Origin of ATP phosphate esters and sulfur thio-esters in early Life

生命早期ATP磷酸酯和硫硫酯的起源

• 批准号: 22H01343
• 负责人: McGlynn Shawn・E.
• 金额: $ 11.07万
• 依托单位: Tokyo Institute of Technology
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for Scientific Research (B)
• 财政年份: 2022
• 资助国家: 日本
• 起止时间: 2022-04-01 至 2025-03-31
• 项目状态: 未结题
• 来源: https://kaken.nii.ac.jp/en/grant/KAKENHI-PROJECT-22H01343/
• 关键词: Enzyme; Isotope; Origin of life; Energy conservation; Evolution; enzyme; thioester; anaerobe; origin of life; sulfur isotope

All life requires energy. One major pathway of energy harvesting in biology is substrate level phosphorylation, which is carried out by the enzyme glyceraldehyde 3-phosphate dehydrogenase. How this enzyme evolved, and what its original chemical reactivity was remains unknown.In this year we successfully surveyed the chemical reactivity of the enzyme glyceraldehyde 3-phosphate dehydrogenase from a thermophilic bacterium. To our surprise, we have identified a new enzymatic reaction which to our knowledge has not been reported before. In addition we find that the conditions of the assay which are being uniquely manipulated within our laboratory can change the reaction kinetics of the enzyme activity in surprising and still not completely understood ways. We are proceeding to draft these results into a manuscript to share with the scientific community.Our results are far reaching. First, they give new insights into the central energy harvesting enzyme of glycolysis which is widely distributed across the tree of life. Second, our results provide new insights which can be used to discuss the possible ancestral activity of this fascinating enzyme which accomplishes substrate phosphorylation.

所有生命都需要精力。生物学中能量收集的一种主要途径是底物水平磷酸化，这是由3-磷酸甘油醛脱氢酶进行的。这种酶如何发展，其原始化学反应性是未知的。今年，我们成功地调查了3-磷酸酶从嗜热细菌中的3-磷酸脱氢酶的化学反应性。令我们惊讶的是，我们已经确定了一种新的酶促反应，据我们所知，以前没有报道过。此外，我们发现在我们实验室内被独特操纵的测定条件可以以令人惊讶的方式改变酶活性的反应动力学，但仍未完全理解。我们正在将这些结果选为手稿以与科学界分享。首先，他们对糖酵解的中央能收集酶有了新的见解，该酶在整个生命之树中广泛分布。其次，我们的结果提供了新的见解，可用于讨论这种引人入胜的酶的祖先活性，从而实现底物磷酸化。