STRUCTURAL STUDIES OF ENZYMES INVOLVED IN COFACTOR BIOSYNTHESIS AND NUCLEOSIDE

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 我们对辅因子的生物合成也很感兴趣。我们目前正致力于硫胺素和吡哆醛5‘-磷酸(PLP)的生物合成。在硫胺素生物合成中，酶催化的许多反应涉及到前所未有的化学，阐明催化机理是一个主要目标。通过研究这些酶，我们还发现了与其他途径的有趣的进化联系。PLP是维生素B6的生物活性形式，是氨基酸和氨基糖等含胺天然产物代谢所涉及的几种酶的重要辅因子。特别令人感兴趣的是，发现有两条不同的PLP生物合成途径尚未被发现在同一生物体中共存

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. We are also interested in cofactor biosynthesis. We are currently focusing our efforts in this area on thiamin and pyridoxal 5'-phosphate (PLP) biosynthesis. Many of the reactions catalyzed by the enzymes in thiamin biosynthesis involve unprecedented chemistry and elucidation of catalytic mechanism is a major goal. By studying these enzymes, we have also discovered interesting evolutionary links to other pathways. PLP is the biologically active form of vitamin B6 and is an important cofactor for several of the enzymes involved in the metabolism of amine-containing natural products such as amino acids and amino-sugars. Of particular evolutionary interest is the finding that there are two distinct PLP biosynthetic pathways that have not yet been found to coexist in the same organism