK6 and TK6/SULT vector cells. Co-incubation of 12-hydroxynevirapine with the competitive SULT2A1 substrate dehydroepiandrosterone decreased the level of 12-sulfoxynevirapine and increased the cytotoxicity in TK6/SULT2A1 cells. These data demonstrate that although 12-sulfoxynevirapine reacts with nucleophiles to form adducts, sulfonation of 12-hydroxynevirapine decreases the cytotoxicity of 12-hydroxynevirapine in TK6 cells. - Source: PubMed
Publication date: 2018/07/18
Fang Jia-LongLoukotková LucieChitranshi PriyankaGamboa da Costa GonçaloBeland Frederick A - Tolvaptan, a vasopressin receptor 2 antagonist used to treat hyponatremia, has recently been reported to be associated with liver injury. Sulfotransferases (SULTs) have been implicated as important detoxifying and/or activating enzymes for numerous xenobiotics, drugs, and endogenous compounds. To characterize better the role of SULTs in tolvaptan metabolism, HEK293 cells stably overexpressing 12 human SULTs were generated. Using these cell lines, the extent of tolvaptan sulfate formation was assessed by reversed-phase high-performance liquid chromatography through comparison to a synthetic standard. Of the 12 known human SULTs, no detectable sulfation of tolvaptan was observed with SULT1A1, SULT1A2, SULT1A3, SULT1C2, SULT1C4, SULT4A1, or SULT6B1. The affinity of individual SULT isozymes, as determined by Km analysis, was SULT1C3 >> SULT2A1 > SULT2B1 ∼ SULT1B1 > SULT1E1. The half inhibitory concentration of tolvaptan on cell growth in HEK293/SULT1C3 cells and HEK293/CYP3A4 & SULT1C3 cells was significantly lower than that in the corresponding HEK293/vector cells or HEK293/CYP3A4 & SULT vector cells. Moreover, exposing cells to tolvaptan in the presence of cyclosporine A, an inhibitor of the drug efflux transporters, significantly increased the intracellular levels of tolvaptan sulfate and decreased the cell viability in HEK293/SULT1C3 cells. These data indicate that sulfation increased the cytotoxicity of tolvaptan. - Source: PubMed
Publication date: 2015/12/10
Fang Jia-LongWu YuanfengGamboa da Costa GonçaloChen SiChitranshi PriyankaBeland Frederick A