Kurokawa Suguru, Berry Marla J
Department of Cell & Molecular Biology, John A. Burns School of Medicine, University of Hawaii at Manoa, Honolulu, HI, 96813, USA,
Met Ions Life Sci. 2013;13:499-534. doi: 10.1007/978-94-007-7500-8_16.
Selenium is an essential micronutrient in mammals, but is also recognized as toxic in excess. It is a non-metal with properties that are intermediate between the chalcogen elements sulfur and tellurium. Selenium exerts its biological functions through selenoproteins. Selenoproteins contain selenium in the form of the 21st amino acid, selenocysteine (Sec), which is an analog of cysteine with the sulfur-containing side chain replaced by a Se-containing side chain. Sec is encoded by the codon UGA, which is one of three termination codons for mRNA translation in non-selenoprotein genes. Recognition of the UGA codon as a Sec insertion site instead of stop requires a Sec insertion sequence (SECIS) element in selenoprotein mRNAs and a unique selenocysteyl-tRNA, both of which are recognized by specialized protein factors. Unlike the 20 standard amino acids, Sec is biosynthesized from serine on its tRNA. Twenty-five selenoproteins are encoded in the human genome. Most of the selenoprotein genes were discovered by bioinformatics approaches, searching for SECIS elements downstream of in-frame UGA codons. Sec has been described as having stronger nucleophilic and electrophilic properties than cysteine, and Sec is present in the catalytic site of all selenoenzymes. Most selenoproteins, whose functions are known, are involved in redox systems and signaling pathways. However, several selenoproteins are not well characterized in terms of their function. The selenium field has grown dramatically in the last few decades, and research on selenium biology is providing extensive new information regarding its importance for human health.
硒是哺乳动物必需的微量营养素,但过量时也被认为具有毒性。它是一种非金属元素,其性质介于硫族元素硫和碲之间。硒通过硒蛋白发挥其生物学功能。硒蛋白含有第21种氨基酸硒代半胱氨酸(Sec)形式的硒,它是半胱氨酸的类似物,含硫侧链被含硒侧链取代。Sec由密码子UGA编码,而UGA在非硒蛋白基因中是mRNA翻译的三个终止密码子之一。要将UGA密码子识别为Sec插入位点而非终止密码子,需要硒蛋白mRNA中的Sec插入序列(SECIS)元件和独特的硒代半胱氨酰 - tRNA,这两者都由特殊的蛋白质因子识别。与20种标准氨基酸不同,Sec是在其tRNA上由丝氨酸生物合成的。人类基因组中编码了25种硒蛋白。大多数硒蛋白基因是通过生物信息学方法发现的,即在符合读框的UGA密码子下游搜索SECIS元件。Sec被描述为比半胱氨酸具有更强的亲核和亲电性质,并且Sec存在于所有硒酶的催化位点。大多数已知功能的硒蛋白都参与氧化还原系统和信号通路。然而,有几种硒蛋白的功能尚未得到很好的表征。在过去几十年中,硒领域发展迅速,关于硒生物学的研究正在提供大量有关其对人类健康重要性的新信息。