Recombinant Human SULT1A3
- Known as:
- Recombinant Human SULT1A3
- Catalog number:
- CG03
- Product Quantity:
- 10ug
- Category:
- -
- Supplier:
- Novoprotein
- Gene target:
- Recombinant Human SULT1A3
Related genes to: Recombinant Human SULT1A3
- Gene:
- SULT1A3 NIH gene
- Name:
- sulfotransferase family 1A member 3
- Previous symbol:
- STM
- Synonyms:
- TL-PST
- Chromosome:
- 16p11.2
- Locus Type:
- gene with protein product
- Date approved:
- 1994-05-18
- Date modifiied:
- 2015-11-06
Related products to: Recombinant Human SULT1A3
Related articles to: Recombinant Human SULT1A3
- Diabetes mellitus is characterized by persistent hyperglycemia that triggers micro-vascular complications in organs such as the eyes and kidneys; a pivotal enzymatic driver is aldose reductase (AR), which reduces glucose to sorbitol. Because existing AR inhibitors often cause off-target toxicity, we implemented an integrative in-silico workflow to discover selective, safer compounds. A library of 4 975 small molecules was docked against AR and, in parallel, against five clinically relevant antitarget proteins or proteins whose unintended inhibition is associated with adverse pharmacological or toxicological effects (CYP2A6, CYP2C9, CYP3A4, SULT1A3 and the pregnane X receptor), retaining 236 ligands whose binding energies to every antitarget were weaker than those of the reference drug tolrestat. These survivors were redocked to five high-resolution human AR crystal structures, and the ten best-scoring ligands underwent 100 ns molecular-dynamics simulations followed by MM-PBSA free-energy calculations to refine affinity estimates and probe complex stability. Ligand 4934, a benzo[a]anthracene-pyrene polyphenol, displayed the strongest predicted affinity for while showing poor affinity for the antitarget panel, outperforming tolrestat by more than 2 kcal mol⁻¹ and adopting a stable plug-like pose that occludes the catalytic pocket through extensive π-π and hydrophobic contacts with Trp111, Phe123 and Lys22. These findings highlight ligand 4934 as a promising scaffold for selective AR inhibition and demonstrate the effectiveness of the stepwise computational strategy in prioritizing lead compounds with reduced off-target liabilities. - Source: PubMed
Publication date: 2025/08/01
Rojas Jicli JosePestana-Nobles RobertoPacheco-Londono Leonardo CUtria-Munive JesúsGalan-Freyle Nataly J - Sulfotransferase (SULT) enzymes contribute significantly to drug metabolism in pediatric patients. The purpose of this study was to develop a PBPK model for acetaminophen (APAP) in pediatric populations that accounts for the ontogeny of SULT isozymes that play a critical role in APAP metabolism. PBPK modeling and simulation were performed using the Simcyp Simulator. The model incorporated the developmental ontogeny of three key hepatic SULT enzymes: SULT1A1, SULT1A3, and SULT2A1 using "best-fit" ontogeny equations for each isozyme as determined by nonlinear regression analysis of enzyme abundance versus age. PBPK model-simulated pharmacokinetic profiles for APAP captured observed clinical data for systemic exposure (Cmax, AUC) in neonates, infants, and children. SULTS accounted for ~60% APAP metabolism in neonates, with decreased contributions to infants and children. Model sensitivity analysis highlighted the potential for APAP metabolic DDIs, primarily through SULT1A1. The study demonstrates that the impact of SULT enzymes on drug metabolism is significant in neonates, which is an important clinical consideration for APAP. A PBPK model that incorporates SULT ontogeny has the potential to help inform dosing decisions in this special patient population. - Source: PubMed
Publication date: 2025/07/13
Sharma SoniaTaft David R - Chlorophenols (CPs) are common organic pollutants widely used in many industries. The current study seeks to examine the inhibition of sulfotransferases (SULTs) by CPs. Four SULT isoforms were significantly inhibited by multiply CPs. Furthermore, half inhibition concentration (IC) was calculated to be 0.31 μM, 0.11 μM and 1.86 μM for the inhibition of PCP (pentachlorophenol) towards SULT1A1, SULT1B1 and SULT1E1. PCP showed competitive inhibition towards SULT1B1 and SULT1E1.The inhibition kinetics (inhibition type and parameters (K)) values were calculated to be 0.34 μM and 0.56 μM for the inhibition of PCP towards SULT1B1 and SULT1E1, respectively. In silico docking was used to explain the inhibition difference among CPs. The binding free energy between 4-CP and SULT1A3 was -4.92 kcal/mol, and the binding free energy between 2.4-DCP and SULT1A3 was -5.63 kcal/mol. Therefore, 2.4-DCP exerted stronger inhibition activity towards SULT1A3 compared with 4-CP, which can well explain the experimental result. These results are crucial for exploring the risks associated with CPs exposure from a novel perspective. - Source: PubMed
Publication date: 2025/01/23
Yang KaiQin Guo-QiangJia Zi-ZhuoGan QiangqiangJia Ruo-YongZhang WeiLiu Yong-ZheFang Zhong-Ze - Hydroxyapatite-based nanoparticles have found diverse applications in drug delivery, gene carriers, diagnostics, bioimaging and tissue engineering, owing to their ability to easily enter the bloodstream and target specific sites. However, there is limited understanding of the potential adverse effects and molecular mechanisms of these nanoparticles with varying geometries upon their entry into the bloodstream. Here, we used two commercially available hydroxyapatite nanoparticles (HANPs) with different geometries (less than 100 nm in size each) to investigate this issue. - Source: PubMed
Publication date: 2024/08/23
Sun WeitangZhong JingbinGao BuyunFeng JielingYe ZijieLin YuelingZhang KelanSu WenqiZhu ShiboLi YinghuaJia Wei - In recent years, a convenient phosphatase-coupled sulfotransferase assay method has been proven to be applicable to most sulfotransferases. The central principle of the method is that phosphatase specifically degrades 3'-phosphoadenosine-5'-phosphate (PAP) and leaves 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Our group previously acquired a yeast 3',5'-bisphosphate nucleotidase (YND), which showed a higher catalytic activity for PAP than PAPS and could be a potential phosphatase for the sulfotransferase assay. Here, we obtained a beneficial mutant of YND with markedly improved substrate specificity towards PAP via rational design. Of 9 chosen mutation sites in the active site pocket, the mutation G236D showed the best specificity for PAP. After optimization of the reaction conditions, the mutant YND displayed a 4.8-fold increase in the catalytic ratio PAP/PAPS compared to the wild-type. We subsequently applied YND to the assay of human SULT1A1 and SULT1A3 with their known substrate 1-naphthol, indicating that the mutant could be used to evaluate sulfotransferase activity by colorimetry. Analysis of the MD simulation results revealed that the improved substrate specificity of the mutant towards PAP may stem from a more stable protein conformation and the changed flexibility of key residues in the entrance of the substrate tunnel. This research will provide a valuable reference for the development of efficient sulfotransferase activity assays. - Source: PubMed
Publication date: 2024/06/18
Jiang JipengSun YanqingSun YananLu FupingLiu FufengZhang Huitu