磺化,主要由磺基转移酶促进,在内源性物质和外源性物质的解毒途径中起着至关重要的作用,促进新陈代谢和消除。传统上,这种生物转化归因于一个人胞质磺基转移酶(hSULTs)家族,以其高度的序列相似性和对3'-磷酸腺苷5'-磷酸硫酸(PAPS)作为磺基供体的依赖性而闻名。然而,最近的研究表明,肠道共生中存在PAPS依赖性磺基转移酶,这表明肠道微生物组可能含有多种磺基转移酶,并通过硫酸化作用促进解毒过程。在这项研究中,我们调查了人体肠道微生物组成员中磺基转移酶的患病率.有趣的是,我们偶然发现了不依赖PAPS的磺基转移酶,称为芳基硫酸盐磺基转移酶(ASSTs)。我们的生物信息学分析显示,肠道微生物属Sutterilla的成员拥有多个asst基因,可能在其成员内编码多种ASST酶。Sutterilla属微生物的波动与各种健康状况有关。出于这个原因,我们从Sutterellawadsworthensis3_1_45B中鉴定了17种不同的ASST。我们的发现表明,SwASST与大肠杆菌ASST具有相似性,但也表现出明显的结构变异和序列多样性。这些差异可能会推动潜在的功能多样化,并可能反映出与PAPS相关的进化差异。
Sulfonation, primarily facilitated by
sulfotransferases, plays a crucial role in the detoxification pathways of endogenous substances and xenobiotics, promoting metabolism and elimination. Traditionally, this bioconversion has been attributed to a family of human cytosolic
sulfotransferases (hSULTs) known for their high sequence similarity and dependence on 3\'-phosphoadenosine 5\'-phosphosulfate (PAPS) as a sulfo donor. However, recent studies have revealed the presence of PAPS-dependent
sulfotransferases within gut commensals, indicating that the gut microbiome may harbor a diverse array of sulfotransferase enzymes and contribute to detoxification processes via sulfation. In this study, we investigated the prevalence of
sulfotransferases in members of the human gut microbiome. Interestingly, we stumbled upon PAPS-independent
sulfotransferases, known as aryl-sulfate
sulfotransferases (ASSTs). Our bioinformatics analyses revealed that members of the gut microbial genus Sutterella harbor multiple asst genes, possibly encoding multiple ASST enzymes within its members. Fluctuations in the microbes of the genus Sutterella have been associated with various health conditions. For this reason, we characterized 17 different ASSTs from Sutterella wadsworthensis 3_1_45B. Our findings reveal that SwASSTs share similarities with E. coli ASST but also exhibit significant structural variations and sequence diversity. These differences might drive potential functional diversification and likely reflect an evolutionary divergence from their PAPS-dependent counterparts.